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Enzyme

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1985: 2323: 3277: 2709: 1459: 3597: 3635: 1765: 2297: 1350: 29: 9178: 4409: 1247: 2698: 785: 613: 4258: 1677: 9299: 4272: 3304:. In a metabolic pathway, one enzyme takes the product of another enzyme as a substrate. After the catalytic reaction, the product is then passed on to another enzyme. Sometimes more than one enzyme can catalyze the same reaction in parallel; this can allow more complex regulation: with, for example, a low constant activity provided by one enzyme but an inducible high activity from a second enzyme. 3782:). In addition, MAP is metal-ion dependent while creatinase is not, hence this property was also lost over time. Small changes of enzymatic activity are extremely common among enzymes. In particular, substrate binding specificity (see above) can easily and quickly change with single amino acid changes in their substrate binding pockets. This is frequently seen in the main enzyme classes such as 86: 2360:. The major contribution of Michaelis and Menten was to think of enzyme reactions in two stages. In the first, the substrate binds reversibly to the enzyme, forming the enzyme-substrate complex. This is sometimes called the Michaelis–Menten complex in their honor. The enzyme then catalyzes the chemical step in the reaction and releases the product. This work was further developed by 2379:. To find the maximum speed of an enzymatic reaction, the substrate concentration is increased until a constant rate of product formation is seen. This is shown in the saturation curve on the right. Saturation happens because, as substrate concentration increases, more and more of the free enzyme is converted into the substrate-bound ES complex. At the maximum reaction rate ( 3341:, because the amount of the end product produced is regulated by its own concentration. Negative feedback mechanism can effectively adjust the rate of synthesis of intermediate metabolites according to the demands of the cells. This helps with effective allocations of materials and energy economy, and it prevents the excess manufacture of end products. Like other 864: 3660:, any malfunction (mutation, overproduction, underproduction or deletion) of a single critical enzyme can lead to a genetic disease. The malfunction of just one type of enzyme out of the thousands of types present in the human body can be fatal. An example of a fatal genetic disease due to enzyme insufficiency is 2446:
specificity constant is called the diffusion limit and is about 10 to 10 (M s). At this point every collision of the enzyme with its substrate will result in catalysis, and the rate of product formation is not limited by the reaction rate but by the diffusion rate. Enzymes with this property are called
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to tetrahydrofolate. The similarity between the structures of dihydrofolate and this drug are shown in the accompanying figure. This type of inhibition can be overcome with high substrate concentration. In some cases, the inhibitor can bind to a site other than the binding-site of the usual substrate
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which then decays into products. Enzymes increase reaction rates by lowering the energy of the transition state. First, binding forms a low energy enzyme-substrate complex (ES). Second, the enzyme stabilises the transition state such that it requires less energy to achieve compared to the uncatalyzed
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also changes shape slightly as it enters the active site. The active site continues to change until the substrate is completely bound, at which point the final shape and charge distribution is determined. Induced fit may enhance the fidelity of molecular recognition in the presence of competition and
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for all steps in the reaction up to and including the first irreversible step. Because the specificity constant reflects both affinity and catalytic ability, it is useful for comparing different enzymes against each other, or the same enzyme with different substrates. The theoretical maximum for the
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Allosteric sites are pockets on the enzyme, distinct from the active site, that bind to molecules in the cellular environment. These molecules then cause a change in the conformation or dynamics of the enzyme that is transduced to the active site and thus affects the reaction rate of the enzyme. In
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suggested a modification to the lock and key model: since enzymes are rather flexible structures, the active site is continuously reshaped by interactions with the substrate as the substrate interacts with the enzyme. As a result, the substrate does not simply bind to a rigid active site; the amino
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proposed that both the enzyme and the substrate possess specific complementary geometric shapes that fit exactly into one another. This is often referred to as "the lock and key" model. This early model explains enzyme specificity, but fails to explain the stabilization of the transition state that
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is a process where the enzyme is sequestered away from its substrate. Enzymes can be sequestered to the plasma membrane away from a substrate in the nucleus or cytosol. Or within the membrane, an enzyme can be sequestered into lipid rafts away from its substrate in the disordered region. When the
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by other molecules. For example, the end product(s) of a metabolic pathway are often inhibitors for one of the first enzymes of the pathway (usually the first irreversible step, called committed step), thus regulating the amount of end product made by the pathways. Such a regulatory mechanism is
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reflect sequence similarity. For instance, two ligases of the same EC number that catalyze exactly the same reaction can have completely different sequences. Independent of their function, enzymes, like any other proteins, have been classified by their sequence similarity into numerous families.
1120:. Each enzyme is described by "EC" followed by a sequence of four numbers which represent the hierarchy of enzymatic activity (from very general to very specific). That is, the first number broadly classifies the enzyme based on its mechanism while the other digits add more and more specificity. 3683:, result in build-up of phenylalanine and related products. Some mutations are in the active site, directly disrupting binding and catalysis, but many are far from the active site and reduce activity by destabilising the protein structure, or affecting correct oligomerisation. This can lead to 3307:
Enzymes determine what steps occur in these pathways. Without enzymes, metabolism would neither progress through the same steps and could not be regulated to serve the needs of the cell. Most central metabolic pathways are regulated at a few key steps, typically through enzymes whose activity
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mechanism. If an enzyme produces too much of one substance in the organism, that substance may act as an inhibitor for the enzyme at the beginning of the pathway that produces it, causing production of the substance to slow down or stop when there is sufficient amount. This is a form of
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catalyzes a reaction in a first step and then checks that the product is correct in a second step. This two-step process results in average error rates of less than 1 error in 100 million reactions in high-fidelity mammalian polymerases. Similar proofreading mechanisms are also found in
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enzyme is released it mixes with its substrate. Alternatively, the enzyme can be sequestered near its substrate to activate the enzyme. For example, the enzyme can be soluble and upon activation bind to a lipid in the plasma membrane and then act upon molecules in the plasma membrane.
1284:) when heated or exposed to chemical denaturants and this disruption to the structure typically causes a loss of activity. Enzyme denaturation is normally linked to temperatures above a species' normal level; as a result, enzymes from bacteria living in volcanic environments such as 1960:
Since coenzymes are chemically changed as a consequence of enzyme action, it is useful to consider coenzymes to be a special class of substrates, or second substrates, which are common to many different enzymes. For example, about 1000 enzymes are known to use the coenzyme NADH.
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contained within the yeast cells called "ferments", which were thought to function only within living organisms. He wrote that "alcoholic fermentation is an act correlated with the life and organization of the yeast cells, not with the death or putrefaction of the cells."
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cannot bind to the free enzyme, only to the enzyme-substrate complex; hence, these types of inhibitors are most effective at high substrate concentration. In the presence of the inhibitor, the enzyme-substrate complex is inactive. This type of inhibition is rare.
1280:. The sequence of the amino acids specifies the structure which in turn determines the catalytic activity of the enzyme. Although structure determines function, a novel enzymatic activity cannot yet be predicted from structure alone. Enzyme structures unfold ( 2000:, which then decays into lower-energy products. When enzyme catalysed (solid line), the enzyme binds the substrates (ES), then stabilizes the transition state (ES) to reduce the activation energy required to produce products (EP) which are finally released. 2278:
Enzymes can couple two or more reactions, so that a thermodynamically favorable reaction can be used to "drive" a thermodynamically unfavourable one so that the combined energy of the products is lower than the substrates. For example, the hydrolysis of
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binds to an allosteric site and the binding of the substrate and the inhibitor affect each other. The enzyme's function is reduced but not eliminated when bound to the inhibitor. This type of inhibitor does not follow the Michaelis–Menten equation.
4765:(Translation: In order to obviate misunderstandings and avoid cumbersome periphrases, suggests designating as "enzymes" the unformed or not organized ferments, whose action can occur without the presence of organisms and outside of the same.) 4759:"Um Missverständnissen vorzubeugen und lästige Umschreibungen zu vermeiden schlägt Vortragender vor, die ungeformten oder nicht organisirten Fermente, deren Wirkung ohne Anwesenheit von Organismen und ausserhalb derselben erfolgen kann, als 2018:
As with all catalysts, enzymes do not alter the position of the chemical equilibrium of the reaction. In the presence of an enzyme, the reaction runs in the same direction as it would without the enzyme, just more quickly. For example,
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Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, et al. (February 2005). "Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II".
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Enzymes are not rigid, static structures; instead they have complex internal dynamic motions – that is, movements of parts of the enzyme's structure such as individual amino acid residues, groups of residues forming a
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and other industrial applications when extremely specific catalysts are required. Enzymes in general are limited in the number of reactions they have evolved to catalyze and also by their lack of stability in
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Since inhibitors modulate the function of enzymes they are often used as drugs. Many such drugs are reversible competitive inhibitors that resemble the enzyme's native substrate, similar to
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Bar-Even A, Noor E, Savir Y, Liebermeister W, Davidi D, Tawfik DS, Milo R (May 2011). "The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters".
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The biochemical identity of enzymes was still unknown in the early 1900s. Many scientists observed that enzymatic activity was associated with proteins, but others (such as Nobel laureate
2239: 2119: 2534: 3754:. A key question is therefore whether and how enzymes can change their enzymatic activities alongside. It is generally accepted that many new enzyme activities have evolved through 971:, he found that sugar was fermented by yeast extracts even when there were no living yeast cells in the mixture. He named the enzyme that brought about the fermentation of sucrose " 5781:"Um ein Bild zu gebrauchen, will ich sagen, dass Enzym und Glucosid wie Schloss und Schlüssel zu einander passen müssen, um eine chemische Wirkung auf einander ausüben zu können." 4969:
Blake CC, Koenig DF, Mair GA, North AC, Phillips DC, Sarma VR (May 1965). "Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution".
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this way, allosteric interactions can either inhibit or activate enzymes. Allosteric interactions with metabolites upstream or downstream in an enzyme's metabolic pathway cause
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where it is activated. This stops the enzyme from digesting the pancreas or other tissues before it enters the gut. This type of inactive precursor to an enzyme is known as a
2667: 3691:, in which the body's ability to break down choline ester drugs is impaired. Oral administration of enzymes can be used to treat some functional enzyme deficiencies, such as 1800:
Some enzymes do not need additional components to show full activity. Others require non-protein molecules called cofactors to be bound for activity. Cofactors can be either
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Renugopalakrishnan V, Garduño-Juárez R, Narasimhan G, Verma CS, Wei X, Li P (November 2005). "Rational design of thermally stable proteins: relevance to bionanotechnology".
1451:, having broad specificity and acting on a range of different physiologically relevant substrates. Many enzymes possess small side activities which arose fortuitously (i.e. 1303:. Only a small portion of their structure (around 2–4 amino acids) is directly involved in catalysis: the catalytic site. This catalytic site is located next to one or more 2569: 1238:
may spread these genes to unrelated species, especially bacteria where they can replace endogenous genes of the same function, leading to hon-homologous gene displacement.
1976:. This continuous regeneration means that small amounts of coenzymes can be used very intensively. For example, the human body turns over its own weight in ATP each day. 1882:
Coenzymes are small organic molecules that can be loosely or tightly bound to an enzyme. Coenzymes transport chemical groups from one enzyme to another. Examples include
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and mutation of the duplicate copies although evolution can also happen without duplication. One example of an enzyme that has changed its activity is the ancestor of
1824:). These cofactors serve many purposes; for instance, metal ions can help in stabilizing nucleophilic species within the active site. Organic cofactors can be either 1109: 1964:
Coenzymes are usually continuously regenerated and their concentrations maintained at a steady level inside the cell. For example, NADPH is regenerated through the
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Enzyme kinetics is the investigation of how enzymes bind substrates and turn them into products. The rate data used in kinetic analyses are commonly obtained from
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evolution. These efforts have begun to be successful, and a few enzymes have now been designed "from scratch" to catalyze reactions that do not occur in nature.
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As enzymes are made up of proteins, their actions are sensitive to change in many physio chemical factors such as pH, temperature, substrate concentration, etc.
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and substrate cannot bind to the enzyme at the same time. Often competitive inhibitors strongly resemble the real substrate of the enzyme. For example, the drug
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is only one of several important kinetic parameters. The amount of substrate needed to achieve a given rate of reaction is also important. This is given by the
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are prized by industrial users for their ability to function at high temperatures, allowing enzyme-catalysed reactions to be operated at a very high rate.
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for "his discovery of cell-free fermentation". Following Buchner's example, enzymes are usually named according to the reaction they carry out: the suffix
5783:(To use an image, I will say that an enzyme and a glucoside must fit like a lock and key, in order to be able to exert a chemical effect on each other.) 2722:(right) are very similar in structure (differences show in green). As a result, methotrexate is a competitive inhibitor of many enzymes that use folates. 2406:), which is the substrate concentration required for an enzyme to reach one-half its maximum reaction rate; generally, each enzyme has a characteristic 7219:
Fisher JF, Meroueh SO, Mobashery S (February 2005). "Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity".
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Ramanathan A, Savol A, Burger V, Chennubhotla CS, Agarwal PK (January 2014). "Protein conformational populations and functionally relevant substates".
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Chapman-Smith A, Cronan JE (September 1999). "The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity".
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that make up the active site are molded into the precise positions that enable the enzyme to perform its catalytic function. In some cases, such as
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and thermodynamically driven random collision. Many biochemical or cellular processes deviate significantly from these conditions, because of
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Flatmark T, Stevens RC (August 1999). "Structural Insight into the Aromatic Amino Acid Hydroxylases and Their Disease-Related Mutant Forms".
7392:"Infrared evidence of cyanide binding to iron and copper sites in bovine heart cytochrome c oxidase. Implications regarding oxygen reduction" 2386:) of the enzyme, all the enzyme active sites are bound to substrate, and the amount of ES complex is the same as the total amount of enzyme. 2484:. The turnover of such enzymes can reach several million reactions per second. But most enzymes are far from perfect: the average values of 7135:(July 1986). "Why is uncompetitive inhibition so rare? A possible explanation, with implications for the design of drugs and pesticides". 1659:
are associated with the substrate binding, catalysis, cofactor release, and product release steps of the catalytic cycle, consistent with
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recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their
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of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules:
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Artificial (in vitro) evolution is now commonly used to modify enzyme activity or specificity for industrial applications (see below).
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is reduced. In contrast to competitive inhibition, non-competitive inhibition cannot be overcome with high substrate concentration.
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In some enzymes, no amino acids are directly involved in catalysis; instead, the enzyme contains sites to bind and orient catalytic
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is an active area of research and involves attempts to create new enzymes with novel properties, either through rational design or
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The naming of enzymes by adding the suffix "-ase" to the substrate on which the enzyme acts, has been traced to French scientist
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Enzymes must bind their substrates before they can catalyse any chemical reaction. Enzymes are usually very specific as to what
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Rodnina MV, Wintermeyer W (2001). "Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanisms".
5437: 5129: 1311:. The remaining majority of the enzyme structure serves to maintain the precise orientation and dynamics of the active site. 800:. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is 5924:(2nd ed.). New York, Chichester, Weinheim, Brisbane, Singapore, Toronto.: John Wiley & Sons, Inc. pp. 137–8. 416: 8143:
Okada S, O'Brien JS (August 1969). "Tay-Sachs disease: generalized absence of a beta-D-N-acetylhexosaminidase component".
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Distorting bound substrate(s) into their transition state form to reduce the energy required to reach the transition state
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of enzyme genes) can be enhanced or diminished by a cell in response to changes in the cell's environment. This form of
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Guzmán-Maldonado H, Paredes-López O (September 1995). "Amylolytic enzymes and products derived from starch: a review".
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and constrained molecular movement. More recent, complex extensions of the model attempt to correct for these effects.
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Farris PL (2009). "Economic Growth and Organization of the U.S. Starch Industry". In BeMiller JN, Whistler RL (eds.).
4688:[Memoir on diastase, the principal products of its reactions, and their applications to the industrial arts]. 1085:. An enzyme's name is often derived from its substrate or the chemical reaction it catalyzes, with the word ending in 9441: 9203: 9167: 9124: 6998: 6727: 6702: 6567: 5929: 5810: 5466: 4788: 4399: 1929: 1883: 1716: 49: 1571:
Creating an environment with a charge distribution complementary to that of the transition state to lower its energy
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characteristics to the substrates. Enzymes can therefore distinguish between very similar substrate molecules to be
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Wlodawer A, Vondrasek J (1998). "Inhibitors of HIV-1 protease: a major success of structure-assisted drug design".
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Warshel A, Sharma PK, Kato M, Xiang Y, Liu H, Olsson MH (August 2006). "Electrostatic basis for enzyme catalysis".
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binds to a site other than where the substrate binds. The substrate still binds with its usual affinity and hence K
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Temporarily reacting with the substrate, forming a covalent intermediate to provide a lower energy transition state
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via a series of intermediate metabolites. Each chemical modification (red box) is performed by a different enzyme.
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Alkorta I, Garbisu C, Llama MJ, Serra JL (January 1998). "Industrial applications of pectic enzymes: a review".
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fashion because the enzymes from the unaffected genes are generally sufficient to prevent symptoms in carriers.
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and closely related compounds (vitamins) must be acquired from the diet. The chemical groups carried include:
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Ochoa D, Bradley D, Beltrao P (February 2018). "Evolution, dynamics and dysregulation of kinase signalling".
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Enzymes are usually much larger than their substrates. Sizes range from just 62 amino acid residues, for the
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Michaelis L, Menten M (1913). "Die Kinetik der Invertinwirkung" [The Kinetics of Invertase Action].
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is an irreversible enzyme inhibitor that combines with the copper and iron in the active site of the enzyme
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enzymes. Defects in these enzymes cause cancer because cells are less able to repair mutations in their
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involves the hydrolysis of ATP. Because this reaction releases so much energy, other reactions that are
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where residues orient the substrates. The catalytic site and binding site together compose the enzyme's
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These families have been documented in dozens of different protein and protein family databases such as
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Sun Y, Cheng J (May 2002). "Hydrolysis of lignocellulosic materials for ethanol production: a review".
6334:"Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms" 3972: 3345:, the control of enzymatic action helps to maintain a stable internal environment in living organisms. 2778: 1660: 1063:
and published in 1965. This high-resolution structure of lysozyme marked the beginning of the field of
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Jiang L, Althoff EA, Clemente FR, Doyle L, Röthlisberger D, Zanghellini A, et al. (March 2008).
4153: 3766:) which are clearly homologous but catalyze very different reactions (MAP removes the amino-terminal 3676: 3601: 2009: 1965: 1652: 1437: 1076: 1047:
The discovery that enzymes could be crystallized eventually allowed their structures to be solved by
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Zenkin N, Yuzenkova Y, Severinov K (July 2006). "Transcript-assisted transcriptional proofreading".
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Jaeger KE, Eggert T (August 2004). "Enantioselective biocatalysis optimized by directed evolution".
4408: 1197:: catalyze the movement of ions or molecules across membranes, or their separation within membranes. 967:
submitted his first paper on the study of yeast extracts in 1897. In a series of experiments at the
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Suzuki H (2015). "Chapter 4: Effect of pH, Temperature, and High Pressure on Enzymatic Activity".
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Khersonsky O, Tawfik DS (2010). "Enzyme promiscuity: a mechanistic and evolutionary perspective".
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for an enzyme reaction showing the relation between the substrate concentration and reaction rate.
9494: 9319: 8063:"Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase" 7895:"Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling" 3684: 3581: 3454: 2798: 2757: 2681: 1832:, which are tightly bound to an enzyme. Organic prosthetic groups can be covalently bound (e.g., 1809: 1795: 1694: 1687: 1656: 1648: 1551: 1517: 1415:
Some of the enzymes showing the highest specificity and accuracy are involved in the copying and
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Chen LH, Kenyon GL, Curtin F, Harayama S, Bembenek ME, Hajipour G, Whitman CP (September 1992).
4459:"A robust methodology to subclassify pseudokinases based on their nucleotide-binding properties" 4422:
Murphy JM, Farhan H, Eyers PA (April 2017). "Bio-Zombie: the rise of pseudoenzymes in biology".
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remains the same. However the inhibitor reduces the catalytic efficiency of the enzyme so that V
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for glucose yet is more sensitive to glucose concentration. This enzyme is involved in sensing
3422: 3389:. Another example of post-translational modification is the cleavage of the polypeptide chain. 3174: 2824: 2280: 1935: 1903: 1891: 1874:; here the holoenzyme is the complete complex containing all the subunits needed for activity. 1769: 1729: 1467: 1424: 1060: 933: 547: 461: 411: 5089:. School of Biological and Chemical Sciences, Queen Mary, University of London. Archived from 4744: 1337:
exist, which again can act alone or in complex with proteins. The most common of these is the
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Murzin AG (November 1993). "Can homologous proteins evolve different enzymatic activities?".
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Johnson LN, Petsko GA (July 1999). "David Phillips and the origin of structural enzymology".
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Enzyme changes shape by induced fit upon substrate binding to form enzyme-substrate complex.
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Begley CG, Paragina S, Sporn A (March 1990). "An analysis of contact lens enzyme cleaners".
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can be coupled to ATP hydrolysis, driving the overall series of linked metabolic reactions.
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reaction (ES). Finally the enzyme-product complex (EP) dissociates to release the products.
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catalyzes its reaction in either direction depending on the concentration of its reactants:
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Enzymes can be compartmentalized, with different metabolic pathways occurring in different
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in 1937. The conclusion that pure proteins can be enzymes was definitively demonstrated by
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Manchester KL (December 1995). "Louis Pasteur (1822–1895)--chance and the prepared mind".
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Schomburg I, Chang A, Placzek S, Söhngen C, Rother M, Lang M, et al. (January 2013).
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Murphy JM, Zhang Q, Young SN, Reese ML, Bailey FP, Eyers PA, et al. (January 2014).
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Froguel P, Zouali H, Vionnet N, Velho G, Vaxillaire M, Sun F, et al. (March 1993).
6944: 6672:(3rd ed.). Baltimore, Maryland: Lippincott Williams & Wilkins. pp. 312–3. 6622: 6394: 6258: 6233: 6190: 6110: 5970: 5843: 5573: 5311:"4-Oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues per monomer" 5209: 5121: 4982: 4568: 9730: 9484: 9393: 9383: 9070: 8844: 8676: 8643: 8607:
Hult K, Berglund P (August 2003). "Engineered enzymes for improved organic synthesis".
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Cleaver JE (May 1968). "Defective repair replication of DNA in xeroderma pigmentosum".
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Changeux JP, Edelstein SJ (June 2005). "Allosteric mechanisms of signal transduction".
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that digests the coating of some bacteria; the structure was solved by a group led by
9269: 9243: 9199: 9163: 9156: 9120: 9097: 9062: 8967: 8867: 8836: 8793: 8765: 8727: 8681: 8624: 8589: 8554: 8519: 8515: 8482: 8451: 8408: 8359: 8268: 8233: 8168: 8125: 8084: 8043: 7994: 7943: 7920: 7873: 7868:
Skett P, Gibson GG (2001). "Chapter 3: Induction and Inhibition of Drug Metabolism".
7850: 7801: 7750: 7720: 7669: 7628: 7593: 7544: 7539: 7514: 7487: 7482: 7465: 7446: 7436: 7413: 7364: 7360: 7329: 7288: 7236: 7201: 7152: 7148: 7106: 7102: 7064: 7027: 6994: 6956: 6913: 6878: 6843: 6794: 6733: 6723: 6698: 6673: 6646: 6563: 6537: 6501: 6464: 6406: 6363: 6314: 6306: 6263: 6214: 6209: 6174: 6153: 6122: 6077: 6054: 6017: 5994: 5935: 5925: 5902: 5867: 5806: 5739: 5698: 5663: 5659: 5628: 5624: 5585: 5534: 5499: 5462: 5433: 5373: 5332: 5289: 5262: 5221: 5178: 5125: 5037: 4994: 4926: 4784: 4724: 4623: 4580: 4537: 4488: 4439: 4395: 4295: 4180: 4129: 3804: 3731: 3703: 3622: 3510: 3470: 3378: 3338: 3301: 3281: 3256:, which can then be absorbed. Different enzymes digest different food substances. In 3229: 2857: 2853: 2267: 2005: 1993: 1989: 1916: 1829: 1782: 1753: 1561: 1557: 1480: 1455:), which may be the starting point for the evolutionary selection of a new function. 1452: 1409: 1367: 1354: 1267: 1201:
These sections are subdivided by other features such as the substrate, products, and
844: 797: 766:
an enzyme, but even in the decades since ribozymes' discovery in 1980-1982, the word
729: 493: 436: 431: 426: 361: 57: 9074: 8848: 7499: 7376: 7164: 6968: 6418: 5597: 5546: 5385: 2424:, which is the number of substrate molecules handled by one active site per second. 9720: 9530: 9525: 9499: 9427: 9054: 9027: 8959: 8930: 8826: 8757: 8719: 8671: 8663: 8616: 8581: 8546: 8511: 8463: 8443: 8398: 8390: 8349: 8339: 8260: 8225: 8216:
Erlandsen H, Stevens RC (October 1999). "The structural basis of phenylketonuria".
8180: 8160: 8115: 8074: 8033: 8025: 7984: 7976: 7910: 7902: 7840: 7832: 7791: 7783: 7710: 7700: 7659: 7620: 7611:
De Clercq E (April 2002). "Highlights in the development of new antiviral agents".
7583: 7579: 7575: 7534: 7526: 7477: 7403: 7356: 7319: 7278: 7270: 7259:"Strategies for discovering and derisking covalent, irreversible enzyme inhibitors" 7228: 7191: 7144: 7118: 7098: 7054: 7023: 6948: 6905: 6870: 6833: 6825: 6784: 6776: 6636: 6626: 6529: 6493: 6398: 6353: 6345: 6298: 6275: 6253: 6245: 6204: 6194: 6134: 6114: 6097:
Benkovic SJ, Hammes-Schiffer S (August 2003). "A perspective on enzyme catalysis".
6046: 5984: 5974: 5894: 5857: 5847: 5770: 5729: 5690: 5655: 5620: 5577: 5526: 5491: 5403: 5363: 5322: 5252: 5213: 5168: 5158: 5117: 5029: 5006: 4986: 4916: 4892: 4716: 4615: 4592: 4572: 4527: 4519: 4478: 4470: 4431: 4037: 3954: 3755: 3651: 3553: 3462: 3430: 3394: 3333: 3329: 3194: 2811: 2730: 2365: 2349: 2303: 2271: 2122: 1997: 1984: 1907: 1870:
can also be applied to enzymes that contain multiple protein subunits, such as the
1813: 1629: 1547: 1405: 1401: 1330: 1273: 1259: 1143: 1008:) argued that proteins were merely carriers for the true enzymes and that proteins 824:
are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal
813: 809: 725: 663: 503: 421: 396: 8748:
Kirk O, Borchert TV, Fuglsang CC (August 2002). "Industrial enzyme applications".
8029: 7059: 7042: 6952: 6896:
Ellis RJ (October 2001). "Macromolecular crowding: obvious but underappreciated".
4887:
Willstätter R (1927). "Faraday lecture. Problems and methods in enzyme research".
4856: 923: 9577: 9561: 9474: 9195:
New Beer in an Old Bottle: Eduard Buchner and the Growth of Biochemical Knowledge
8164: 6765:"The original Michaelis constant: translation of the 1913 Michaelis-Menten paper" 5979: 5495: 5217: 5196:
Anfinsen CB (July 1973). "Principles that govern the folding of protein chains".
4866: 4619: 4606:
Callahan BP, Miller BG (December 2007). "OMP decarboxylase--An enigma persists".
4290: 4157: 4054: 3809: 3719: 3672: 3605: 3557: 3549: 3498: 3458: 3374: 3358: 2339: 1609: 1590:
By orienting the substrates into a productive arrangement to reduce the reaction
1416: 1319: 1277: 1013: 843:. Some household products use enzymes to speed up chemical reactions: enzymes in 836:
when exposed to excessive heat, losing their structure and catalytic properties.
732:
depend upon enzymes to catalyze individual steps. The study of enzymes is called
466: 138: 9045:
Bajpai P (March 1999). "Application of enzymes in the pulp and paper industry".
8120: 8103: 5368: 5351: 4747:[On the behavior of various organized and so-called unformed ferments]. 9615: 9556: 9342: 8571: 8293:. Bethesda (MD): National Center for Biotechnology Information (US). 1998–2015. 8286: 7705: 6611:
Proceedings of the National Academy of Sciences of the United States of America
6179:
Proceedings of the National Academy of Sciences of the United States of America
5832:
Proceedings of the National Academy of Sciences of the United States of America
4389: 4263: 4102: 3715: 3665: 3442: 3362: 3276: 2896: 2892: 1871: 1644: 1433: 1428: 1128: 1098: 998: 964: 887:
were known but the mechanisms by which these occurred had not been identified.
721: 532: 441: 386: 8963: 8550: 8379:"Lactose malabsorption and intolerance: pathogenesis, diagnosis and treatment" 8079: 8062: 6249: 5794: 5257: 5240: 3506: 2735:
Enzyme reaction rates can be decreased by various types of enzyme inhibitors.
2697: 2477: 928: 770:
alone often means the protein type specifically (as is used in this article).
9714: 9520: 9479: 9363: 9353: 8394: 8328:"Enzyme replacement therapy for pancreatic insufficiency: present and future" 7624: 7450: 7196: 7179: 6737: 6199: 5920:
Boyer R (2002). "Chapter 6: Enzymes I, Reactions, Kinetics, and Inhibition".
5774: 4863:– the first enzyme to be isolated – by introducing this practice in his book 4745:"Über das Verhalten verschiedener organisirter und sog. ungeformter Fermente" 4199: 4176: 3940: 3680: 3609: 3542: 3502: 3366: 3222: 3210: 2904: 2828: 2442: 2376: 1773: 1613: 1362: 1187: 911: 891: 793: 451: 324: 265: 248: 243: 201: 188: 8667: 6631: 6402: 6118: 5939: 5581: 5056: 4576: 1862:. An enzyme together with the cofactor(s) required for activity is called a 1594:
change (the contribution of this mechanism to catalysis is relatively small)
1205:. An enzyme is fully specified by four numerical designations. For example, 1067:
and the effort to understand how enzymes work at an atomic level of detail.
855:
break down proteins into smaller molecules, making the meat easier to chew.
9469: 9358: 9209: 9066: 8840: 8769: 8731: 8685: 8628: 8593: 8558: 8412: 8363: 8272: 8237: 8229: 8088: 8047: 7998: 7805: 7724: 7632: 7548: 7292: 7240: 7205: 7110: 7068: 6960: 6917: 6882: 6847: 6798: 6650: 6541: 6505: 6410: 6367: 6318: 6267: 6218: 6173:
Villa J, Strajbl M, Glennon TM, Sham YY, Chu ZT, Warshel A (October 2000).
6126: 6058: 5998: 5906: 5871: 5743: 5702: 5667: 5632: 5589: 5538: 5503: 5266: 5182: 5163: 5041: 4930: 4627: 4541: 4492: 4443: 4211: 3642:
fashion because there are more non-X chromosomes than X-chromosomes, and a
3390: 3182: 2900: 2864: 2753: 2719: 2708: 2356:
proposed a quantitative theory of enzyme kinetics, which is referred to as
2345: 2322: 1828:, which are released from the enzyme's active site during the reaction, or 1817: 1526: 1304: 1230:. Unrelated enzymes that have the same enzymatic activity have been called 1113: 1041: 747:
Enzymes are known to catalyze more than 5,000 biochemical reaction types.
737: 712:, and the enzyme converts the substrates into different molecules known as 562: 557: 520: 498: 366: 77: 20: 9101: 8971: 8523: 8455: 8377:
Misselwitz B, Pohl D, Frühauf H, Fried M, Vavricka SR, Fox M (June 2013).
8172: 8129: 7980: 7924: 7872:(3 ed.). Cheltenham, UK: Nelson Thornes Publishers. pp. 87–118. 7854: 7673: 7597: 7491: 7417: 7368: 7333: 7156: 5377: 5352:"The animal fatty acid synthase: one gene, one polypeptide, seven enzymes" 5336: 5225: 4998: 4728: 4584: 4523: 3449:
within the penicillin molecule. Another example comes from enzymes in the
2887:. A common example of an irreversible inhibitor that is used as a drug is 784: 9693: 9628: 9464: 8585: 7836: 7530: 5852: 5799: 4896: 4277: 4120: 4041: 3958: 3892:
Remove protein, starch, and fat or oil stains from laundry and dishware.
3727: 3657: 3585: 3573: 3514: 3446: 3386: 3342: 3320:
There are five main ways that enzyme activity is controlled in the cell.
3309: 3261: 3166: 2872: 1600:
Enzymes may use several of these mechanisms simultaneously. For example,
1556:
Enzymes can accelerate reactions in several ways, all of which lower the
1458: 1397: 1393: 1308: 1194: 1139: 1044:. These three scientists were awarded the 1946 Nobel Prize in Chemistry. 915: 825: 305: 283: 278: 273: 253: 226: 221: 128: 45: 33: 4435: 1764: 1101:. Different enzymes that catalyze the same chemical reaction are called 9174:, A biochemistry textbook available free online through NCBI Bookshelf. 8864:
Ingredients in Meat Products Properties, Functionality and Applications
8344: 7180:"A Perspective on the Kinetics of Covalent and Irreversible Inhibition" 6722:(Third, enlarged and improved ed.). Weinheim, Germany: Wiley-VCH. 5885:
Vasella A, Davies GJ, Böhm M (October 2002). "Glycosidase mechanisms".
4474: 4190: 4143: 4139: 3999: 3767: 3763: 3751: 3747: 3707: 3569: 3565: 3486: 3466: 3438: 3285: 3198: 2880: 2832: 2761: 2715: 1947: 1941: 1701: in this section. Unsourced material may be challenged and removed. 1651:
of slightly different structures that interconvert with one another at
1617: 1522: 1463: 1285: 1206: 1158: 1079:
similarity (and thus evolutionary relationship) or enzymatic activity.
1020:
was a pure protein and crystallized it; he did likewise for the enzyme
946: 840: 741: 717: 572: 238: 206: 161: 143: 9058: 8831: 8814: 8264: 7906: 7787: 7274: 7232: 6874: 6829: 6780: 6533: 6310: 6302: 6050: 5116:. Chichester, UK: John Wiley & Sons, Ltd. pp. a0003058.pub2. 3626: 1786: 1490: 1484: 1371: 61: 9667: 9641: 9378: 8447: 6349: 5718:"Catalytic promiscuity and the evolution of new enzymatic activities" 4990: 4749:
Verhandlungen des Naturhistorisch-medicinischen Vereins zu Heidelberg
4670:
Volume IV: Modern Development of the Chemical and Biological Sciences
4114: 4110: 4045: 4019: 3922: 3897: 3858: 3844: 3775: 3545: 3530: 3526: 3518: 3465:. Enzyme levels can also be regulated by changing the rate of enzyme 3265: 3218: 3202: 2677: 2296: 1854:
Enzymes that require a cofactor but do not have one bound are called
1801: 1475: 1172: 1154: 1132: 1056: 961:
was used to refer to chemical activity produced by living organisms.
839:
Some enzymes are used commercially, for example, in the synthesis of
705: 28: 5828:"Application of a Theory of Enzyme Specificity to Protein Synthesis" 5087:
International Union of Biochemistry and Molecular Biology (NC-IUBMB)
4937: 3501:
and used by a different set of enzymes as a source of energy in the
2441:. This is also called the specificity constant and incorporates the 2195: 2075: 1676: 1392:
is achieved by binding pockets with complementary shape, charge and
6436:. International Union of Pure and Applied Chemistry. Archived from 5530: 4860: 4257: 4205: 4172: 4135: 4078: 4014: 3979: 3926: 3903: 3879: 3771: 3743: 3577: 3522: 3398: 3382: 3293: 3257: 3237: 2848: 2473: 2469: 1825: 1749: 1601: 1530: 1441: 1358: 1349: 1338: 1334: 1168:: cleave various bonds by means other than hydrolysis and oxidation 1052: 1021: 895: 755: 751: 697: 567: 297: 258: 196: 5795:"Chapter 2.2: The Central Role of Enzymes as Biological Catalysts" 3849:
Break down cellulose into sugars that can be fermented to produce
3714:. This causes a slow accumulation of mutations and results in the 2368:, who derived kinetic equations that are still widely used today. 9403: 9398: 9311: 8194: 8061:
Kamata K, Mitsuya M, Nishimura T, Eiki J, Nagata Y (March 2004).
6288: 4327: 4236: 4226: 4096: 4088: 4060: 3988: 3918: 3912: 3883: 3864: 3838: 3561: 3513:
of the enzyme to different compartments may change the degree of
3490: 3406: 3402: 3370: 3289: 3253: 3249: 3245: 3233: 2908: 2888: 2836: 1925: 1911: 1752:
regulation, altering the activity of the enzyme according to the
1605: 1591: 1292: 1102: 1090: 1037: 994: 990: 903: 693: 41: 37: 6583: 6463:. Hoboken, New Jersey: John Wiley & Sons, Inc. p. 336. 4797: 3300:
Several enzymes can work together in a specific order, creating
863: 9680: 9298: 7308:"The discovery and development of HMG-CoA reductase inhibitors" 7014:
Price NC (1979). "What is meant by 'competitive inhibition'?".
6175:"How important are entropic contributions to enzyme catalysis?" 5761:[Influence of configuration on the action of enzymes]. 4945:"Nobel Prizes and Laureates: The Nobel Prize in Chemistry 1946" 4555:
Radzicka A, Wolfenden R (January 1995). "A proficient enzyme".
4317: 4312: 4307: 4232: 4220: 4186: 4066: 4031: 4023: 3994: 3887: 3783: 3742:
Similar to any other protein, enzymes change over time through
3711: 3241: 3186: 3170: 3162: 2907:. Other enzyme inhibitors are poisons. For example, the poison 2868: 1833: 1471: 1466:
has a large induced fit motion that closes over the substrates
1420: 1183: 1176: 1033: 1017: 972: 954: 884: 876: 852: 821: 213: 6860: 5517:
Shevelev IV, Hübscher U (May 2002). "The 3' 5' exonucleases".
3197:. Enzymes are also involved in more exotic functions, such as 1612:, stabilize charge build-up on the transition states using an 1246: 9654: 9408: 9388: 8949: 6763:
Michaelis L, Menten ML, Johnson KA, Goody RS (October 2011).
5145:
Omelchenko MV, Galperin MY, Wolf YI, Koonin EV (April 2010).
4166: 4084: 4008: 3702:
Another way enzyme malfunctions can cause disease comes from
3450: 3206: 1848: 1165: 907: 880: 6434:"Glossary of Terms Used in Bioinorganic Chemistry: Cofactor" 5144: 4505: 4271: 3671:
One example of enzyme deficiency is the most common type of
3656:
Since the tight control of enzyme activity is essential for
3638:
Hereditary defects in enzymes are generally inherited in an
3604:
over 300 different mutations throughout the structure cause
1341:
which is a complex of protein and catalytic RNA components.
871:
By the late 17th and early 18th centuries, the digestion of
85: 6762: 6518: 6076:(6th ed.). New York, N.Y.: W.H. Freeman. p. 195. 6072:
Cox MM, Nelson DL (2013). "Chapter 6.2: How enzymes work".
5112:
Mulder NJ (28 September 2007). "Protein Family Databases".
4322: 3964: 3946: 3932: 3779: 3675:. Many different single amino acid mutations in the enzyme 3617: 2242: 1821: 1221: 981: 872: 817: 678: 669: 329: 9419: 8812: 8481:(11th ed.). London: Saunders/ Elsevier. p. 567. 8376: 8060: 7745:
Suzuki H (2015). "Chapter 8: Control of Enzyme Activity".
6931:
Kopelman R (September 1988). "Fractal reaction kinetics".
3209:
can also contain enzymes for infecting cells, such as the
3181:, and also transport cargo around the cell as part of the 1361:
example. Binding sites in blue, catalytic site in red and
8641: 8101: 7821:"Molecular basis of beta-lactamase induction in bacteria" 6604: 5061:
International Union of Biochemistry and Molecular Biology
3268:, to break down the cellulose cell walls of plant fiber. 3264:
diets, microorganisms in the gut produce another enzyme,
2930:
The following table shows pH optima for various enzymes.
2884: 2827:
permanently inactivates the enzyme, usually by forming a
2427:
The efficiency of an enzyme can be expressed in terms of
2227: 2214: 2184: 2166: 2107: 2094: 2064: 2046: 1805: 1110:
International Union of Biochemistry and Molecular Biology
848: 9017: 6692: 5763:
Berichte der Deutschen Chemischen Gesellschaft zu Berlin
5559: 5308: 4831:"Eduard Buchner – Nobel Lecture: Cell-Free Fermentation" 3393:, a digestive protease, is produced in inactive form as 1503:
To explain the observed specificity of enzymes, in 1894
953:
was used later to refer to nonliving substances such as
728:
in order to occur at rates fast enough to sustain life.
7963:
Noree C, Sato BK, Broyer RM, Wilhelm JE (August 2010).
7772:"GSK-3: tricks of the trade for a multi-tasking kinase" 7256: 6172: 6096: 5759:"Einfluss der Configuration auf die Wirkung der Enzyme" 5402:. The European Bioinformatics Institute. Archived from 3679:, which catalyzes the first step in the degradation of 3560:
and therefore have different sets of enzymes (known as
1075:
Enzymes can be classified by two main criteria: either
829: 816:
are molecules that increase activity. Many therapeutic
8018:
Critical Reviews in Biochemistry and Molecular Biology
7962: 7349:
Annual Review of Biophysics and Biomolecular Structure
7218: 6984: 6982: 6980: 6978: 6036: 5461:(3rd ed.). Weinheim: Wiley-VCH. pp. 89–114. 4859:(1840–1904), who intended to honor the discoverers of 1992:. Uncatalysed (dashed line), substrates need a lot of 1250:
Enzyme activity initially increases with temperature (
8644:"De novo computational design of retro-aldol enzymes" 7689:"Cyclooxygenases: structural and functional insights" 5428:
Suzuki H (2015). "Chapter 7: Active Site Structure".
4868:
Traité de microbiologie: Diastases, toxines et venins
4781:
The Oxford Companion to the History of Modern Science
4644:(1752). "Observations sur la digestion des oiseaux". 4456: 3746:
and sequence divergence. Given their central role in
3461:. Induction or inhibition of these enzymes can cause 2638: 2577: 2542: 2490: 2154: 2034: 684: 675: 672: 8747: 8325: 6584:"BRENDA The Comprehensive Enzyme Information System" 5715: 4968: 4253: 3157:
inside living organisms. They are indispensable for
2922: 1914:. These coenzymes cannot be synthesized by the body 1843:
An example of an enzyme that contains a cofactor is
1388:
they bind and then the chemical reaction catalysed.
744:
sequences and unusual 'pseudocatalytic' properties.
9087: 8536: 8479:
Andrews' Diseases of the Skin: Clinical Dermatology
6975: 6483: 6331: 5611:Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis". 4873:
Microbiology Treatise: diastases, toxins and venoms
2847:In many organisms, inhibitors may act as part of a 681: 666: 9155: 9153: 5798: 5645: 5459:Biochemistry of Signal Transduction and Regulation 5080: 4387: 3348: 2661: 2625:{\displaystyle 10^{5}{\rm {s}}^{-1}{\rm {M}}^{-1}} 2624: 2563: 2528: 2413:for a given substrate. Another useful constant is 2233: 2113: 1070: 898:, in 1833. A few decades later, when studying the 8813:Dulieu C, Moll M, Boudrant J, Poncelet D (2000). 8476: 7861: 7346: 7257:Johnson DS, Weerapana E, Cravatt BF (June 2010). 6663: 6605:Törnroth-Horsefield S, Neutze R (December 2008). 6380: 5884: 4554: 4421: 3902:Remove food stains from the common food additive 2283:is often used to drive other chemical reactions. 1498: 1474:. Binding sites in blue, substrates in black and 914:concluded that this fermentation was caused by a 812:are molecules that decrease enzyme activity, and 48:residues in red, maltose substrate in black, and 16:Large biological molecule that acts as a catalyst 9712: 8916: 8215: 8142: 7892: 7740: 7738: 7736: 7734: 7564:"Molecular biology of bacterial bioluminescence" 7512: 7389: 7081: 7034: 6988: 6090: 5680: 5516: 5423: 5421: 4880: 4875:] (in French). Paris, France: Masson and Co. 4783:. Oxford: Oxford University Press. p. 270. 3687:if the disease is untreated. Another example is 3381:, helps control the synthesis or degradation of 2676:, which is derived from the assumptions of free 1776:. Thiamine pyrophosphate cofactor in yellow and 949:, in yeast', to describe this process. The word 8983: 8981: 8250: 8197:. U.S. National Human Genome Research Institute 8014:"Metabolic regulation via enzyme filamentation" 6750: 5432:. Boca Raton, FL: CRC Press. pp. 117–140. 5238: 2769:to change the shape of the usual binding-site. 1322:where the binding of a small molecule causes a 9263: 9191: 9090:Journal of the American Optometric Association 8995:. European Union. 10 July 2010. Archived from 8952:Critical Reviews in Food Science and Nutrition 8894:. European Union. 10 July 2010. Archived from 7749:. Boca Raton, FL: CRC Press. pp. 141–69. 7131: 7082:Wu P, Clausen MH, Nielsen TE (December 2015). 6666:"Chapter 9: The Pulmonary System and Exercise" 6553: 6551: 6016:. San Francisco: W.H. Freeman. pp. 50–2. 5953:Savir Y, Tlusty T (May 2007). Scalas E (ed.). 4605: 4383: 4381: 4379: 4377: 4375: 4373: 4371: 4369: 4367: 4365: 4363: 2302:A chemical reaction mechanism with or without 1946:formyl, methenyl or methyl groups, carried by 1576:By providing an alternative reaction pathway: 9435: 9327: 9162:(5th ed.). New York, NY: W. H. Freeman. 8209: 7942:. Boca Raton, FL: CRC Press. pp. 53–74. 7931: 7818: 7769: 7731: 7686: 7084:"Allosteric small-molecule kinase inhibitors" 6854: 6811: 6720:Enzyme kinetics : principles and methods 6458: 6332:Tsai CJ, Del Sol A, Nussinov R (March 2009). 5805:(2nd ed.). Washington (DC ): ASM Press. 5418: 5019: 4394:(5th ed.). San Francisco: W.H. Freeman. 4361: 4359: 4357: 4355: 4353: 4351: 4349: 4347: 4345: 4343: 3978:Increase fermentation efficiency by reducing 3489:are synthesized by one set of enzymes in the 3385:and allows the cell to respond to changes in 1584:By destabilizing the substrate ground state: 638: 9240:How Enzymes Work: From Structure to Function 8978: 8606: 7940:How Enzymes Work: From Structure to Function 7747:How Enzymes Work: From Structure to Function 7604: 7513:Berg JS, Powell BC, Cheney RE (April 2001). 6693:Ferguson SJ, Nicholls D, Ferguson S (2002). 6477: 5481: 5430:How Enzymes Work: From Structure to Function 5013: 3812:and at high temperatures. As a consequence, 3770:in new proteins while creatinase hydrolyses 3750:, enzyme evolution plays a critical role in 3217:, or for viral release from cells, like the 875:by stomach secretions and the conversion of 7867: 7812: 7680: 7645: 6548: 6005: 5952: 5786: 5279: 4886: 4683: 4599: 4450: 3476: 3228:An important function of enzymes is in the 2266:The rate of a reaction is dependent on the 2234:{\displaystyle {\ce {CO2{}+H2O<-H2CO3}}} 2114:{\displaystyle {\ce {CO2{}+H2O->H2CO3}}} 9442: 9428: 9334: 9320: 8792:(1st ed.). London: Blackie Academic. 8783: 8781: 8779: 8332:Clinical and Experimental Gastroenterology 7763: 7252: 7250: 7007: 6717: 6431: 6234:"The catalytic triad of serine peptidases" 4706: 4646:Histoire de l'Académie Royale des Sciences 4640: 4634: 4340: 3931:Split polysaccharides and proteins in the 3792: 2842: 2839:are common drugs that act in this manner. 2766: 645: 631: 8934: 8917:Molimard P, Spinnler HE (February 1996). 8830: 8697: 8695: 8675: 8574:Journal of Nanoscience and Nanotechnology 8402: 8353: 8343: 8119: 8078: 8037: 8011: 7988: 7914: 7844: 7795: 7714: 7704: 7663: 7610: 7587: 7538: 7481: 7407: 7323: 7282: 7195: 7058: 7043:"The molecular perspective: methotrexate" 6837: 6814:"A Note on the Kinetics of Enzyme Action" 6788: 6640: 6630: 6607:"Opening and closing the metabolite gate" 6557: 6357: 6257: 6208: 6198: 6147: 6071: 5988: 5978: 5861: 5851: 5792: 5733: 5367: 5326: 5256: 5172: 5162: 4920: 4889:Journal of the Chemical Society (Resumed) 4864: 4531: 4482: 3591: 2867:above; other well-known examples include 2756:is a competitive inhibitor of the enzyme 2529:{\displaystyle k_{\rm {cat}}/K_{\rm {m}}} 1717:Learn how and when to remove this message 1666: 792:Like all catalysts, enzymes increase the 9237: 8743: 8741: 8701: 8470: 8383:United European Gastroenterology Journal 7937: 7744: 7299: 7040: 6930: 6686: 6011: 5825: 5674: 5610: 5452: 5427: 5195: 4662: 3730:in response to even minimal exposure to 3633: 3595: 3275: 2672:Michaelis–Menten kinetics relies on the 1983: 1763: 1736: 1457: 1348: 1254:) until the enzyme's structure unfolds ( 1245: 862: 858: 783: 27: 9154:Berg JM, Tymoczko JL, Stryer L (2002). 8776: 8425: 8326:Fieker A, Philpott J, Armand M (2011). 7561: 7247: 7177: 5756: 5282:"Chapter 1: From sequence to structure" 4905:"So do we understand how enzymes work?" 4548: 4388:Stryer L, Berg JM, Tymoczko JL (2002). 3572:pathway, has a specialized form called 3536: 3445:are induced that hydrolyse the crucial 2856:. Major metabolic pathways such as the 1299:, to over 2,500 residues in the animal 1055:, an enzyme found in tears, saliva and 9713: 9114: 9044: 8787: 8692: 8501: 8477:James WD, Elston D, Berger TG (2011). 7893:Faergeman NJ, Knudsen J (April 1997). 7819:Bennett PM, Chopra I (February 1993). 7463: 6993:(3 ed.). London: Portland Press. 6664:McArdle WD, Katch F, Katch VL (2006). 6231: 5716:O'Brien PJ, Herschlag D (April 1999). 5519:Nature Reviews. Molecular Cell Biology 5111: 4774: 3525:) or oxidative state (e.g., oxidizing 3469:. The opposite of enzyme induction is 3315: 3148: 2738: 1427:" mechanisms. Here, an enzyme such as 1326:that increases or decreases activity. 1032:, who worked on the digestive enzymes 1012:were incapable of catalysis. In 1926, 708:upon which enzymes may act are called 9423: 9315: 9268:(4th ed.). Weinheim: Wiley-VCH. 8861: 8738: 8539:Current Opinion in Structural Biology 7825:Antimicrobial Agents and Chemotherapy 7013: 6895: 6697:(3rd ed.). San Diego: Academic. 6586:. Technische Universität Braunschweig 6150:Catalysis in Chemistry and Enzymology 5919: 5695:10.1146/annurev-biochem-030409-143718 5349: 4742: 4666:A History of Science: in Five Volumes 3949:and beer filtration characteristics. 3762:(MAP) and creatine amidinohydrolase ( 1568:By stabilizing the transition state: 1318:. Enzyme structures may also contain 894:was the first to discover an enzyme, 832:, and many enzymes are (permanently) 9142: 7770:Doble BW, Woodgett JR (April 2003). 7687:Rouzer CA, Marnett LJ (April 2009). 7646:Mackie RI, White BA (October 1990). 7430: 7390:Yoshikawa S, Caughey WS (May 1990). 7305: 6238:Cellular and Molecular Life Sciences 6074:Lehninger Principles of Biochemistry 5455:"The Regulations of Enzyme Activity" 5048: 4902: 3664:, in which patients lack the enzyme 3401:and transported in this form to the 3169:. They also generate movement, with 2145: 2025: 1699:adding citations to reliable sources 1670: 1511: 1379: 1232:non-homologous isofunctional enzymes 1228:Non-homologous isofunctional enzymes 1118:EC numbers (for "Enzyme Commission") 997:) or to the type of reaction (e.g., 802:orotidine 5'-phosphate decarboxylase 758:. They are sometimes described as a 8866:. New York: Springer. p. 177. 8307:. U.S. National Library of Medicine 8108:The New England Journal of Medicine 7613:Mini Reviews in Medicinal Chemistry 7396:The Journal of Biological Chemistry 5887:Current Opinion in Chemical Biology 5315:The Journal of Biological Chemistry 5288:. London: New Science. p. 27. 5239:Dunaway-Mariano D (November 2008). 5122:10.1002/9780470015902.a0003058.pub2 4741:Kühne coined the word "enzyme" in: 4301: 3588:and regulating insulin production. 3433:. For example, bacteria may become 2760:, which catalyzes the reduction of 1620:using an oriented water substrate. 1608:perform covalent catalysis using a 1333:-based biological catalysts called 13: 9341: 9137: 9119:(3rd ed.). London: Academic. 8195:"Learning About Tay–Sachs Disease" 3726:, which causes the development of 3718:. An example of such a hereditary 3369:. For example, in the response to 2772: 2645: 2608: 2591: 2555: 2552: 2549: 2520: 2503: 2500: 2497: 851:stains on clothes, and enzymes in 14: 9752: 9291: 8936:10.3168/jds.S0022-0302(96)76348-8 8305:"Pseudocholinesterase deficiency" 8218:Molecular Genetics and Metabolism 7665:10.3168/jds.S0022-0302(90)78986-2 6670:Essentials of Exercise Physiology 4877:See Chapter 1, especially page 9. 2923:Factors affecting enzyme activity 1979: 1756:through the rest of the pathway. 1447:Conversely, some enzymes display 1123:The top-level classification is: 985:is combined with the name of the 9297: 9222:, A history of early enzymology. 9176: 9108: 9081: 9038: 9011: 8943: 8910: 8880: 8855: 8806: 8750:Current Opinion in Biotechnology 8635: 8609:Current Opinion in Biotechnology 8600: 8565: 8530: 8495: 8419: 8370: 8319: 8297: 8279: 8244: 7361:10.1146/annurev.biophys.27.1.249 7103:10.1016/j.pharmthera.2015.10.002 6459:Voet D, Voet J, Pratt C (2016). 5660:10.1146/annurev.biochem.70.1.415 5625:10.1146/annurev.biochem.69.1.617 5484:Current Opinion in Biotechnology 5054: 4690:Annales de chimie et de physique 4424:Biochemical Society Transactions 4407: 4270: 4256: 3153:Enzymes serve a wide variety of 2792: 2718:(left) and the anti-cancer drug 2707: 2696: 2662:{\displaystyle 10{\rm {s}}^{-1}} 2321: 2295: 1988:The energies of the stages of a 1934:the phosphate group, carried by 1675: 1179:changes within a single molecule 926:(1837–1900) first used the term 662: 612: 611: 84: 9266:Fundamentals of Enzyme Kinetics 9117:Starch Chemistry and Technology 8187: 8136: 8095: 8054: 8005: 7956: 7886: 7870:Introduction to Drug Metabolism 7639: 7555: 7506: 7457: 7424: 7383: 7340: 7212: 7171: 7125: 7091:Pharmacology & Therapeutics 7075: 6991:Fundamentals of Enzyme Kinetics 6924: 6889: 6805: 6744: 6711: 6657: 6598: 6576: 6512: 6452: 6425: 6374: 6325: 6282: 6225: 6166: 6141: 6065: 6030: 5946: 5913: 5878: 5819: 5750: 5709: 5639: 5604: 5553: 5510: 5475: 5446: 5392: 5343: 5302: 5273: 5232: 5189: 5138: 5105: 5074: 4962: 4849: 4768: 4735: 4700: 3689:pseudocholinesterase deficiency 3377:of multiple enzymes, including 3355:post-translational modification 3349:Post-translational modification 3161:and cell regulation, often via 2818: 1894:(ATP). Some coenzymes, such as 1686:needs additional citations for 1647:. These motions give rise to a 1262:at an intermediate temperature. 1071:Classification and nomenclature 9394:"Minerals" (Chemical elements) 9232:Enzyme structure and mechanism 9192:Cornish-Bowden A, ed. (1997). 8504:Trends in Biochemical Sciences 7580:10.1128/MMBR.55.1.123-142.1991 7435:. New Delhi: S. Chand and Co. 7016:Trends in Biochemical Sciences 6898:Trends in Biochemical Sciences 6812:Briggs GE, Haldane JB (1925). 6486:Trends in Biochemical Sciences 6014:Enzyme Structure and Mechanism 5801:The Cell: a Molecular Approach 5286:Protein structure and function 5022:Trends in Biochemical Sciences 4757:Relevant passage on page 190: 4677: 4656: 4499: 4415: 4022:protein in the manufacture of 3288:releases energy by converting 2743: 2456:. Example of such enzymes are 1974:methionine adenosyltransferase 1423:. Some of these enzymes have " 847:break down protein, starch or 1: 9242:. Boca Raton, FL: CRC Press. 9032:10.1016/S0032-9592(97)00046-0 8762:10.1016/S0958-1669(02)00328-2 8724:10.1016/S0960-8524(01)00212-7 8621:10.1016/S0958-1669(03)00095-8 8030:10.3109/10409238.2016.1172555 7519:Molecular Biology of the Cell 7409:10.1016/S0021-9258(19)39023-4 7325:10.1016/S0022-2275(20)41379-3 7060:10.1634/theoncologist.4-4-340 7041:Goodsell DS (1 August 1999). 6953:10.1126/science.241.4873.1620 6910:10.1016/S0968-0004(01)01938-7 6498:10.1016/s0968-0004(99)01438-3 6291:Accounts of Chemical Research 5899:10.1016/S1367-5931(02)00380-0 5826:Koshland DE (February 1958). 5735:10.1016/S1074-5521(99)80033-7 5683:Annual Review of Biochemistry 5648:Annual Review of Biochemistry 5613:Annual Review of Biochemistry 5328:10.1016/S0021-9258(19)37101-7 5034:10.1016/S0968-0004(99)01423-1 4922:10.1016/S0969-2126(00)00125-8 4721:10.1016/S0167-7799(00)89014-9 4518:(Database issue): D764–D772. 4333: 3323: 3310:thermodynamically unfavorable 3271: 2687: 2564:{\displaystyle k_{\rm {cat}}} 1953:the methyl group, carried by 1940:the acetyl group, carried by 922:In 1877, German physiologist 8516:10.1016/0968-0004(93)90132-7 8165:10.1126/science.165.3894.698 7901:. 323 ( Pt 1) (Pt 1): 1–12. 7515:"A millennial myosin census" 7483:10.1016/0092-8674(95)90405-0 7433:Fundamentals of biochemistry 7149:10.1016/0014-5793(86)81424-7 7028:10.1016/0968-0004(79)90205-6 6461:Fundamentals of Biochemistry 5980:10.1371/journal.pone.0000468 5496:10.1016/j.copbio.2004.06.007 5218:10.1126/science.181.4096.223 4620:10.1016/j.bioorg.2007.07.004 3737: 3240:break down large molecules ( 3232:of animals. Enzymes such as 2860:make use of this mechanism. 1877: 1759: 1541: 1344: 1297:4-oxalocrotonate tautomerase 1276:, acting alone or in larger 1241: 1150:a methyl or phosphate group) 975:". In 1907, he received the 788:IUPAC definition for enzymes 762:of enzyme rather than being 7: 9449: 9198:. Universitat de València. 8121:10.1056/NEJM199303113281005 7969:The Journal of Cell Biology 7178:Strelow JM (January 2017). 5369:10.1096/fasebj.8.15.8001737 5280:Petsko GA, Ringe D (2003). 5241:"Enzyme function discovery" 4684:Payen A, Persoz JF (1833). 4249: 4083:Lower the protein level of 3967:and adjust fermentability. 3576:expressed in the liver and 3556:have different patterns of 3412: 3339:negative feedback mechanism 2286: 2256: 2136: 1900:flavin adenine dinucleotide 1623: 1536:conformational proofreading 993:is the enzyme that cleaves 779:three-dimensional structure 543:Bioorganometallic chemistry 472:Volume combustion synthesis 10: 9757: 8012:Aughey GN, Liu JL (2015). 7706:10.1194/jlr.R800042-JLR200 7263:Future Medicinal Chemistry 5400:"The Catalytic Site Atlas" 4751:. new series (in German). 4217: 4196: 4163: 4126: 4108: 4094: 4076: 4051: 4029: 4005: 3985: 3973:Acetolactate decarboxylase 3970: 3952: 3938: 3909: 3895: 3870: 3856: 3835: 3796: 3649: 3568:, the first enzyme in the 2728: 2458:triose-phosphate isomerase 2366:J. B. S. Haldane 2337: 2003: 1866:(or haloenzyme). The term 1793: 1740: 1661:catalytic resonance theory 1627: 1545: 1438:aminoacyl tRNA synthetases 1265: 1186:: join two molecules with 1051:. This was first done for 845:biological washing powders 402:Enantioselective synthesis 18: 9606: 9598:Michaelis–Menten kinetics 9570: 9539: 9508: 9457: 9349: 9264:Cornish-Bowden A (2012). 8989:"Protease – GMO Database" 8964:10.1080/10408399509527706 8888:"Chymosin – GMO Database" 8551:10.1016/j.sbi.2017.12.008 8080:10.1016/j.str.2004.02.005 7693:Journal of Lipid Research 7562:Meighen EA (March 1991). 7464:Hunter T (January 1995). 7312:Journal of Lipid Research 6989:Cornish-Bowden A (2004). 6250:10.1007/s00018-005-5160-x 6232:Polgár L (October 2005). 5350:Smith S (December 1994). 5258:10.1016/j.str.2008.10.001 4218: 4154:polymerase chain reaction 4052: 4006: 3910: 3871: 3836: 3677:phenylalanine hydroxylase 3602:phenylalanine hydroxylase 3457:, which are important in 3189:in the cell membrane are 2899:enzymes that produce the 2779:non-competitive inhibitor 2397:Michaelis–Menten constant 2375:conditions and substrate 2358:Michaelis–Menten kinetics 2010:Thermodynamic equilibrium 1966:pentose phosphate pathway 1772:and protein structure of 1258:), leading to an optimal 407:Fully automated synthesis 352:Artificial gene synthesis 9490:Diffusion-limited enzyme 8923:Journal of Dairy Science 8395:10.1177/2050640613484463 7652:Journal of Dairy Science 7625:10.2174/1389557024605474 7306:Endo A (November 1992). 7197:10.1177/1087057116671509 6200:10.1073/pnas.97.22.11899 5922:Concepts in Biochemistry 5775:10.1002/cber.18940270364 5081:Nomenclature Committee. 4809:Nobel Laureate Biography 4779:. In Heilbron JL (ed.). 4071:high-fructose corn syrup 3867:for biofuel production. 3803:Enzymes are used in the 3760:methionyl aminopeptidase 3693:pancreatic insufficiency 3477:Subcellular distribution 3455:cytochrome P450 oxidases 3435:resistant to antibiotics 2805: 1910:(THF), are derived from 1236:Horizontal gene transfer 1030:Wendell Meredith Stanley 977:Nobel Prize in Chemistry 382:Custom peptide synthesis 9258:Kinetics and inhibition 8668:10.1126/science.1152692 7899:The Biochemical Journal 7776:Journal of Cell Science 7568:Microbiological Reviews 6818:The Biochemical Journal 6632:10.1073/pnas.0810654106 6403:10.1126/science.1108595 6152:. Mineola, N.Y: Dover. 6119:10.1126/science.1085515 5722:Chemistry & Biology 5582:10.1126/science.1127422 4709:Trends in Biotechnology 4577:10.1126/science.7809611 4463:The Biochemical Journal 4214:to prevent infections. 3793:Industrial applications 3685:intellectual disability 3616:coenzyme in black, and 3441:because enzymes called 3125:Adenosine triphosphate 2843:Functions of inhibitors 2799:uncompetitive inhibitor 2758:dihydrofolate reductase 2682:macromolecular crowding 2371:Enzyme rates depend on 2306:. The enzyme (E) binds 1972:-adenosylmethionine by 1796:Cofactor (biochemistry) 1768:Chemical structure for 1657:dihydrofolate reductase 1649:conformational ensemble 1552:Transition state theory 1016:showed that the enzyme 932:, which comes from 752:catalytic RNA molecules 750:Other biocatalysts are 696:that act as biological 509:Bioorthogonal chemistry 9047:Biotechnology Progress 8819:Biotechnology Progress 8704:Bioresource Technology 8230:10.1006/mgme.1999.2922 6560:Vitamins and Coenzymes 6432:de Bolster MW (1997). 5164:10.1186/1745-6150-5-31 4673:. Harper and Brothers. 4512:Nucleic Acids Research 3716:development of cancers 3647: 3631: 3592:Involvement in disease 3328:Enzymes can be either 3297: 3175:adenosine triphosphate 2825:irreversible inhibitor 2663: 2626: 2565: 2530: 2235: 2115: 2001: 1936:adenosine triphosphate 1904:thiamine pyrophosphate 1892:adenosine triphosphate 1791: 1770:thiamine pyrophosphate 1730:Substrate presentation 1667:Substrate presentation 1495: 1468:adenosine triphosphate 1376: 1272:Enzymes are generally 1263: 1061:David Chilton Phillips 883:by plant extracts and 868: 789: 777:comes from its unique 548:Bioinorganic chemistry 462:Solvothermal synthesis 412:Hydrothermal synthesis 66: 9583:Eadie–Hofstee diagram 9516:Allosteric regulation 9374:Essential fatty acids 9186:Etymology and history 7981:10.1083/jcb.201003001 6718:Bisswanger H (2017). 4903:Blow D (April 2000). 4150:restriction digestion 3724:xeroderma pigmentosum 3637: 3620:cofactor in yellow. ( 3599: 3548:, cells in different 3495:endoplasmic reticulum 3483:cellular compartments 3279: 3215:reverse transcriptase 2891:, which inhibits the 2750:competitive inhibitor 2664: 2627: 2566: 2531: 2449:catalytically perfect 2236: 2116: 1987: 1896:flavin mononucleotide 1780:substrate in black. ( 1767: 1743:Allosteric regulation 1737:Allosteric modulation 1478:cofactor in yellow. ( 1461: 1365:substrate in black. ( 1352: 1324:conformational change 1249: 1095:alcohol dehydrogenase 1049:x-ray crystallography 1001:forms DNA polymers). 866: 859:Etymology and history 787: 738:pseudoenzyme analysis 598:Glossary of chemistry 553:Biophysical chemistry 457:Solid-phase synthesis 311:Amino acid metabolism 289:Nucleotide metabolism 232:Fatty-acid metabolism 31: 9593:Lineweaver–Burk plot 9306:at Wikimedia Commons 9020:Process Biochemistry 8586:10.1166/jnn.2005.441 7837:10.1128/aac.37.2.153 7531:10.1091/mbc.12.4.780 7431:Jain JL (May 1999). 6338:Molecular BioSystems 6244:(19–20): 2161–2172. 5853:10.1073/pnas.44.2.98 5406:on 27 September 2018 4897:10.1039/JR9270001359 4663:Williams HS (1904). 4608:Bioorganic Chemistry 4069:, such as in making 4065:Produce sugars from 3874:Biological detergent 3706:in genes coding for 3537:Organ specialization 3201:generating light in 2982:Lipase (castor oil) 2917:cellular respiration 2913:cytochrome c oxidase 2636: 2575: 2540: 2488: 2482:superoxide dismutase 2466:acetylcholinesterase 2152: 2032: 2014:Chemical equilibrium 1955:S-adenosylmethionine 1928:ion (H), carried by 1838:pyruvate carboxylase 1810:iron–sulfur clusters 1778:xylulose 5-phosphate 1695:improve this article 1643:, or even an entire 1499:"Lock and key" model 1135:/reduction reactions 1026:John Howard Northrop 969:University of Berlin 538:Bioorganic chemistry 377:Convergent synthesis 357:Biomimetic synthesis 179:Biomolecule families 9212:on 13 December 2010 8999:on 24 February 2015 8716:2002BiTec..83....1S 8660:2008Sci...319.1387J 8654:(5868): 1387–1391. 8440:1968Natur.218..652C 8157:1969Sci...165..698O 7782:(Pt 7): 1175–1186. 6945:1988Sci...241.1620K 6939:(4873): 1620–1626. 6623:2008PNAS..10519565T 6617:(50): 19565–19566. 6395:2005Sci...308.1424C 6389:(5727): 1424–1428. 6191:2000PNAS...9711899V 6185:(22): 11899–11904. 6111:2003Sci...301.1196B 6105:(5637): 1196–1202. 5971:2007PLoSO...2..468S 5844:1958PNAS...44...98K 5574:2006Sci...313..518Z 5321:(25): 17716–17721. 5210:1973Sci...181..223A 4983:1965Natur.206..757B 4692:. 2nd (in French). 4569:1995Sci...267...90R 4524:10.1093/nar/gks1049 4436:10.1042/bst20160400 4210:Remove proteins on 3814:protein engineering 3697:lactose intolerance 3614:tetrahydrobiopterin 3517:(e.g., the neutral 3417:Enzyme production ( 3343:homeostatic devices 3316:Control of activity 3159:signal transduction 3149:Biological function 3015:Amylase (pancreas) 2934: 2883:infections such as 2877:protease inhibitors 2871:used to treat high 2739:Types of inhibition 2454:kinetically perfect 2354:Maud Leonora Menten 2270:needed to form the 2229: 2216: 2201: 2186: 2168: 2109: 2096: 2081: 2066: 2048: 1836:in enzymes such as 1641:secondary structure 1301:fatty acid synthase 1215:. EC categories do 1213:Sequence similarity 1077:amino acid sequence 1006:Richard Willstätter 718:metabolic processes 593:Glossary of biology 516:Medicinal chemistry 486:Biochemistry fields 392:Divergent synthesis 167:List of biochemists 156:List of biochemists 72:Part of a series on 36:converts the sugar 9552:Enzyme superfamily 9485:Enzyme promiscuity 8788:Briggs DE (1998). 8345:10.2147/CEG.S17634 8291:Genes and Disease 7699:(Suppl): S29–S34. 6562:. Krieger Pub Co. 6558:Wagner AL (1975). 6440:on 21 January 2017 6148:Jencks WP (1987). 5793:Cooper GM (2000). 5757:Fischer E (1894). 5093:on 1 December 2014 4865:Duclaux E (1899). 4775:Holmes FL (2003). 4475:10.1042/BJ20131174 4286:Industrial enzymes 4181:lignin peroxidases 4002:meat for cooking. 3851:cellulosic ethanol 3799:Industrial enzymes 3704:germline mutations 3648: 3632: 3302:metabolic pathways 3298: 3179:muscle contraction 3177:(ATP) to generate 2993:Lipase (pancreas) 2933: 2674:law of mass action 2659: 2622: 2561: 2526: 2462:carbonic anhydrase 2420:, also called the 2231: 2217: 2204: 2198:Carbonic anhydrase 2174: 2156: 2111: 2097: 2084: 2078:Carbonic anhydrase 2054: 2036: 2021:carbonic anhydrase 2002: 1845:carbonic anhydrase 1792: 1496: 1449:enzyme promiscuity 1377: 1329:A small number of 1264: 1203:chemical mechanism 1065:structural biology 869: 790: 730:Metabolic pathways 702:chemical reactions 528:Clinical chemistry 344:Chemical synthesis 67: 9741:Process chemicals 9708: 9707: 9417: 9416: 9302:Media related to 9288: 9287: 9249:978-981-4463-92-8 9238:Suzuki H (2015). 9059:10.1021/bp990013k 8873:978-0-387-71327-4 8832:10.1021/bp000128k 8790:Malts and Malting 8580:(11): 1759–1767. 8434:(5142): 652–656. 8287:"Phenylketonuria" 8265:10.1021/cr980450y 8151:(3894): 698–700. 7949:978-981-4463-92-8 7907:10.1042/bj3230001 7788:10.1242/jcs.00384 7756:978-981-4463-92-8 7658:(10): 2971–2995. 7402:(14): 7945–7958. 7318:(11): 1569–1582. 7275:10.4155/fmc.10.21 7233:10.1021/cr030102i 7022:(11): N272–N273. 6875:10.1021/bi2002289 6869:(21): 4402–4410. 6830:10.1042/bj0190338 6781:10.1021/bi201284u 6775:(39): 8264–8269. 6534:10.1021/bi0480279 6470:978-1-118-91840-1 6303:10.1021/ar400084s 6159:978-0-486-65460-7 6051:10.1021/cr0503106 6023:978-0-7167-1615-0 6012:Fersht A (1985). 5568:(5786): 518–520. 5453:Krauss G (2003). 5439:978-981-4463-92-8 5362:(15): 1248–1259. 5251:(11): 1599–1600. 5204:(4096): 223–230. 5131:978-0-470-01617-6 4977:(4986): 757–761. 4296:Molecular machine 4247: 4246: 4130:Molecular biology 3963:Make low-calorie 3805:chemical industry 3732:ultraviolet light 3662:Tay–Sachs disease 3580:that has a lower 3471:enzyme repression 3463:drug interactions 3379:glycogen synthase 3282:metabolic pathway 3230:digestive systems 3146: 3145: 2971:Lipase (stomach) 2858:citric acid cycle 2854:negative feedback 2767:allosteric effect 2362:G. E. Briggs 2268:activation energy 2264: 2263: 2220: 2207: 2202: 2199: 2189: 2177: 2159: 2144: 2143: 2100: 2087: 2082: 2079: 2069: 2057: 2039: 2006:Activation energy 1994:activation energy 1990:chemical reaction 1830:prosthetic groups 1814:organic compounds 1727: 1726: 1719: 1562:Gibbs free energy 1558:activation energy 1512:Induced fit model 1508:enzymes achieve. 1380:Substrate binding 1274:globular proteins 1268:Protein structure 1116:for enzymes, the 1112:have developed a 798:activation energy 736:and the field of 655: 654: 494:Molecular biology 437:Peptide synthesis 432:Organic synthesis 427:One-pot synthesis 362:Bioretrosynthesis 91:Chemistry of life 9748: 9588:Hanes–Woolf plot 9531:Enzyme activator 9526:Enzyme inhibitor 9500:Enzyme catalysis 9444: 9437: 9430: 9421: 9420: 9336: 9329: 9322: 9313: 9312: 9301: 9279: 9253: 9221: 9219: 9217: 9208:. Archived from 9181: 9180: 9173: 9161: 9143: 9131: 9130: 9112: 9106: 9105: 9085: 9079: 9078: 9042: 9036: 9035: 9015: 9009: 9008: 9006: 9004: 8985: 8976: 8975: 8947: 8941: 8940: 8938: 8914: 8908: 8907: 8905: 8903: 8898:on 26 March 2015 8884: 8878: 8877: 8862:Tarté R (2008). 8859: 8853: 8852: 8834: 8810: 8804: 8803: 8785: 8774: 8773: 8745: 8736: 8735: 8699: 8690: 8689: 8679: 8639: 8633: 8632: 8604: 8598: 8597: 8569: 8563: 8562: 8534: 8528: 8527: 8499: 8493: 8492: 8474: 8468: 8467: 8448:10.1038/218652a0 8423: 8417: 8416: 8406: 8374: 8368: 8367: 8357: 8347: 8323: 8317: 8316: 8314: 8312: 8301: 8295: 8294: 8283: 8277: 8276: 8259:(8): 2137–2160. 8253:Chemical Reviews 8248: 8242: 8241: 8213: 8207: 8206: 8204: 8202: 8191: 8185: 8184: 8140: 8134: 8133: 8123: 8099: 8093: 8092: 8082: 8058: 8052: 8051: 8041: 8009: 8003: 8002: 7992: 7960: 7954: 7953: 7935: 7929: 7928: 7918: 7890: 7884: 7883: 7865: 7859: 7858: 7848: 7816: 7810: 7809: 7799: 7767: 7761: 7760: 7742: 7729: 7728: 7718: 7708: 7684: 7678: 7677: 7667: 7643: 7637: 7636: 7608: 7602: 7601: 7591: 7559: 7553: 7552: 7542: 7510: 7504: 7503: 7485: 7461: 7455: 7454: 7428: 7422: 7421: 7411: 7387: 7381: 7380: 7344: 7338: 7337: 7327: 7303: 7297: 7296: 7286: 7254: 7245: 7244: 7221:Chemical Reviews 7216: 7210: 7209: 7199: 7175: 7169: 7168: 7133:Cornish-Bowden A 7129: 7123: 7122: 7088: 7079: 7073: 7072: 7062: 7038: 7032: 7031: 7011: 7005: 7004: 6986: 6973: 6972: 6928: 6922: 6921: 6893: 6887: 6886: 6858: 6852: 6851: 6841: 6809: 6803: 6802: 6792: 6760: 6748: 6742: 6741: 6715: 6709: 6708: 6690: 6684: 6683: 6661: 6655: 6654: 6644: 6634: 6602: 6596: 6595: 6593: 6591: 6580: 6574: 6573: 6555: 6546: 6545: 6528:(4): 1097–1105. 6516: 6510: 6509: 6481: 6475: 6474: 6456: 6450: 6449: 6447: 6445: 6429: 6423: 6422: 6378: 6372: 6371: 6361: 6350:10.1039/b819720b 6329: 6323: 6322: 6286: 6280: 6279: 6261: 6229: 6223: 6222: 6212: 6202: 6170: 6164: 6163: 6145: 6139: 6138: 6094: 6088: 6087: 6069: 6063: 6062: 6045:(8): 3210–3235. 6039:Chemical Reviews 6034: 6028: 6027: 6009: 6003: 6002: 5992: 5982: 5950: 5944: 5943: 5917: 5911: 5910: 5882: 5876: 5875: 5865: 5855: 5823: 5817: 5816: 5804: 5790: 5784: 5779:From page 2992: 5778: 5754: 5748: 5747: 5737: 5713: 5707: 5706: 5678: 5672: 5671: 5643: 5637: 5636: 5608: 5602: 5601: 5557: 5551: 5550: 5514: 5508: 5507: 5479: 5473: 5472: 5450: 5444: 5443: 5425: 5416: 5415: 5413: 5411: 5396: 5390: 5389: 5371: 5347: 5341: 5340: 5330: 5306: 5300: 5299: 5277: 5271: 5270: 5260: 5236: 5230: 5229: 5193: 5187: 5186: 5176: 5166: 5142: 5136: 5135: 5109: 5103: 5102: 5100: 5098: 5078: 5072: 5071: 5069: 5067: 5052: 5046: 5045: 5017: 5011: 5010: 4991:10.1038/206757a0 4966: 4960: 4959: 4957: 4955: 4941: 4935: 4934: 4924: 4900: 4884: 4878: 4876: 4853: 4847: 4846: 4844: 4842: 4827: 4821: 4820: 4818: 4816: 4811:. Nobelprize.org 4805:"Eduard Buchner" 4801: 4795: 4794: 4772: 4766: 4756: 4743:Kühne W (1877). 4739: 4733: 4732: 4704: 4698: 4697: 4681: 4675: 4674: 4660: 4654: 4653: 4638: 4632: 4631: 4603: 4597: 4596: 4552: 4546: 4545: 4535: 4503: 4497: 4496: 4486: 4454: 4448: 4447: 4419: 4413: 4412: 4411: 4405: 4385: 4302:Enzyme databases 4280: 4275: 4274: 4266: 4261: 4260: 4038:Camembert cheese 3955:Amyloglucosidase 3913:Brewing industry 3863:Pretreatment of 3839:Biofuel industry 3823: 3822: 3810:organic solvents 3756:gene duplication 3652:Genetic disorder 3629: 3447:beta-lactam ring 3431:enzyme induction 3395:chymotrypsinogen 3195:active transport 3142:Highly alkaline 2935: 2932: 2831:to the protein. 2731:Enzyme inhibitor 2711: 2700: 2669:, respectively. 2668: 2666: 2665: 2660: 2658: 2657: 2649: 2648: 2631: 2629: 2628: 2623: 2621: 2620: 2612: 2611: 2604: 2603: 2595: 2594: 2587: 2586: 2570: 2568: 2567: 2562: 2560: 2559: 2558: 2535: 2533: 2532: 2527: 2525: 2524: 2523: 2513: 2508: 2507: 2506: 2350:Leonor Michaelis 2329:Saturation curve 2325: 2304:enzyme catalysis 2299: 2272:transition state 2258: 2240: 2238: 2237: 2232: 2230: 2228: 2225: 2218: 2215: 2212: 2205: 2203: 2200: 2197: 2191: 2187: 2185: 2182: 2175: 2170: 2167: 2164: 2157: 2146: 2138: 2120: 2118: 2117: 2112: 2110: 2108: 2105: 2098: 2095: 2092: 2085: 2083: 2080: 2077: 2071: 2067: 2065: 2062: 2055: 2050: 2047: 2044: 2037: 2026: 1998:transition state 1908:tetrahydrofolate 1789: 1722: 1715: 1711: 1708: 1702: 1679: 1671: 1630:Protein dynamics 1548:Enzyme catalysis 1529:, the substrate 1493: 1487: 1374: 1355:enzyme structure 1353:Organisation of 1320:allosteric sites 1260:rate of reaction 1161:of various bonds 1144:functional group 796:by lowering its 726:enzyme catalysis 700:by accelerating 691: 690: 687: 686: 683: 680: 677: 674: 671: 668: 647: 640: 633: 620: 615: 614: 504:Chemical biology 422:Mechanosynthesis 397:Electrosynthesis 88: 69: 68: 64: 9756: 9755: 9751: 9750: 9749: 9747: 9746: 9745: 9711: 9710: 9709: 9704: 9616:Oxidoreductases 9602: 9578:Enzyme kinetics 9566: 9562:List of enzymes 9535: 9504: 9475:Catalytic triad 9453: 9448: 9418: 9413: 9345: 9340: 9294: 9289: 9276: 9250: 9226: 9215: 9213: 9206: 9175: 9170: 9140: 9138:Further reading 9135: 9134: 9127: 9113: 9109: 9086: 9082: 9043: 9039: 9016: 9012: 9002: 9000: 8987: 8986: 8979: 8948: 8944: 8915: 8911: 8901: 8899: 8886: 8885: 8881: 8874: 8860: 8856: 8811: 8807: 8800: 8786: 8777: 8746: 8739: 8700: 8693: 8640: 8636: 8605: 8601: 8570: 8566: 8535: 8531: 8510:(11): 403–405. 8500: 8496: 8489: 8475: 8471: 8424: 8420: 8375: 8371: 8324: 8320: 8310: 8308: 8303: 8302: 8298: 8285: 8284: 8280: 8249: 8245: 8214: 8210: 8200: 8198: 8193: 8192: 8188: 8141: 8137: 8114:(10): 697–702. 8100: 8096: 8059: 8055: 8010: 8006: 7961: 7957: 7950: 7936: 7932: 7891: 7887: 7880: 7866: 7862: 7817: 7813: 7768: 7764: 7757: 7743: 7732: 7685: 7681: 7644: 7640: 7609: 7605: 7560: 7556: 7511: 7507: 7462: 7458: 7443: 7429: 7425: 7388: 7384: 7345: 7341: 7304: 7300: 7255: 7248: 7217: 7213: 7176: 7172: 7130: 7126: 7086: 7080: 7076: 7039: 7035: 7012: 7008: 7001: 6987: 6976: 6929: 6925: 6904:(10): 597–604. 6894: 6890: 6859: 6855: 6810: 6806: 6749: 6745: 6730: 6716: 6712: 6705: 6695:Bioenergetics 3 6691: 6687: 6680: 6662: 6658: 6603: 6599: 6589: 6587: 6582: 6581: 6577: 6570: 6556: 6549: 6517: 6513: 6482: 6478: 6471: 6457: 6453: 6443: 6441: 6430: 6426: 6379: 6375: 6330: 6326: 6287: 6283: 6230: 6226: 6171: 6167: 6160: 6146: 6142: 6095: 6091: 6084: 6070: 6066: 6035: 6031: 6024: 6010: 6006: 5951: 5947: 5932: 5918: 5914: 5883: 5879: 5824: 5820: 5813: 5791: 5787: 5755: 5751: 5728:(4): R91–R105. 5714: 5710: 5679: 5675: 5644: 5640: 5609: 5605: 5558: 5554: 5515: 5511: 5480: 5476: 5469: 5451: 5447: 5440: 5426: 5419: 5409: 5407: 5398: 5397: 5393: 5348: 5344: 5307: 5303: 5296: 5278: 5274: 5237: 5233: 5194: 5190: 5143: 5139: 5132: 5110: 5106: 5096: 5094: 5079: 5075: 5065: 5063: 5053: 5049: 5018: 5014: 4967: 4963: 4953: 4951: 4943: 4942: 4938: 4885: 4881: 4854: 4850: 4840: 4838: 4829: 4828: 4824: 4814: 4812: 4803: 4802: 4798: 4791: 4773: 4769: 4763:zu bezeichnen." 4740: 4736: 4715:(12): 511–515. 4705: 4701: 4682: 4678: 4661: 4657: 4639: 4635: 4604: 4600: 4563:(5194): 90–93. 4553: 4549: 4504: 4500: 4455: 4451: 4420: 4416: 4406: 4402: 4386: 4341: 4336: 4304: 4291:List of enzymes 4276: 4269: 4262: 4255: 4252: 4221:Starch industry 4158:recombinant DNA 4055:Food processing 3801: 3795: 3740: 3720:cancer syndrome 3673:phenylketonuria 3654: 3621: 3606:phenylketonuria 3594: 3558:gene expression 3539: 3521:and the acidic 3509:. In addition, 3485:. For example, 3479: 3459:drug metabolism 3443:beta-lactamases 3427:gene regulation 3415: 3375:phosphorylation 3359:phosphorylation 3351: 3326: 3318: 3274: 3252:and eventually 3151: 3081:Cholinesterase 3021:Acidic-neutral 3004:Amylase (malt) 2944:pH description 2925: 2845: 2821: 2812:mixed inhibitor 2808: 2795: 2788: 2784: 2775: 2773:Non-competitive 2746: 2741: 2733: 2727: 2726: 2725: 2724: 2723: 2712: 2703: 2702: 2701: 2690: 2650: 2644: 2643: 2642: 2637: 2634: 2633: 2613: 2607: 2606: 2605: 2596: 2590: 2589: 2588: 2582: 2578: 2576: 2573: 2572: 2548: 2547: 2543: 2541: 2538: 2537: 2519: 2518: 2514: 2509: 2496: 2495: 2491: 2489: 2486: 2485: 2440: 2433: 2422:turnover number 2419: 2412: 2405: 2394: 2385: 2342: 2340:Enzyme kinetics 2336: 2335: 2334: 2333: 2332: 2326: 2317: 2316: 2315: 2310:(S) to produce 2300: 2289: 2248: 2226: 2221: 2213: 2208: 2196: 2190: 2183: 2178: 2169: 2165: 2160: 2155: 2153: 2150: 2149: 2128: 2106: 2101: 2093: 2088: 2076: 2070: 2063: 2058: 2049: 2045: 2040: 2035: 2033: 2030: 2029: 2016: 2004:Main articles: 1982: 1880: 1872:DNA polymerases 1798: 1781: 1762: 1745: 1739: 1723: 1712: 1706: 1703: 1692: 1680: 1669: 1632: 1626: 1610:catalytic triad 1554: 1544: 1518:Daniel Koshland 1514: 1501: 1489: 1479: 1382: 1366: 1347: 1270: 1252:Q10 coefficient 1244: 1157:: catalyze the 1129:Oxidoreductases 1089:. Examples are 1083:Enzyme activity 1073: 1014:James B. Sumner 957:, and the word 890:French chemist 861: 853:meat tenderizer 665: 661: 651: 610: 603: 602: 588: 580: 579: 578: 577: 487: 479: 478: 477: 476: 467:Total synthesis 345: 337: 336: 335: 334: 180: 172: 171: 157: 149: 148: 139:Gene expression 124: 116: 93: 56: 24: 17: 12: 11: 5: 9754: 9744: 9743: 9738: 9733: 9728: 9723: 9706: 9705: 9703: 9702: 9689: 9676: 9663: 9650: 9637: 9624: 9610: 9608: 9604: 9603: 9601: 9600: 9595: 9590: 9585: 9580: 9574: 9572: 9568: 9567: 9565: 9564: 9559: 9554: 9549: 9543: 9541: 9540:Classification 9537: 9536: 9534: 9533: 9528: 9523: 9518: 9512: 9510: 9506: 9505: 9503: 9502: 9497: 9492: 9487: 9482: 9477: 9472: 9467: 9461: 9459: 9455: 9454: 9447: 9446: 9439: 9432: 9424: 9415: 9414: 9412: 9411: 9406: 9401: 9396: 9391: 9386: 9381: 9376: 9371: 9366: 9361: 9356: 9350: 9347: 9346: 9343:Food chemistry 9339: 9338: 9331: 9324: 9316: 9308: 9307: 9293: 9292:External links 9290: 9286: 9285: 9281: 9280: 9275:978-3527330744 9274: 9260: 9259: 9255: 9254: 9248: 9234: 9233: 9228: 9224: 9223: 9204: 9188: 9187: 9183: 9182: 9168: 9150: 9149: 9141: 9139: 9136: 9133: 9132: 9125: 9107: 9096:(3): 190–194. 9080: 9053:(2): 147–157. 9037: 9010: 8977: 8958:(5): 373–403. 8942: 8929:(2): 169–184. 8909: 8879: 8872: 8854: 8825:(6): 958–965. 8805: 8799:978-0412298004 8798: 8775: 8756:(4): 345–351. 8737: 8691: 8634: 8615:(4): 395–400. 8599: 8564: 8529: 8494: 8488:978-1437703146 8487: 8469: 8418: 8389:(3): 151–159. 8369: 8318: 8296: 8278: 8243: 8224:(2): 103–125. 8208: 8186: 8135: 8094: 8073:(3): 429–438. 8053: 8024:(4): 282–293. 8004: 7975:(4): 541–551. 7955: 7948: 7930: 7885: 7879:978-0748760114 7878: 7860: 7831:(2): 153–158. 7811: 7762: 7755: 7730: 7679: 7638: 7619:(2): 163–175. 7603: 7574:(1): 123–142. 7554: 7525:(4): 780–794. 7505: 7476:(2): 225–236. 7456: 7441: 7423: 7382: 7339: 7298: 7269:(6): 949–964. 7246: 7227:(2): 395–424. 7211: 7184:SLAS Discovery 7170: 7124: 7074: 7053:(4): 340–341. 7047:The Oncologist 7033: 7006: 6999: 6974: 6923: 6888: 6853: 6824:(2): 338–339. 6804: 6743: 6728: 6710: 6703: 6685: 6679:978-0781749916 6678: 6656: 6597: 6575: 6568: 6547: 6511: 6492:(9): 359–363. 6476: 6469: 6451: 6424: 6373: 6344:(3): 207–216. 6324: 6297:(1): 149–156. 6281: 6224: 6165: 6158: 6140: 6089: 6083:978-1464109621 6082: 6064: 6029: 6022: 6004: 5945: 5930: 5912: 5893:(5): 619–629. 5877: 5818: 5811: 5785: 5769:(3): 2985–93. 5749: 5708: 5673: 5638: 5603: 5552: 5531:10.1038/nrm804 5525:(5): 364–376. 5509: 5490:(4): 305–313. 5474: 5467: 5445: 5438: 5417: 5391: 5342: 5301: 5295:978-1405119221 5294: 5272: 5231: 5188: 5151:Biology Direct 5137: 5130: 5104: 5073: 5047: 5028:(7): 287–289. 5012: 4961: 4949:Nobelprize.org 4936: 4915:(4): R77–R81. 4879: 4848: 4835:Nobelprize.org 4822: 4796: 4789: 4767: 4734: 4699: 4676: 4655: 4633: 4614:(6): 465–469. 4598: 4547: 4498: 4469:(2): 323–334. 4449: 4430:(2): 537–544. 4414: 4400: 4338: 4337: 4335: 4332: 4331: 4330: 4325: 4320: 4315: 4310: 4303: 4300: 4299: 4298: 4293: 4288: 4282: 4281: 4267: 4264:Biology portal 4251: 4248: 4245: 4244: 4229: 4224: 4216: 4215: 4212:contact lenses 4208: 4203: 4195: 4194: 4183: 4177:hemicellulases 4170: 4167:Paper industry 4162: 4161: 4146: 4133: 4125: 4124: 4117: 4107: 4106: 4103:hypoallergenic 4099: 4093: 4092: 4081: 4075: 4074: 4063: 4058: 4050: 4049: 4034: 4028: 4027: 4017: 4012: 4009:Dairy industry 4004: 4003: 3997: 3992: 3984: 3983: 3976: 3969: 3968: 3961: 3951: 3950: 3943: 3941:Betaglucanases 3937: 3936: 3929: 3916: 3908: 3907: 3900: 3894: 3893: 3890: 3877: 3869: 3868: 3861: 3855: 3854: 3847: 3842: 3834: 3833: 3830: 3827: 3797:Main article: 3794: 3791: 3739: 3736: 3666:hexosaminidase 3612:substrate and 3593: 3590: 3538: 3535: 3478: 3475: 3414: 3411: 3409:or proenzyme. 3363:myristoylation 3350: 3347: 3325: 3322: 3317: 3314: 3273: 3270: 3150: 3147: 3144: 3143: 3140: 3137: 3133: 3132: 3129: 3126: 3122: 3121: 3118: 3115: 3111: 3110: 3107: 3104: 3100: 3099: 3096: 3093: 3089: 3088: 3085: 3082: 3078: 3077: 3074: 3071: 3067: 3066: 3063: 3060: 3056: 3055: 3052: 3049: 3045: 3044: 3041: 3038: 3034: 3033: 3030: 3027: 3023: 3022: 3019: 3016: 3012: 3011: 3008: 3005: 3001: 3000: 2997: 2994: 2990: 2989: 2986: 2983: 2979: 2978: 2975: 2972: 2968: 2967: 2964: 2961: 2957: 2956: 2955:Highly acidic 2953: 2950: 2946: 2945: 2942: 2939: 2924: 2921: 2879:used to treat 2844: 2841: 2820: 2817: 2807: 2804: 2794: 2791: 2786: 2782: 2774: 2771: 2745: 2742: 2740: 2737: 2729:Main article: 2713: 2706: 2705: 2704: 2695: 2694: 2693: 2692: 2691: 2689: 2686: 2656: 2653: 2647: 2641: 2619: 2616: 2610: 2602: 2599: 2593: 2585: 2581: 2557: 2554: 2551: 2546: 2522: 2517: 2512: 2505: 2502: 2499: 2494: 2443:rate constants 2438: 2431: 2417: 2410: 2403: 2392: 2383: 2338:Main article: 2327: 2320: 2319: 2318: 2301: 2294: 2293: 2292: 2291: 2290: 2288: 2285: 2262: 2261: 2252: 2250: 2249:concentration) 2246: 2224: 2211: 2194: 2181: 2173: 2163: 2142: 2141: 2132: 2130: 2129:concentration) 2126: 2104: 2091: 2074: 2061: 2053: 2043: 1981: 1980:Thermodynamics 1978: 1958: 1957: 1951: 1944: 1938: 1932: 1879: 1876: 1794:Main article: 1761: 1758: 1741:Main article: 1738: 1735: 1725: 1724: 1683: 1681: 1674: 1668: 1665: 1645:protein domain 1625: 1622: 1598: 1597: 1596: 1595: 1588: 1582: 1581: 1580: 1574: 1573: 1572: 1543: 1540: 1534:noise via the 1513: 1510: 1500: 1497: 1434:RNA polymerase 1429:DNA polymerase 1410:stereospecific 1406:regioselective 1402:chemoselective 1381: 1378: 1346: 1343: 1243: 1240: 1199: 1198: 1191: 1188:covalent bonds 1180: 1169: 1162: 1151: 1136: 1099:DNA polymerase 1072: 1069: 999:DNA polymerase 965:Eduard Buchner 867:Eduard Buchner 860: 857: 754:, also called 653: 652: 650: 649: 642: 635: 627: 624: 623: 622: 621: 605: 604: 601: 600: 595: 589: 586: 585: 582: 581: 576: 575: 570: 565: 560: 555: 550: 545: 540: 535: 533:Neurochemistry 530: 525: 524: 523: 513: 512: 511: 501: 496: 490: 489: 488: 485: 484: 481: 480: 475: 474: 469: 464: 459: 454: 449: 447:Retrosynthesis 444: 442:Radiosynthesis 439: 434: 429: 424: 419: 414: 409: 404: 399: 394: 389: 387:Direct process 384: 379: 374: 372:Chemosynthesis 369: 364: 359: 354: 348: 347: 346: 343: 342: 339: 338: 333: 332: 327: 322: 315: 314: 313: 303: 293: 292: 291: 281: 276: 271: 261: 256: 251: 246: 241: 236: 235: 234: 224: 219: 209: 204: 199: 194: 183: 182: 181: 178: 177: 174: 173: 170: 169: 164: 158: 155: 154: 151: 150: 147: 146: 141: 136: 131: 125: 123:Key components 122: 121: 118: 117: 115: 114: 109: 104: 98: 95: 94: 89: 81: 80: 74: 73: 15: 9: 6: 4: 3: 2: 9753: 9742: 9739: 9737: 9734: 9732: 9729: 9727: 9724: 9722: 9719: 9718: 9716: 9700: 9696: 9695: 9690: 9687: 9683: 9682: 9677: 9674: 9670: 9669: 9664: 9661: 9657: 9656: 9651: 9648: 9644: 9643: 9638: 9635: 9631: 9630: 9625: 9622: 9618: 9617: 9612: 9611: 9609: 9605: 9599: 9596: 9594: 9591: 9589: 9586: 9584: 9581: 9579: 9576: 9575: 9573: 9569: 9563: 9560: 9558: 9557:Enzyme family 9555: 9553: 9550: 9548: 9545: 9544: 9542: 9538: 9532: 9529: 9527: 9524: 9522: 9521:Cooperativity 9519: 9517: 9514: 9513: 9511: 9507: 9501: 9498: 9496: 9493: 9491: 9488: 9486: 9483: 9481: 9480:Oxyanion hole 9478: 9476: 9473: 9471: 9468: 9466: 9463: 9462: 9460: 9456: 9452: 9445: 9440: 9438: 9433: 9431: 9426: 9425: 9422: 9410: 9407: 9405: 9402: 9400: 9397: 9395: 9392: 9390: 9387: 9385: 9384:Fortification 9382: 9380: 9377: 9375: 9372: 9370: 9367: 9365: 9362: 9360: 9359:Carbohydrates 9357: 9355: 9352: 9351: 9348: 9344: 9337: 9332: 9330: 9325: 9323: 9318: 9317: 9314: 9310: 9305: 9300: 9296: 9295: 9284: 9277: 9271: 9267: 9262: 9261: 9257: 9256: 9251: 9245: 9241: 9236: 9235: 9231: 9230: 9229: 9227: 9211: 9207: 9205:84-370-3328-4 9201: 9197: 9196: 9190: 9189: 9185: 9184: 9179: 9171: 9169:0-7167-3051-0 9165: 9160: 9159: 9152: 9151: 9147: 9146: 9145: 9144: 9128: 9126:9780080926551 9122: 9118: 9111: 9103: 9099: 9095: 9091: 9084: 9076: 9072: 9068: 9064: 9060: 9056: 9052: 9048: 9041: 9033: 9029: 9025: 9021: 9014: 8998: 8994: 8990: 8984: 8982: 8973: 8969: 8965: 8961: 8957: 8953: 8946: 8937: 8932: 8928: 8924: 8920: 8913: 8897: 8893: 8889: 8883: 8875: 8869: 8865: 8858: 8850: 8846: 8842: 8838: 8833: 8828: 8824: 8820: 8816: 8809: 8801: 8795: 8791: 8784: 8782: 8780: 8771: 8767: 8763: 8759: 8755: 8751: 8744: 8742: 8733: 8729: 8725: 8721: 8717: 8713: 8709: 8705: 8698: 8696: 8687: 8683: 8678: 8673: 8669: 8665: 8661: 8657: 8653: 8649: 8645: 8638: 8630: 8626: 8622: 8618: 8614: 8610: 8603: 8595: 8591: 8587: 8583: 8579: 8575: 8568: 8560: 8556: 8552: 8548: 8544: 8540: 8533: 8525: 8521: 8517: 8513: 8509: 8505: 8498: 8490: 8484: 8480: 8473: 8465: 8461: 8457: 8453: 8449: 8445: 8441: 8437: 8433: 8429: 8422: 8414: 8410: 8405: 8400: 8396: 8392: 8388: 8384: 8380: 8373: 8365: 8361: 8356: 8351: 8346: 8341: 8337: 8333: 8329: 8322: 8306: 8300: 8292: 8288: 8282: 8274: 8270: 8266: 8262: 8258: 8254: 8247: 8239: 8235: 8231: 8227: 8223: 8219: 8212: 8196: 8190: 8182: 8178: 8174: 8170: 8166: 8162: 8158: 8154: 8150: 8146: 8139: 8131: 8127: 8122: 8117: 8113: 8109: 8105: 8098: 8090: 8086: 8081: 8076: 8072: 8068: 8064: 8057: 8049: 8045: 8040: 8035: 8031: 8027: 8023: 8019: 8015: 8008: 8000: 7996: 7991: 7986: 7982: 7978: 7974: 7970: 7966: 7959: 7951: 7945: 7941: 7934: 7926: 7922: 7917: 7912: 7908: 7904: 7900: 7896: 7889: 7881: 7875: 7871: 7864: 7856: 7852: 7847: 7842: 7838: 7834: 7830: 7826: 7822: 7815: 7807: 7803: 7798: 7793: 7789: 7785: 7781: 7777: 7773: 7766: 7758: 7752: 7748: 7741: 7739: 7737: 7735: 7726: 7722: 7717: 7712: 7707: 7702: 7698: 7694: 7690: 7683: 7675: 7671: 7666: 7661: 7657: 7653: 7649: 7642: 7634: 7630: 7626: 7622: 7618: 7614: 7607: 7599: 7595: 7590: 7585: 7581: 7577: 7573: 7569: 7565: 7558: 7550: 7546: 7541: 7536: 7532: 7528: 7524: 7520: 7516: 7509: 7501: 7497: 7493: 7489: 7484: 7479: 7475: 7471: 7467: 7460: 7452: 7448: 7444: 7438: 7434: 7427: 7419: 7415: 7410: 7405: 7401: 7397: 7393: 7386: 7378: 7374: 7370: 7366: 7362: 7358: 7354: 7350: 7343: 7335: 7331: 7326: 7321: 7317: 7313: 7309: 7302: 7294: 7290: 7285: 7280: 7276: 7272: 7268: 7264: 7260: 7253: 7251: 7242: 7238: 7234: 7230: 7226: 7222: 7215: 7207: 7203: 7198: 7193: 7189: 7185: 7181: 7174: 7166: 7162: 7158: 7154: 7150: 7146: 7142: 7138: 7134: 7128: 7120: 7116: 7112: 7108: 7104: 7100: 7096: 7092: 7085: 7078: 7070: 7066: 7061: 7056: 7052: 7048: 7044: 7037: 7029: 7025: 7021: 7017: 7010: 7002: 7000:1-85578-158-1 6996: 6992: 6985: 6983: 6981: 6979: 6970: 6966: 6962: 6958: 6954: 6950: 6946: 6942: 6938: 6934: 6927: 6919: 6915: 6911: 6907: 6903: 6899: 6892: 6884: 6880: 6876: 6872: 6868: 6864: 6857: 6849: 6845: 6840: 6835: 6831: 6827: 6823: 6819: 6815: 6808: 6800: 6796: 6791: 6786: 6782: 6778: 6774: 6770: 6766: 6758: 6755:(in German). 6754: 6747: 6739: 6735: 6731: 6729:9783527806461 6725: 6721: 6714: 6706: 6704:0-12-518121-3 6700: 6696: 6689: 6681: 6675: 6671: 6667: 6660: 6652: 6648: 6643: 6638: 6633: 6628: 6624: 6620: 6616: 6612: 6608: 6601: 6585: 6579: 6571: 6569:0-88275-258-8 6565: 6561: 6554: 6552: 6543: 6539: 6535: 6531: 6527: 6523: 6515: 6507: 6503: 6499: 6495: 6491: 6487: 6480: 6472: 6466: 6462: 6455: 6439: 6435: 6428: 6420: 6416: 6412: 6408: 6404: 6400: 6396: 6392: 6388: 6384: 6377: 6369: 6365: 6360: 6355: 6351: 6347: 6343: 6339: 6335: 6328: 6320: 6316: 6312: 6308: 6304: 6300: 6296: 6292: 6285: 6277: 6273: 6269: 6265: 6260: 6255: 6251: 6247: 6243: 6239: 6235: 6228: 6220: 6216: 6211: 6206: 6201: 6196: 6192: 6188: 6184: 6180: 6176: 6169: 6161: 6155: 6151: 6144: 6136: 6132: 6128: 6124: 6120: 6116: 6112: 6108: 6104: 6100: 6093: 6085: 6079: 6075: 6068: 6060: 6056: 6052: 6048: 6044: 6040: 6033: 6025: 6019: 6015: 6008: 6000: 5996: 5991: 5986: 5981: 5976: 5972: 5968: 5964: 5960: 5956: 5949: 5941: 5937: 5933: 5931:0-470-00379-0 5927: 5923: 5916: 5908: 5904: 5900: 5896: 5892: 5888: 5881: 5873: 5869: 5864: 5859: 5854: 5849: 5845: 5841: 5838:(2): 98–104. 5837: 5833: 5829: 5822: 5814: 5812:0-87893-106-6 5808: 5803: 5802: 5796: 5789: 5782: 5776: 5772: 5768: 5765:(in German). 5764: 5760: 5753: 5745: 5741: 5736: 5731: 5727: 5723: 5719: 5712: 5704: 5700: 5696: 5692: 5688: 5684: 5677: 5669: 5665: 5661: 5657: 5653: 5649: 5642: 5634: 5630: 5626: 5622: 5618: 5614: 5607: 5599: 5595: 5591: 5587: 5583: 5579: 5575: 5571: 5567: 5563: 5556: 5548: 5544: 5540: 5536: 5532: 5528: 5524: 5520: 5513: 5505: 5501: 5497: 5493: 5489: 5485: 5478: 5470: 5468:9783527605767 5464: 5460: 5456: 5449: 5441: 5435: 5431: 5424: 5422: 5405: 5401: 5395: 5387: 5383: 5379: 5375: 5370: 5365: 5361: 5357: 5356:FASEB Journal 5353: 5346: 5338: 5334: 5329: 5324: 5320: 5316: 5312: 5305: 5297: 5291: 5287: 5283: 5276: 5268: 5264: 5259: 5254: 5250: 5246: 5242: 5235: 5227: 5223: 5219: 5215: 5211: 5207: 5203: 5199: 5192: 5184: 5180: 5175: 5170: 5165: 5160: 5156: 5152: 5148: 5141: 5133: 5127: 5123: 5119: 5115: 5108: 5092: 5088: 5084: 5077: 5062: 5058: 5051: 5043: 5039: 5035: 5031: 5027: 5023: 5016: 5008: 5004: 5000: 4996: 4992: 4988: 4984: 4980: 4976: 4972: 4965: 4950: 4946: 4940: 4932: 4928: 4923: 4918: 4914: 4910: 4906: 4898: 4894: 4891:: 1359–1381. 4890: 4883: 4874: 4870: 4869: 4862: 4858: 4857:Émile Duclaux 4852: 4836: 4832: 4826: 4810: 4806: 4800: 4792: 4790:9780199743766 4786: 4782: 4778: 4771: 4764: 4760: 4755:(3): 190–193. 4754: 4750: 4746: 4738: 4730: 4726: 4722: 4718: 4714: 4710: 4703: 4695: 4691: 4687: 4680: 4672: 4671: 4667: 4659: 4651: 4647: 4643: 4642:de Réaumur RA 4637: 4629: 4625: 4621: 4617: 4613: 4609: 4602: 4594: 4590: 4586: 4582: 4578: 4574: 4570: 4566: 4562: 4558: 4551: 4543: 4539: 4534: 4529: 4525: 4521: 4517: 4513: 4509: 4502: 4494: 4490: 4485: 4480: 4476: 4472: 4468: 4464: 4460: 4453: 4445: 4441: 4437: 4433: 4429: 4425: 4418: 4410: 4403: 4401:0-7167-4955-6 4397: 4393: 4392: 4384: 4382: 4380: 4378: 4376: 4374: 4372: 4370: 4368: 4366: 4364: 4362: 4360: 4358: 4356: 4354: 4352: 4350: 4348: 4346: 4344: 4339: 4329: 4326: 4324: 4321: 4319: 4316: 4314: 4311: 4309: 4306: 4305: 4297: 4294: 4292: 4289: 4287: 4284: 4283: 4279: 4273: 4268: 4265: 4259: 4254: 4242: 4238: 4234: 4230: 4228: 4225: 4223: 4222: 4213: 4209: 4207: 4204: 4202: 4201: 4200:Personal care 4197: 4192: 4188: 4184: 4182: 4178: 4174: 4171: 4169: 4168: 4164: 4159: 4155: 4151: 4147: 4145: 4141: 4137: 4134: 4132: 4131: 4127: 4122: 4118: 4116: 4112: 4109: 4104: 4100: 4098: 4095: 4090: 4086: 4082: 4080: 4077: 4072: 4068: 4064: 4062: 4059: 4057: 4056: 4047: 4043: 4039: 4035: 4033: 4030: 4025: 4021: 4018: 4016: 4013: 4011: 4010: 4001: 3998: 3996: 3993: 3991: 3990: 3989:Culinary uses 3986: 3981: 3977: 3974: 3971: 3966: 3962: 3960: 3956: 3953: 3948: 3944: 3942: 3939: 3934: 3930: 3928: 3924: 3920: 3917: 3915: 3914: 3905: 3901: 3899: 3896: 3891: 3889: 3885: 3881: 3878: 3876: 3875: 3866: 3862: 3860: 3857: 3852: 3848: 3846: 3843: 3841: 3840: 3831: 3829:Enzymes used 3828: 3825: 3824: 3821: 3819: 3815: 3811: 3806: 3800: 3790: 3787: 3785: 3781: 3777: 3773: 3769: 3765: 3761: 3757: 3753: 3749: 3745: 3735: 3733: 3729: 3725: 3721: 3717: 3713: 3709: 3705: 3700: 3698: 3694: 3690: 3686: 3682: 3681:phenylalanine 3678: 3674: 3669: 3667: 3663: 3659: 3653: 3645: 3641: 3636: 3628: 3624: 3619: 3615: 3611: 3610:Phenylalanine 3607: 3603: 3598: 3589: 3587: 3583: 3579: 3575: 3571: 3567: 3563: 3559: 3555: 3551: 3547: 3544: 3543:multicellular 3534: 3532: 3528: 3524: 3520: 3516: 3512: 3508: 3504: 3503:mitochondrion 3500: 3496: 3492: 3488: 3484: 3474: 3472: 3468: 3464: 3460: 3456: 3452: 3448: 3444: 3440: 3436: 3432: 3428: 3424: 3420: 3419:transcription 3410: 3408: 3404: 3400: 3396: 3392: 3388: 3384: 3380: 3376: 3372: 3368: 3367:glycosylation 3364: 3360: 3356: 3346: 3344: 3340: 3335: 3331: 3321: 3313: 3311: 3305: 3303: 3295: 3291: 3287: 3283: 3278: 3269: 3267: 3263: 3260:, which have 3259: 3255: 3251: 3247: 3243: 3239: 3235: 3231: 3226: 3224: 3223:neuraminidase 3220: 3216: 3212: 3211:HIV integrase 3208: 3204: 3200: 3196: 3192: 3188: 3184: 3180: 3176: 3172: 3168: 3164: 3160: 3156: 3141: 3138: 3135: 3134: 3130: 3127: 3124: 3123: 3119: 3116: 3113: 3112: 3108: 3105: 3102: 3101: 3097: 3094: 3092:Ribonuclease 3091: 3090: 3086: 3083: 3080: 3079: 3075: 3072: 3069: 3068: 3064: 3061: 3058: 3057: 3053: 3050: 3047: 3046: 3042: 3039: 3036: 3035: 3031: 3028: 3025: 3024: 3020: 3017: 3014: 3013: 3009: 3006: 3003: 3002: 2998: 2995: 2992: 2991: 2987: 2984: 2981: 2980: 2976: 2973: 2970: 2969: 2965: 2962: 2959: 2958: 2954: 2951: 2948: 2947: 2943: 2940: 2937: 2936: 2931: 2928: 2920: 2918: 2914: 2910: 2906: 2905:prostaglandin 2902: 2898: 2894: 2890: 2886: 2882: 2878: 2874: 2870: 2866: 2861: 2859: 2855: 2850: 2840: 2838: 2834: 2830: 2829:covalent bond 2826: 2816: 2813: 2803: 2800: 2793:Uncompetitive 2790: 2780: 2770: 2768: 2765:and exert an 2763: 2762:dihydrofolate 2759: 2755: 2751: 2736: 2732: 2721: 2717: 2714:The coenzyme 2710: 2699: 2685: 2683: 2679: 2675: 2670: 2654: 2651: 2639: 2617: 2614: 2600: 2597: 2583: 2579: 2544: 2515: 2510: 2492: 2483: 2479: 2475: 2471: 2467: 2463: 2459: 2455: 2451: 2450: 2444: 2437: 2430: 2425: 2423: 2416: 2409: 2402: 2398: 2391: 2387: 2382: 2378: 2377:concentration 2374: 2369: 2367: 2363: 2359: 2355: 2351: 2347: 2346:enzyme assays 2341: 2330: 2324: 2313: 2309: 2305: 2298: 2284: 2282: 2276: 2273: 2269: 2260: 2253: 2251: 2244: 2222: 2209: 2192: 2179: 2171: 2161: 2148: 2147: 2140: 2133: 2131: 2124: 2102: 2089: 2072: 2059: 2051: 2041: 2028: 2027: 2024: 2022: 2015: 2011: 2007: 1999: 1995: 1991: 1986: 1977: 1975: 1971: 1967: 1962: 1956: 1952: 1949: 1945: 1943: 1939: 1937: 1933: 1931: 1927: 1923: 1922: 1921: 1919: 1918: 1913: 1909: 1905: 1901: 1897: 1893: 1889: 1885: 1875: 1873: 1869: 1865: 1861: 1857: 1852: 1850: 1846: 1841: 1839: 1835: 1831: 1827: 1823: 1819: 1815: 1811: 1807: 1804:(e.g., metal 1803: 1797: 1788: 1784: 1779: 1775: 1774:transketolase 1771: 1766: 1757: 1755: 1751: 1744: 1734: 1731: 1721: 1718: 1710: 1700: 1696: 1690: 1689: 1684:This section 1682: 1678: 1673: 1672: 1664: 1662: 1658: 1654: 1650: 1646: 1642: 1638: 1631: 1621: 1619: 1615: 1614:oxyanion hole 1611: 1607: 1603: 1593: 1589: 1586: 1585: 1583: 1578: 1577: 1575: 1570: 1569: 1567: 1566: 1565: 1563: 1559: 1553: 1549: 1539: 1537: 1532: 1528: 1524: 1519: 1509: 1506: 1492: 1486: 1482: 1477: 1473: 1469: 1465: 1460: 1456: 1454: 1450: 1445: 1443: 1439: 1435: 1430: 1426: 1425:proof-reading 1422: 1418: 1413: 1411: 1407: 1403: 1399: 1395: 1391: 1387: 1373: 1369: 1364: 1363:peptidoglycan 1360: 1356: 1351: 1342: 1340: 1336: 1332: 1327: 1325: 1321: 1317: 1312: 1310: 1306: 1305:binding sites 1302: 1298: 1294: 1289: 1287: 1283: 1279: 1275: 1269: 1261: 1257: 1253: 1248: 1239: 1237: 1233: 1229: 1225: 1223: 1218: 1214: 1210: 1208: 1204: 1196: 1192: 1189: 1185: 1181: 1178: 1177:isomerization 1174: 1170: 1167: 1163: 1160: 1156: 1152: 1149: 1145: 1142:: transfer a 1141: 1137: 1134: 1130: 1126: 1125: 1124: 1121: 1119: 1115: 1111: 1106: 1104: 1100: 1096: 1092: 1088: 1084: 1080: 1078: 1068: 1066: 1062: 1058: 1054: 1050: 1045: 1043: 1039: 1035: 1031: 1027: 1023: 1019: 1015: 1011: 1007: 1002: 1000: 996: 992: 988: 984: 983: 978: 974: 970: 966: 962: 960: 956: 952: 948: 944: 941: 938: 935: 934:Ancient Greek 931: 930: 925: 924:Wilhelm Kühne 920: 917: 913: 912:Louis Pasteur 909: 905: 901: 897: 893: 892:Anselme Payen 888: 886: 882: 878: 874: 865: 856: 854: 850: 846: 842: 837: 835: 831: 827: 823: 819: 815: 811: 807: 803: 799: 795: 794:reaction rate 786: 782: 780: 776: 771: 769: 765: 761: 757: 753: 748: 745: 743: 739: 735: 731: 727: 723: 719: 716:. Almost all 715: 711: 707: 703: 699: 695: 689: 659: 648: 643: 641: 636: 634: 629: 628: 626: 625: 619: 609: 608: 607: 606: 599: 596: 594: 591: 590: 584: 583: 574: 571: 569: 566: 564: 561: 559: 556: 554: 551: 549: 546: 544: 541: 539: 536: 534: 531: 529: 526: 522: 519: 518: 517: 514: 510: 507: 506: 505: 502: 500: 497: 495: 492: 491: 483: 482: 473: 470: 468: 465: 463: 460: 458: 455: 453: 452:Semisynthesis 450: 448: 445: 443: 440: 438: 435: 433: 430: 428: 425: 423: 420: 418: 415: 413: 410: 408: 405: 403: 400: 398: 395: 393: 390: 388: 385: 383: 380: 378: 375: 373: 370: 368: 365: 363: 360: 358: 355: 353: 350: 349: 341: 340: 331: 328: 326: 325:Tetrapyrroles 323: 321: 320: 316: 312: 309: 308: 307: 304: 302: 301: 299: 294: 290: 287: 286: 285: 282: 280: 277: 275: 272: 270: 269: 267: 266:Nucleic acids 262: 260: 257: 255: 252: 250: 249:Sphingolipids 247: 245: 244:Phospholipids 242: 240: 237: 233: 230: 229: 228: 225: 223: 220: 218: 217: 215: 210: 208: 205: 203: 202:Glycoproteins 200: 198: 195: 193: 192: 190: 189:Carbohydrates 185: 184: 176: 175: 168: 165: 163: 160: 159: 153: 152: 145: 142: 140: 137: 135: 132: 130: 127: 126: 120: 119: 113: 110: 108: 105: 103: 100: 99: 97: 96: 92: 87: 83: 82: 79: 76: 75: 71: 70: 63: 59: 54: 51: 47: 43: 39: 35: 30: 26: 22: 9726:Biomolecules 9694:Translocases 9691: 9678: 9665: 9652: 9639: 9629:Transferases 9626: 9613: 9470:Binding site 9450: 9368: 9309: 9282: 9265: 9239: 9225: 9214:. Retrieved 9210:the original 9194: 9158:Biochemistry 9157: 9116: 9110: 9093: 9089: 9083: 9050: 9046: 9040: 9026:(1): 21–28. 9023: 9019: 9013: 9001:. Retrieved 8997:the original 8992: 8955: 8951: 8945: 8926: 8922: 8912: 8900:. Retrieved 8896:the original 8891: 8882: 8863: 8857: 8822: 8818: 8808: 8789: 8753: 8749: 8707: 8703: 8651: 8647: 8637: 8612: 8608: 8602: 8577: 8573: 8567: 8542: 8538: 8532: 8507: 8503: 8497: 8478: 8472: 8431: 8427: 8421: 8386: 8382: 8372: 8335: 8331: 8321: 8309:. Retrieved 8299: 8290: 8281: 8256: 8252: 8246: 8221: 8217: 8211: 8199:. Retrieved 8189: 8148: 8144: 8138: 8111: 8107: 8097: 8070: 8066: 8056: 8021: 8017: 8007: 7972: 7968: 7958: 7939: 7933: 7898: 7888: 7869: 7863: 7828: 7824: 7814: 7779: 7775: 7765: 7746: 7696: 7692: 7682: 7655: 7651: 7641: 7616: 7612: 7606: 7571: 7567: 7557: 7522: 7518: 7508: 7473: 7469: 7459: 7432: 7426: 7399: 7395: 7385: 7352: 7348: 7342: 7315: 7311: 7301: 7266: 7262: 7224: 7220: 7214: 7187: 7183: 7173: 7140: 7137:FEBS Letters 7136: 7127: 7094: 7090: 7077: 7050: 7046: 7036: 7019: 7015: 7009: 6990: 6936: 6932: 6926: 6901: 6897: 6891: 6866: 6863:Biochemistry 6862: 6856: 6821: 6817: 6807: 6772: 6769:Biochemistry 6768: 6756: 6752: 6746: 6719: 6713: 6694: 6688: 6669: 6659: 6614: 6610: 6600: 6588:. Retrieved 6578: 6559: 6525: 6522:Biochemistry 6521: 6514: 6489: 6485: 6479: 6460: 6454: 6442:. 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Retrieved 4808: 4799: 4780: 4770: 4762: 4758: 4752: 4748: 4737: 4712: 4708: 4702: 4693: 4689: 4679: 4669: 4665: 4658: 4649: 4645: 4636: 4611: 4607: 4601: 4560: 4556: 4550: 4515: 4511: 4501: 4466: 4462: 4452: 4427: 4423: 4417: 4391:Biochemistry 4390: 4239:and various 4219: 4198: 4165: 4128: 4121:fruit juices 4105:baby foods. 4101:Manufacture 4053: 4042:blue cheeses 4007: 3987: 3959:pullulanases 3945:Improve the 3911: 3872: 3837: 3826:Application 3817: 3802: 3788: 3741: 3728:skin cancers 3701: 3670: 3655: 3540: 3529:or reducing 3480: 3416: 3391:Chymotrypsin 3353:Examples of 3352: 3327: 3319: 3306: 3299: 3227: 3193:involved in 3183:cytoskeleton 3173:hydrolyzing 3167:phosphatases 3152: 2929: 2926: 2901:inflammation 2865:methotrexate 2862: 2846: 2822: 2819:Irreversible 2809: 2796: 2776: 2754:methotrexate 2747: 2734: 2720:methotrexate 2671: 2453: 2447: 2435: 2428: 2426: 2421: 2414: 2407: 2400: 2389: 2388: 2380: 2370: 2343: 2277: 2265: 2254: 2134: 2017: 1969: 1963: 1959: 1915: 1881: 1867: 1863: 1859: 1855: 1853: 1842: 1799: 1746: 1728: 1713: 1707:October 2023 1704: 1693:Please help 1688:verification 1685: 1637:protein loop 1633: 1599: 1555: 1527:glycosidases 1515: 1505:Emil Fischer 1502: 1446: 1414: 1383: 1328: 1313: 1290: 1271: 1256:denaturation 1231: 1227: 1226: 1216: 1212: 1211: 1200: 1195:Translocases 1147: 1140:Transferases 1122: 1114:nomenclature 1107: 1086: 1082: 1081: 1074: 1046: 1042:chymotrypsin 1009: 1003: 980: 963: 958: 950: 942: 937: 927: 921: 902:of sugar to 900:fermentation 889: 870: 838: 791: 773:An enzyme's 772: 767: 763: 759: 749: 746: 733: 657: 656: 563:parasitology 558:Bacteriology 521:Pharmacology 499:Cell biology 367:Biosynthesis 318: 317: 296: 295: 264: 263: 212: 211: 187: 186: 133: 129:Biomolecules 90: 78:Biochemistry 55:in yellow. ( 25: 21:Biocatalysis 9465:Active site 9003:28 February 8993:GMO Compass 8892:GMO Compass 8710:(1): 1–11. 8545:: 133–140. 8311:5 September 7355:: 249–284. 7190:(1): 3–20. 6753:Biochem. Z. 6590:23 February 5965:(5): e468. 5689:: 471–505. 5654:: 415–435. 5619:: 617–650. 4954:23 February 4841:23 February 4815:23 February 4652:: 266, 461. 4278:Food portal 4144:polymerases 3982:formation. 3658:homeostasis 3586:blood sugar 3574:glucokinase 3515:protonation 3511:trafficking 3507:β-oxidation 3487:fatty acids 3467:degradation 3423:translation 3387:blood sugar 3262:herbivorous 3026:Cellobiase 2941:Optimum pH 2915:and blocks 2873:cholesterol 2744:Competitive 2478:β-lactamase 1996:to reach a 1930:NAD or NADP 1906:(TPP), and 1860:apoproteins 1851:reactions. 1653:equilibrium 1639:or unit of 1616:, complete 1538:mechanism. 1523:side-chains 1398:hydrophobic 1394:hydrophilic 1390:Specificity 1309:active site 1286:hot springs 1175:: catalyze 1131:: catalyze 916:vital force 841:antibiotics 826:temperature 806:equilibrium 775:specificity 306:Amino acids 284:Nucleotides 279:Nucleosides 274:Nucleobases 254:Cholesterol 227:Fatty acids 222:Eicosanoids 46:Active site 34:glucosidase 32:The enzyme 9736:Metabolism 9715:Categories 9668:Isomerases 9642:Hydrolases 9509:Regulation 7442:8121903432 7143:(1): 3–6. 6759:: 333–369. 6444:30 October 4901:quoted in 4334:References 4191:kraft pulp 4156:to create 4140:DNA ligase 4115:pectinases 4111:Cellulases 3923:glucanases 3898:Mannanases 3859:Ligninases 3845:Cellulases 3768:methionine 3764:creatinase 3752:adaptation 3748:metabolism 3708:DNA repair 3650:See also: 3570:glycolysis 3566:hexokinase 3546:eukaryotes 3505:, through 3439:penicillin 3429:is called 3324:Regulation 3286:glycolysis 3272:Metabolism 3199:luciferase 2960:Invertase 2903:messenger 2881:retroviral 2833:Penicillin 2716:folic acid 2688:Inhibition 2571:are about 2348:. In 1913 1948:folic acid 1942:coenzyme A 1868:holoenzyme 1864:holoenzyme 1856:apoenzymes 1628:See also: 1618:hydrolysis 1546:See also: 1464:Hexokinase 1417:expression 1386:substrates 1266:See also: 1207:hexokinase 1173:Isomerases 1159:hydrolysis 1155:Hydrolases 1057:egg whites 814:activators 810:inhibitors 742:amino acid 734:enzymology 710:substrates 587:Glossaries 573:immunology 239:Glycerides 207:Glycosides 162:Biochemist 144:Metabolism 9731:Catalysis 9547:EC number 9354:Additives 8338:: 55–73. 8067:Structure 7451:818809626 7097:: 59–68. 6738:992976641 5245:Structure 5157:(1): 31. 5066:28 August 5055:Moss GP. 4909:Structure 4777:"Enzymes" 4206:Proteases 4173:Xylanases 4136:Nucleases 4091:-making. 4079:Proteases 4046:Roquefort 4020:Hydrolyze 4000:Tenderize 3927:proteases 3880:Proteases 3776:sarcosine 3744:mutations 3738:Evolution 3644:recessive 3640:autosomal 3531:cytoplasm 3527:periplasm 3519:cytoplasm 3337:called a 3334:inhibited 3330:activated 3266:cellulase 3258:ruminants 3238:proteases 3219:influenza 3203:fireflies 3191:ion pumps 3155:functions 3136:Arginase 3131:Alkaline 3120:Alkaline 3109:Alkaline 3103:Fumarase 3059:Catalase 2999:Alkaline 2678:diffusion 2652:− 2615:− 2598:− 2308:substrate 2125:; high CO 1878:Coenzymes 1826:coenzymes 1802:inorganic 1760:Cofactors 1602:proteases 1542:Catalysis 1516:In 1958, 1488:​, 1453:neutrally 1442:ribosomes 1345:Mechanism 1335:ribozymes 1316:cofactors 1278:complexes 1242:Structure 1133:oxidation 987:substrate 943:(énzymon) 834:denatured 756:ribozymes 706:molecules 698:catalysts 40:into two 9571:Kinetics 9495:Cofactor 9458:Activity 9404:Vitamins 9399:Proteins 9364:Coloring 9075:26080240 9067:10194388 8849:25674881 8841:11101321 8770:12323357 8732:12058826 8686:18323453 8629:12943848 8594:16433409 8559:29316484 8413:24917953 8364:21753892 8273:11849022 8238:10527663 8089:15016359 8048:27098510 7999:20713603 7806:12615961 7725:18952571 7633:12370077 7549:11294886 7500:13999125 7377:10205781 7293:20640225 7241:15700950 7206:27703080 7165:45356060 7111:26478442 7069:10476546 6969:23465446 6961:17820893 6918:11590012 6883:21506553 6848:16743508 6799:21888353 6651:19073922 6542:15667203 6506:10470036 6419:10621930 6411:15933191 6368:19225609 6319:23988159 6268:16003488 6259:11139141 6219:11050223 6127:12947189 6059:16895325 5999:17520027 5959:PLOS ONE 5940:51720783 5907:12413546 5872:16590179 5744:10099128 5703:20235827 5668:11395413 5633:10966471 5598:40772789 5590:16873663 5547:31605786 5539:11988770 5504:15358000 5386:22853095 5267:19000810 5183:20433725 5042:10390620 4931:10801479 4861:diastase 4696:: 73–92. 4628:17889251 4542:23203881 4493:24107129 4444:28408493 4250:See also 4231:Convert 4227:Amylases 4152:and the 4119:Clarify 4087:, as in 4061:Amylases 4044:such as 4036:Produce 3980:diacetyl 3904:guar gum 3884:amylases 3818:in vitro 3772:creatine 3630:​) 3582:affinity 3578:pancreas 3562:isozymes 3523:lysosome 3437:such as 3413:Quantity 3399:pancreas 3383:glycogen 3357:include 3294:pyruvate 3246:proteins 3234:amylases 3185:. Other 3117:7.8–8.7 3114:Trypsin 3098:Neutral 3095:7.0–7.5 3087:Neutral 3076:Neutral 3065:Neutral 3048:Sucrase 3040:6.1–6.8 3037:Maltase 3018:6.7–7.0 3007:4.6–5.2 2974:4.0–5.0 2952:1.5–1.6 2849:feedback 2474:fumarase 2470:catalase 2373:solution 2287:Kinetics 2245:; low CO 2193:← 2073:→ 1912:vitamins 1790:​) 1750:feedback 1624:Dynamics 1604:such as 1531:molecule 1494:​) 1375:​) 1359:lysozyme 1339:ribosome 1282:denature 1103:isozymes 1053:lysozyme 1036:(1930), 1022:catalase 947:leavened 896:diastase 714:products 694:proteins 618:Category 568:virology 298:Proteins 259:Steroids 197:Alcohols 65:​) 53:cofactor 44:sugars. 9721:Enzymes 9681:Ligases 9451:Enzymes 9379:Flavors 9369:Enzymes 9304:Enzymes 9216:27 June 9148:General 9102:2186082 8972:8573280 8902:1 March 8712:Bibcode 8677:3431203 8656:Bibcode 8648:Science 8524:8291080 8464:4171859 8456:5655953 8436:Bibcode 8404:4040760 8355:3132852 8201:1 March 8181:8473726 8173:5793973 8153:Bibcode 8145:Science 8130:8433729 8039:4915340 7990:2928026 7925:9173866 7916:1218279 7855:8452343 7797:3006448 7716:2674713 7674:2178174 7598:2030669 7492:7834742 7418:2159465 7369:9646869 7334:1464741 7284:2904065 7157:3720956 7119:1550698 6941:Bibcode 6933:Science 6839:1259181 6790:3381512 6642:2604989 6619:Bibcode 6391:Bibcode 6383:Science 6359:2898650 6311:1565147 6276:3343824 6187:Bibcode 6135:7899320 6107:Bibcode 6099:Science 5990:1868595 5967:Bibcode 5840:Bibcode 5570:Bibcode 5562:Science 5410:4 April 5378:8001737 5337:1339435 5226:4124164 5206:Bibcode 5198:Science 5174:2876114 5097:6 March 5007:4161467 4999:5891407 4979:Bibcode 4729:8595136 4593:8145198 4585:7809611 4565:Bibcode 4557:Science 4533:3531171 4484:5679212 4328:MetaCyc 4237:glucose 4185:Remove 4097:Trypsin 4089:biscuit 4032:Lipases 3975:(ALDC) 3919:Amylase 3888:lipases 3865:biomass 3784:kinases 3712:genomes 3554:tissues 3491:cytosol 3453:called 3407:zymogen 3403:stomach 3397:in the 3371:insulin 3290:glucose 3254:glucose 3250:maltose 3207:Viruses 3187:ATPases 3163:kinases 3070:Urease 3054:Acidic 3043:Acidic 3032:Acidic 3010:Acidic 2988:Acidic 2977:Acidic 2966:Acidic 2949:Pepsin 2938:Enzyme 2909:cyanide 2889:aspirin 2869:statins 2837:aspirin 2312:product 2123:tissues 1926:hydride 1917:de novo 1902:(FAD), 1898:(FMN), 1816:(e.g., 1606:trypsin 1592:entropy 1419:of the 1293:monomer 1184:Ligases 1091:lactase 1038:trypsin 995:lactose 991:lactase 989:(e.g., 959:ferment 945: ' 940:ἔνζυμον 904:alcohol 822:poisons 720:in the 658:Enzymes 134:Enzymes 112:History 107:Outline 42:glucose 38:maltose 9655:Lyases 9389:Lipids 9283: 9272:  9246:  9202:  9166:  9123:  9100:  9073:  9065:  8970:  8870:  8847:  8839:  8796:  8768:  8730:  8684:  8674:  8627:  8592:  8557:  8522:  8485:  8462:  8454:  8428:Nature 8411:  8401:  8362:  8352:  8271:  8236:  8179:  8171:  8128:  8087:  8046:  8036:  7997:  7987:  7946:  7923:  7913:  7876:  7853:  7846:187630 7843:  7804:  7794:  7753:  7723:  7713:  7672:  7631:  7596:  7589:372803 7586:  7547:  7537:  7498:  7490:  7449:  7439:  7416:  7375:  7367:  7332:  7291:  7281:  7239:  7204:  7163:  7155:  7117:  7109:  7067:  6997:  6967:  6959:  6916:  6881:  6846:  6836:  6797:  6787:  6736:  6726:  6701:  6676:  6649:  6639:  6566:  6540:  6504:  6467:  6417:  6409:  6366:  6356:  6317:  6309:  6274:  6266:  6256:  6217:  6207:  6156:  6133:  6125:  6080:  6057:  6020:  5997:  5987:  5938:  5928:  5905:  5870:  5863:335371 5860:  5809:  5742:  5701:  5666:  5631:  5596:  5588:  5545:  5537:  5502:  5465:  5436:  5384:  5376:  5335:  5292:  5265:  5224:  5181:  5171:  5128:  5040:  5005:  4997:  4971:Nature 4929:  4837:. 1907 4787:  4761:Enzyme 4727:  4626:  4591:  4583:  4540:  4530:  4491:  4481:  4442:  4398:  4318:IntEnz 4313:ExPASy 4308:BRENDA 4241:syrups 4233:starch 4187:lignin 4067:starch 4024:cheese 4015:Rennin 3995:Papain 3550:organs 3373:, the 3242:starch 3221:virus 3171:myosin 2875:, and 2480:, and 2012:, and 1834:biotin 1818:flavin 1472:xylose 1421:genome 1193:EC 7, 1182:EC 6, 1171:EC 5, 1166:Lyases 1164:EC 4, 1153:EC 3, 1138:EC 2, 1127:EC 1, 1034:pepsin 1018:urease 1010:per se 973:zymase 955:pepsin 951:enzyme 929:enzyme 885:saliva 881:sugars 877:starch 768:enzyme 704:. The 692:) are 616:  319:Other: 214:Lipids 9607:Types 9409:Water 9071:S2CID 8845:S2CID 8460:S2CID 8177:S2CID 7540:32266 7496:S2CID 7373:S2CID 7161:S2CID 7115:S2CID 7087:(PDF) 6965:S2CID 6415:S2CID 6272:S2CID 6210:17266 6131:S2CID 5594:S2CID 5543:S2CID 5382:S2CID 5003:S2CID 4871:[ 4589:S2CID 4235:into 4189:from 4085:flour 3832:Uses 3499:Golgi 3451:liver 3139:10.0 2897:COX-2 2893:COX-1 2806:Mixed 2243:lungs 1888:NADPH 1849:redox 1812:) or 1560:(ΔG, 1521:acid 936: 908:yeast 818:drugs 724:need 417:LASiS 102:Index 9699:list 9692:EC7 9686:list 9679:EC6 9673:list 9666:EC5 9660:list 9653:EC4 9647:list 9640:EC3 9634:list 9627:EC2 9621:list 9614:EC1 9270:ISBN 9244:ISBN 9218:2006 9200:ISBN 9164:ISBN 9121:ISBN 9098:PMID 9063:PMID 9005:2015 8968:PMID 8904:2015 8868:ISBN 8837:PMID 8794:ISBN 8766:PMID 8728:PMID 8682:PMID 8625:PMID 8590:PMID 8555:PMID 8520:PMID 8483:ISBN 8452:PMID 8409:PMID 8360:PMID 8313:2013 8269:PMID 8234:PMID 8203:2015 8169:PMID 8126:PMID 8085:PMID 8044:PMID 7995:PMID 7944:ISBN 7921:PMID 7874:ISBN 7851:PMID 7802:PMID 7751:ISBN 7721:PMID 7670:PMID 7629:PMID 7594:PMID 7545:PMID 7488:PMID 7470:Cell 7447:OCLC 7437:ISBN 7414:PMID 7365:PMID 7330:PMID 7289:PMID 7237:PMID 7202:PMID 7153:PMID 7107:PMID 7065:PMID 6995:ISBN 6957:PMID 6914:PMID 6879:PMID 6844:PMID 6795:PMID 6734:OCLC 6724:ISBN 6699:ISBN 6674:ISBN 6647:PMID 6592:2015 6564:ISBN 6538:PMID 6502:PMID 6465:ISBN 6446:2007 6407:PMID 6364:PMID 6315:PMID 6307:OSTI 6264:PMID 6215:PMID 6154:ISBN 6123:PMID 6078:ISBN 6055:PMID 6018:ISBN 5995:PMID 5936:OCLC 5926:ISBN 5903:PMID 5868:PMID 5807:ISBN 5740:PMID 5699:PMID 5664:PMID 5629:PMID 5586:PMID 5535:PMID 5500:PMID 5463:ISBN 5434:ISBN 5412:2007 5374:PMID 5333:PMID 5290:ISBN 5263:PMID 5222:PMID 5179:PMID 5126:ISBN 5099:2015 5068:2021 5038:PMID 4995:PMID 4956:2015 4927:PMID 4843:2015 4817:2015 4785:ISBN 4725:PMID 4650:1752 4624:PMID 4581:PMID 4538:PMID 4489:PMID 4440:PMID 4396:ISBN 4323:KEGG 4179:and 4148:Use 4142:and 4040:and 3965:beer 3957:and 3947:wort 3933:malt 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Index

Biocatalysis
Ribbon diagram of glycosidase with an arrow showing the cleavage of the maltose sugar substrate into two glucose products.
glucosidase
maltose
glucose
Active site
NAD
cofactor
PDB
1OBB
Biochemistry

Index
Outline
History
Biomolecules
Enzymes
Gene expression
Metabolism
Biochemist
List of biochemists
Carbohydrates
Alcohols
Glycoproteins
Glycosides
Lipids
Eicosanoids
Fatty acids
Fatty-acid metabolism
Glycerides

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