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
2764:
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
2274:
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
1533:
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
2445:
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
1747:
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
1520:
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
1507:
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
1732:
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
3336:
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
1219:
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
2851:
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
1431:
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
1733:
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.
918:
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."
2801:
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
2814:
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,
3533:) which in turn affects enzyme activity. In contrast to partitioning into membrane bound organelles, enzyme subcellular localisation may also be altered through polymerisation of enzymes into macromolecular cytoplasmic filaments.
1847:, which uses a zinc cofactor bound as part of its active site. These tightly bound ions or molecules are usually found in the active site and are involved in catalysis. For example, flavin and heme cofactors are often involved in
3248:, respectively) into smaller ones, so they can be absorbed by the intestines. Starch molecules, for example, are too large to be absorbed from the intestine, but enzymes hydrolyze the starch chains into smaller molecules such as
6519:
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".
1634:
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
3807:
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
804:, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the
5057:"Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes by the Reactions they Catalyse"
2630:
2863:
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
6861:
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".
1004:
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".
1748:
this way, allosteric interactions can either inhibit or activate enzymes. Allosteric interactions with metabolites upstream or downstream in an enzyme's metabolic pathway cause
3405:
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
8572:
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
6665:
3758:
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
2344:
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
3820:
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.
2927:
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.
2752:
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
2395:
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
1655:. Different states within this ensemble may be associated with different aspects of an enzyme's function. For example, different conformations of the enzyme
1288:
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.
979:
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".
6289:
Ramanathan A, Savol A, Burger V, Chennubhotla CS, Agarwal PK (January 2014). "Protein conformational populations and functionally relevant substates".
6484:
Chapman-Smith A, Cronan JE (September 1999). "The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity".
1525:
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
5454:
5281:
4776:
1209:(EC 2.7.1.1) is a transferase (EC 2) that adds a phosphate group (EC 2.7) to a hexose sugar, a molecule containing an alcohol group (EC 2.7.1).
4508:"BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA"
644:
8988:
8887:
2680:
and thermodynamically driven random collision. Many biochemical or cellular processes deviate significantly from these conditions, because of
8251:
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
740:
recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their
1887:
808:
of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules:
7083:
3789:
Artificial (in vitro) evolution is now commonly used to modify enzyme activity or specificity for industrial applications (see below).
6433:
5082:
2789:
is reduced. In contrast to competitive inhibition, non-competitive inhibition cannot be overcome with high substrate concentration.
1314:
In some enzymes, no amino acids are directly involved in catalysis; instead, the enzyme contains sites to bind and orient catalytic
9333:
3816:
is an active area of research and involves attempts to create new enzymes with novel properties, either through rational design or
3564:) available for metabolic reactions. This provides a mechanism for regulating the overall metabolism of the organism. For example,
4855:
The naming of enzymes by adding the suffix "-ase" to the substrate on which the enzyme acts, has been traced to French scientist
801:
1384:
Enzymes must bind their substrates before they can catalyse any chemical reaction. Enzymes are usually very specific as to what
4641:
5399:
9247:
8871:
7947:
7754:
6468:
6157:
6021:
5646:
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".
1587:
Distorting bound substrate(s) into their transition state form to reduce the energy required to reach the transition state
8815:"Improved performances and control of beer fermentation using encapsulated alpha-acetolactate decarboxylase and modeling"
3425:
of enzyme genes) can be enhanced or diminished by a cell in response to changes in the cell's environment. This form of
2574:
9273:
8950:
Guzmán-Maldonado H, Paredes-López O (September 1995). "Amylolytic enzymes and products derived from starch: a review".
8797:
8486:
7877:
6677:
6081:
5293:
2684:
and constrained molecular movement. More recent, complex extensions of the model attempt to correct for these effects.
637:
9193:
9115:
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
1400:
characteristics to the substrates. Enzymes can therefore distinguish between very similar substrate molecules to be
7347:
Wlodawer A, Vondrasek J (1998). "Inhibitors of HIV-1 protease: a major success of structure-assisted drug design".
6037:
Warshel A, Sharma PK, Kato M, Xiang Y, Liu H, Olsson MH (August 2006). "Electrostatic basis for enzyme catalysis".
4830:
2781:
binds to a site other than where the substrate binds. The substrate still binds with its usual affinity and hence K
1579:
Temporarily reacting with the substrate, forming a covalent intermediate to provide a lower energy transition state
3296:
via a series of intermediate metabolites. Each chemical modification (red box) is performed by a different enzyme.
3688:
3354:
371:
9018:
Alkorta I, Garbisu C, Llama MJ, Serra JL (January 1998). "Industrial applications of pectic enzymes: a review".
2151:
2031:
7440:
5955:"Conformational proofreading: the impact of conformational changes on the specificity of molecular recognition"
4804:
3646:
fashion because the enzymes from the unaffected genes are generally sufficient to prevent symptoms in carriers.
2487:
1973:
1920:
and closely related compounds (vitamins) must be acquired from the diet. The chemical groups carried include:
1698:
101:
4686:"Mémoire sur la diastase, les principaux produits de ses réactions et leurs applications aux arts industriels"
9597:
8537:
Ochoa D, Bradley D, Beltrao P (February 2018). "Evolution, dynamics and dysregulation of kinase signalling".
3426:
2396:
2357:
2328:
1291:
Enzymes are usually much larger than their substrates. Sizes range from just 62 amino acid residues, for the
1251:
968:
630:
6751:
Michaelis L, Menten M (1913). "Die
Kinetik der Invertinwirkung" [The Kinetics of Invertase Action].
2911:
is an irreversible enzyme inhibitor that combines with the copper and iron in the active site of the enzyme
9326:
7965:"Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster"
2448:
1296:
5147:"Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution"
1899:
1640:
1535:
1281:
1255:
833:
597:
542:
471:
3710:
enzymes. Defects in these enzymes cause cancer because cells are less able to repair mutations in their
3308:
involves the hydrolysis of ATP. Because this reaction releases so much energy, other reactions that are
1307:
where residues orient the substrates. The catalytic site and binding site together compose the enzyme's
1220:
These families have been documented in dozens of different protein and protein family databases such as
9740:
8702:
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
401:
8104:"Familial hyperglycemia due to mutations in glucokinase. Definition of a subtype of diabetes mellitus"
3634:
2635:
939:
9698:
9685:
9672:
9659:
9646:
9633:
9620:
9582:
8642:
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
406:
351:
9177:
5560:
Zenkin N, Yuzenkova Y, Severinov K (July 2006). "Transcript-assisted transcriptional proofreading".
5482:
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
9592:
9546:
9489:
9303:
8996:
8895:
8304:
4070:
3759:
3692:
3418:
2539:
2457:
1385:
1235:
1117:
1029:
986:
976:
381:
8919:"Review: Compounds Involved in the Flavor of Surface Mold-Ripened Cheeses: Origins and Properties"
7938:
Suzuki H (2015). "Chapter 4: Effect of pH, Temperature, and High
Pressure on Enzymatic Activity".
5681:
Khersonsky O, Tawfik DS (2010). "Enzyme promiscuity: a mechanistic and evolutionary perspective".
2331:
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
1315:
508:
446:
111:
106:
52:
7648:"Recent advances in rumen microbial ecology and metabolism: potential impact on nutrient output"
5758:
5309:
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".
2785:
remains the same. However the inhibitor reduces the catalytic efficiency of the enzyme so that V
4944:
4664:
3584:
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
1005:
9725:
9515:
9434:
8502:
Murzin AG (November 1993). "Can homologous proteins evolve different enzymatic activities?".
7466:"Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling"
5020:
Johnson LN, Petsko GA (July 1999). "David
Phillips and the origin of structural enzymology".
4685:
3723:
3661:
3643:
3639:
3494:
3434:
3214:
2749:
2307:
1895:
1742:
1462:
Enzyme changes shape by induced fit upon substrate binding to form enzyme-substrate complex.
1323:
1094:
1048:
709:
617:
552:
456:
310:
288:
231:
9088:
Begley CG, Paragina S, Sporn A (March 1990). "An analysis of contact lens enzyme cleaners".
3312:
can be coupled to ATP hydrolysis, driving the overall series of linked metabolic reactions.
2275:
reaction (ES). Finally the enzyme-product complex (EP) dissociates to release the products.
2023:
catalyzes its reaction in either direction depending on the concentration of its reactants:
9587:
9373:
8711:
8655:
8435:
8152:
7132:
6940:
6618:
6390:
6186:
6106:
5966:
5839:
5569:
5205:
4978:
4564:
4240:
3873:
3482:
3481:
Enzymes can be compartmentalized, with different metabolic pathways occurring in different
2916:
2912:
2481:
2465:
2372:
2361:
2013:
1954:
1837:
1777:
1504:
1389:
1025:
1024:
in 1937. The conclusion that pure proteins can be enzymes was definitively demonstrated by
805:
774:
537:
376:
356:
8935:
8918:
7664:
7647:
5694:
4707:
Manchester KL (December 1995). "Louis
Pasteur (1822–1895)--chance and the prepared mind".
4506:
Schomburg I, Chang A, Placzek S, Söhngen C, Rother M, Lang M, et al. (January 2013).
8:
9735:
9551:
5090:
4823:
4457:
Murphy JM, Zhang Q, Young SN, Reese ML, Bailey FP, Eyers PA, et al. (January 2014).
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3696:
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2353:
2311:
1636:
1300:
899:
713:
592:
515:
391:
166:
19:"Biocatalyst" redirects here. For the use of natural catalysts in organic chemistry, see
8715:
8659:
8439:
8156:
8102:
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".
8459:
8426:
Cleaver JE (May 1968). "Defective repair replication of DNA in xeroderma pigmentosum".
8403:
8378:
8354:
8327:
8176:
8038:
8013:
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Changeux JP, Edelstein SJ (June 2005). "Allosteric mechanisms of signal transduction".
6358:
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2020:
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that digests the coating of some bacteria; the structure was solved by a group led by
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8125:
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8043:
7994:
7943:
7920:
7873:
7868:
Skett P, Gibson GG (2001). "Chapter 3: Induction and
Inhibition of Drug Metabolism".
7850:
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7487:
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6994:
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5373:
5332:
5289:
5262:
5221:
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5125:
5037:
4994:
4926:
4784:
4724:
4623:
4580:
4537:
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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:
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7118:
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7054:
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6905:
6870:
6833:
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6784:
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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:
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5403:
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3333:
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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:
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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:. Retrieved
6438:the original
6427:
6386:
6382:
6376:
6341:
6337:
6327:
6294:
6290:
6284:
6241:
6237:
6227:
6182:
6178:
6168:
6149:
6143:
6102:
6098:
6092:
6073:
6067:
6042:
6038:
6032:
6013:
6007:
5962:
5958:
5948:
5921:
5915:
5890:
5886:
5880:
5835:
5831:
5821:
5800:
5788:
5780:
5766:
5762:
5752:
5725:
5721:
5711:
5686:
5682:
5676:
5651:
5647:
5641:
5616:
5612:
5606:
5565:
5561:
5555:
5522:
5518:
5512:
5487:
5483:
5477:
5458:
5448:
5429:
5408:. Retrieved
5404:the original
5394:
5359:
5355:
5345:
5318:
5314:
5304:
5285:
5275:
5248:
5244:
5234:
5201:
5197:
5191:
5154:
5150:
5140:
5113:
5107:
5095:. Retrieved
5091:the original
5086:
5083:"EC 2.7.1.1"
5076:
5064:. Retrieved
5060:
5050:
5025:
5021:
5015:
4974:
4970:
4964:
4952:. Retrieved
4948:
4939:
4912:
4908:
4888:
4882:
4872:
4867:
4851:
4839:. Retrieved
4834:
4825:
4813:. 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
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191::
23:.
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