360:
31:
1110:
515:. It is necessary to break down proteins into small peptides (tripeptides and dipeptides) and amino acids so they can be absorbed by the intestines, and the absorbed tripeptides and dipeptides are also further broken into amino acids intracellularly before they enter the bloodstream. Different enzymes have different specificity for their substrate; trypsin, for example, cleaves the peptide bond after a positively charged residue (
390:
The ubiquitin-mediated process is selective. Proteins marked for degradation are covalently linked to ubiquitin. Many molecules of ubiquitin may be linked in tandem to a protein destined for degradation. The polyubiquinated protein is targeted to an ATP-dependent protease complex, the proteasome. The
293:
Proteases in particular are synthesized in the inactive form so that they may be safely stored in cells, and ready for release in sufficient quantity when required. This is to ensure that the protease is activated only in the correct location or context, as inappropriate activation of these proteases
807:
Protein backbones are very stable in water at neutral pH and room temperature, although the rate of hydrolysis of different peptide bonds can vary. The half life of a peptide bond under normal conditions can range from 7 years to 350 years, even higher for peptides protected by modified terminus or
399:
Different proteins are degraded at different rates. Abnormal proteins are quickly degraded, whereas the rate of degradation of normal proteins may vary widely depending on their functions. Enzymes at important metabolic control points may be degraded much faster than those enzymes whose activity is
607:
Some enzymes at important metabolic control points such as ornithine decarboxylase is regulated entirely by its rate of synthesis and its rate of degradation. Other rapidly degraded proteins include the protein products of proto-oncogenes, which play central roles in the regulation of cell growth.
350:
Proteins in cells are broken into amino acids. This intracellular degradation of protein serves multiple functions: It removes damaged and abnormal proteins and prevents their accumulation. It also serves to regulate cellular processes by removing enzymes and regulatory proteins that are no longer
92:
break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes including
459:, and methionine, the absence of stabilizing ligands, the presence of attached carbohydrate or phosphate groups, the presence of free α-amino group, the negative charge of protein, and the flexibility and stability of the protein. Proteins with larger degrees of
140:
is first synthesized as preproalbumin and contains an uncleaved signal peptide. This forms the proalbumin after the signal peptide is cleaved, and a further processing to remove the N-terminal 6-residue propeptide yields the mature form of the protein.
599:
Proteolysis is also involved in the regulation of many cellular processes by activating or deactivating enzymes, transcription factors, and receptors, for example in the biosynthesis of cholesterol, or the mediation of thrombin signalling through
869:
Like other biomolecules, proteins can also be broken down by high heat alone. At 250 °C, the peptide bond may be easily hydrolyzed, with its half-life dropping to about a minute. Protein may also be broken down without hydrolysis through
383:-lysosomal pathway is normally a non-selective process, but it may become selective upon starvation whereby proteins with peptide sequence KFERQ or similar are selectively broken down. The lysosome contains a large number of proteases such as
708:
YscU protein, as well as cleavage of the Gly-Ser bond in a subset of sea urchin sperm protein, enterokinase, and agrin (SEA) domains. In some cases, the autoproteolytic cleavage is promoted by conformational strain of the peptide bond.
341:. Microbial degradation of protein in the environment can be regulated by nutrient availability. For example, limitation for major elements in proteins (carbon, nitrogen, and sulfur) induces proteolytic activity in the fungus
195:
Some proteins and most eukaryotic polypeptide hormones are synthesized as a large precursor polypeptide known as a polyprotein that requires proteolytic cleavage into individual smaller polypeptide chains. The polyprotein
2418:
Ramesh K. Sharmaa; W.Geoffrey Chana; Jeffrey I. Seemanb; Mohammad R. Hajaligola (January 2003). "Formation of low molecular weight heterocycles and polycyclic aromatic compounds (PACs) in the pyrolysis of α-amino acids".
808:
within the protein interior. The rate of hydrolysis however can be significantly increased by extremes of pH and heat. Spontaneous cleavage of proteins may also involve catalysis by zinc on serine and threonine.
1072:, can also cause proteolysis. These venoms are, in fact, complex digestive fluids that begin their work outside of the body. Proteolytic venoms cause a wide range of toxic effects, including effects that are:
470:
The rate of proteolysis may also depend on the physiological state of the organism, such as its hormonal state as well as nutritional status. In time of starvation, the rate of protein degradation increases.
289:
occurs in the single-chain proinsulin form which facilitates formation of the ultimate inter-peptide disulfide bonds, and the ultimate intra-peptide disulfide bond, found in the native structure of insulin.
2855:
is an open access journal that provides an international forum for the electronic publication of the whole spectrum of high-quality articles and reviews in all areas of proteolysis and proteolytic pathways.
200:(POMC) contains many polypeptide hormones. The cleavage pattern of POMC, however, may vary between different tissues, yielding different sets of polypeptide hormones from the same polyprotein.
686:, these autoproteolytic proteins participate in a "single turnover" reaction and do not catalyze further reactions post-cleavage. Examples include cleavage of the Asp-Pro bond in a subset of
329:
whereby proteolytic cleavage breaks proteins into smaller peptides and amino acids so that they may be absorbed and used. In animals the food may be processed extracellularly in specialized
733:
may involve the release of lysosomal enzymes into extracellular space that break down surrounding tissues. Abnormal proteolysis may result in many age-related neurological diseases such as
834:
Certain chemicals cause proteolysis only after specific residues, and these can be used to selectively break down a protein into smaller polypeptides for laboratory analysis. For example,
2489:
White JL, Conner BT, Perfetti TA, Bombick BR, Avalos JT, Fowler KW, Smith CJ, Doolittle DJ (May 2001). "Effect of pyrolysis temperature on the mutagenicity of tobacco smoke condensate".
1452:
van der Lee, Robin; Lang, Benjamin; Kruse, Kai; Gsponer, Jörg; Sánchez de Groot, Natalia; Huynen, Martijn A.; Matouschek, Andreas; Fuxreiter, Monika; Babu, M. Madan (25 September 2014).
100:
Proteolysis can also be used as an analytical tool for studying proteins in the laboratory, and it may also be used in industry, for example in food processing and stain removal.
1256:
Hanson, M.A., Marzluf, G.A., 1975. Control of the synthesis of a single enzyme by multiple regulatory circuits in
Neurospora crassa. Proc. Natl. Acad. Sci. U.S.A. 72, 1240–1244.
1973:
Johansson, Denny G. A.; Macao, Bertil; Sandberg, Anders; Härd, Torleif (2008-04-04). "SEA domain autoproteolysis accelerated by conformational strain: mechanistic aspects".
578:. The trypsin, once activated, can also cleave other trypsinogens as well as the precursors of other proteases such as chymotrypsin and carboxypeptidase to activate them.
2175:
Radzicka, Anna; Wolfenden, Richard (January 1996). "Rates of
Uncatalyzed Peptide Bond Hydrolysis in Neutral Solution and the Transition State Affinities of Proteases".
780:, thereby resulting in the breaking down of connective tissues in the lung. Other proteases and their inhibitors may also be involved in this disease, for example
97:, as well as preventing the accumulation of unwanted or misfolded proteins in cells. Consequently, abnormality in the regulation of proteolysis can cause disease.
3526:
3869:
4125:
2932:
819:). The standard way to hydrolyze a protein or peptide into its constituent amino acids for analysis is to heat it to 105 °C for around 24 hours in 6M
2804:
1752:"Processing, localization and binding activity of zonadhesin suggest a function in sperm adhesion to the zona pellucida during exocytosis of the acrosome"
3588:
2885:
325:
Protein degradation may take place intracellularly or extracellularly. In digestion of food, digestive enzymes may be released into the environment for
1344:
Tompa, P.; Prilusky, J.; Silman, I.; Sussman, J. L. (2008-05-01). "Structural disorder serves as a weak signal for intracellular protein degradation".
538:
In order to prevent inappropriate or premature activation of the digestive enzymes (they may, for example, trigger pancreatic self-digestion causing
2017:
463:
also tend to have short cellular half-life, with disordered segments having been proposed to facilitate efficient initiation of degradation by the
132:, and/or the conversion of an inactive or non-functional protein to an active one. The precursor to the final functional form of protein is termed
3004:
2544:"Stimulation of Proteinase K action by denaturing agents: application to the isolation of nucleic acids and the degradation of 'masked' proteins"
2134:
309:
whereby an initial event triggers a cascade of sequential proteolytic activation of many specific proteases, resulting in blood coagulation. The
591:, is produced as preprosubtilisin, and is released only if the signal peptide is cleaved and autocatalytic proteolytic activation has occurred.
305:
Proteolysis can, therefore, be a method of regulating biological processes by turning inactive proteins into active ones. A good example is the
3353:
3934:
3343:
729:
may have increased lysosomal activity and the degradation of some proteins can increase significantly. Chronic inflammatory diseases such as
2801:
1200:"Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid"
2585:"Selective Elimination of the Exonuclease Activity of the Deoxyribonucleic Acid Polymerase from Escherichia coli B by Limited Proteolysis"
302:, a slight rearrangement of the protein structure that completes the active site of the protease occurs, thereby activating the protein.
281:
after the signal peptide has been cleaved. The proinsulin is then cleaved at two positions to yield two polypeptide chains linked by two
3964:
159:, fMet is efficiently removed if the second residue is small and uncharged, but not if the second residue is bulky and charged. In both
3916:
4446:
2446:
Fabbri D, Adamiano A, Torri C (2010). "GC-MS determination of polycyclic aromatic hydrocarbons evolved from pyrolysis of biomass".
654:. The precursors of caspase, procaspase, may be activated by proteolysis through its association with a protein complex that forms
4041:
2878:
972:
785:
183:
that directs the protein to its final destination. This signal peptide is removed by proteolysis after their transport through a
1915:"Autoproteolysis of YscU of Yersinia pseudotuberculosis Is Important for Regulation of Expression and Secretion of Yop Proteins"
3762:
3749:
748:, and imbalance between proteases and antiproteases can result in diseases, for example, in the destruction of lung tissues in
2836:
2351:
2296:
2213:
2107:
Abboud RT1, Vimalanathan S (2008). "Pathogenesis of COPD. Part I. The role of protease-antiprotease imbalance in emphysema".
1328:
1297:
1182:
3834:
2375:
White RH (1984). "Hydrolytic stability of biomolecules at high temperatures and its implication for life at 250 degrees C".
211:
mRNA. This polypeptide is subsequently cleaved into individual polypeptide chains. Common names for the polyprotein include
17:
2524:
317:
also involves a complex sequential proteolytic activation and interaction that result in an attack on invading pathogens.
4093:
3723:
1809:"Single-step affinity purification of recombinant proteins using a self-excising module from Neisseria meningitidis FrpC"
447:) have short half-life. Other factors suspected to affect degradation rate include the rate deamination of glutamine and
1703:"An autocatalytic cleavage in the C terminus of the human MUC2 mucin occurs at the low pH of the late secretory pathway"
1265:
Sims, G. K., and M. M. Wander. 2002. Proteolytic activity under nitrogen or sulfur limitation. Appl. Soil Ecol. 568:1-5.
2871:
2072:
De
Strooper B. (2010). "Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process".
907:
4167:
460:
4078:
1858:"Domain Structure of Salmonella FlhB, a Flagellar Export Component Responsible for Substrate Specificity Switching"
1560:"The SREBP Pathway: Regulation of Cholesterol Metabolism by Proteolysis of a Membrane-Bound Transcription Factor"
879:
2863:
294:
can be very destructive for an organism. Proteolysis of the zymogen yields an active protein; for example, when
2898:
663:
4323:
4009:
3924:
1807:
Sadilkova, Lenka; Osicka, Radim; Sulc, Miroslav; Linhartova, Irena; Novak, Petr; Sebo, Peter (October 2008).
3942:
3548:
745:
721:, leakage of proteases and their premature activation in the pancreas results in the self-digestion of the
2858:
2417:
601:
2048:
2018:"Ubiquitin-dependent proteolysis: its role in human diseases and the design of therapeutic strategies"
929:
Complete inactivation of undesirable enzymatic activity or removal of unwanted proteins. For example,
4424:
4411:
4398:
4385:
4372:
4359:
4346:
4308:
2999:
2894:
43:
952:
Partial inactivation, or changing the functionality, of specific protein. For example, treatment of
550:, is secreted by the stomach, and is activated only in the acidic environment found in stomach. The
4318:
4272:
4215:
3904:
3740:
2335:
1057:
781:
363:
Structure of a proteasome. Its active sites are inside the tube (blue) where proteins are degraded.
1000:
Production of digested protein used in growth media to culture bacteria and other organisms, e.g.
400:
largely constant under all physiological conditions. One of the most rapidly degraded proteins is
4220:
4083:
4073:
3899:
3800:
3790:
3716:
3642:
679:
623:
involved in cell division. The degradation of cyclins is the key step that governs the exit from
401:
326:
1289:
1283:
207:
also produce their proteins initially as a single polypeptide chain that were translated from a
3887:
3775:
1174:
1168:
938:
692:
306:
216:
179:
Proteins that are to be targeted to a particular organelle or for secretion have an N-terminal
2288:
2282:
2203:
4241:
4160:
3894:
3795:
3441:
2128:
1454:"Intrinsically Disordered Segments Affect Protein Half-Life in the Cell and during Evolution"
1320:
1314:
1128:
875:
687:
651:
167:, the exposed N-terminal residue may determine the half-life of the protein according to the
114:
2327:
1750:
Bi, Ming; Hickox, John R; Winfrey, Virginia P; Olson, Gary E; Hardy, Daniel M (2003-10-15).
4313:
4068:
3877:
2917:
2714:
2655:
2596:
1659:
1211:
911:
859:
730:
631:. Cyclins accumulate in the course the cell cycle, then abruptly disappear just before the
238:
197:
118:
2644:"Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp"
1650:
Glotzer M, Murray AW, Kirschner MW (1991). "Cyclin is degraded by the ubiquitin pathway".
1023:
Proteases may be classified according to the catalytic group involved in its active site.
8:
4451:
4277:
4027:
3989:
3973:
2762:"New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases"
2328:
1123:
984:
773:
535:); elastase cleaves the bond after a small non-polar residue such as alanine or glycine.
2718:
2659:
2642:
Minde DP; Maurice, Madelon M.; RĂĽdiger, Stefan G. D. (2012). Uversky, Vladimir N (ed.).
2600:
1663:
1215:
581:
In bacteria, a similar strategy of employing an inactive zymogen or prezymogen is used.
4210:
4063:
4004:
3994:
3984:
3709:
3247:
3097:
2826:
2737:
2702:
2678:
2643:
2560:
2543:
2471:
2400:
2357:
2255:
2230:
2148:
Daniel. Kahne; W. Clark Still (1988). "Hydrolysis of a peptide bond in neutral water".
1947:
1914:
1833:
1808:
1784:
1751:
1683:
1632:
1589:
1535:
1510:
1486:
1453:
1429:
1396:
1377:
1279:
1037:
792:
427:
may partially determine the half-life of a protein, and proteins with segments rich in
2619:
2584:
2502:
2432:
2036:
1890:
1857:
1576:
1559:
1234:
1199:
823:. However, some proteins are resistant to acid hydrolysis. One well-known example is
285:. Removal of two C-terminal residues from the B-chain then yields the mature insulin.
4058:
3951:
3201:
3087:
3046:
2832:
2783:
2742:
2683:
2624:
2565:
2506:
2463:
2392:
2347:
2292:
2260:
2209:
2116:
2089:
2040:
1998:
1990:
1952:
1934:
1895:
1877:
1873:
1838:
1789:
1771:
1732:
1724:
1687:
1675:
1624:
1581:
1540:
1491:
1473:
1434:
1416:
1369:
1361:
1324:
1293:
1239:
1178:
1047:
1042:
1027:
988:
820:
726:
587:
484:
343:
310:
234:
89:
2475:
1593:
1381:
367:
The intracellular degradation of protein may be achieved in two ways—proteolysis in
4256:
4251:
4225:
4153:
4108:
4103:
3979:
3504:
3482:
3381:
3300:
3191:
3168:
3092:
3064:
2773:
2732:
2722:
2673:
2663:
2614:
2604:
2555:
2498:
2455:
2428:
2404:
2384:
2361:
2339:
2250:
2242:
2184:
2157:
2081:
2032:
1982:
1942:
1926:
1885:
1869:
1828:
1820:
1779:
1763:
1714:
1667:
1636:
1616:
1571:
1530:
1522:
1481:
1465:
1424:
1408:
1353:
1229:
1219:
1139:
976:
953:
835:
504:
155:
1913:
Björnfot, Ann-Catrin; Lavander, Moa; Forsberg, Åke; Wolf-Watz, Hans (2009-07-01).
1607:
Shaun R. Coughlin (2000). "Thrombin signalling and protease-activated receptors".
737:'s due to generation and ineffective removal of peptides that aggregate in cells.
635:
of mitosis. The cyclins are removed via a ubiquitin-mediated proteolytic pathway.
4456:
4303:
4287:
4200:
4113:
4098:
4053:
3615:
3315:
3206:
3082:
3041:
2893:
2808:
2727:
2703:"In situ proteolysis to generate crystals for structure determination: An update"
2668:
2231:"Spontaneous cleavage of proteins at serine and threonine is facilitated by zinc"
1469:
1052:
1032:
961:
816:
330:
314:
286:
282:
204:
3701:
2312:
136:, and these proproteins may be first synthesized as preproprotein. For example,
4341:
4282:
4134:
3770:
3477:
3371:
3348:
3290:
3140:
3122:
3009:
2975:
2085:
1115:
1005:
899:
824:
508:
180:
129:
2459:
1986:
1412:
795:, degenerative skin disorders, respiratory and gastrointestinal diseases, and
4440:
4246:
4205:
4045:
3847:
3496:
3423:
3399:
3338:
3333:
3285:
3280:
3229:
3186:
3107:
3051:
2955:
1994:
1938:
1881:
1775:
1728:
1477:
1420:
1365:
942:
828:
812:
524:
444:
432:
334:
274:
257:
Many proteins and hormones are synthesized in the form of their precursors -
208:
184:
1701:
Lidell, Martin E.; Johansson, Malin E. V.; Hansson, Gunnar C. (2003-04-18).
1224:
994:
Analysis of the stability of folded domain under a wide range of conditions.
914:
may be removed. The proteases used have high degree of specificity, such as
831:
so that other proteins become degraded while ribonuclease A is left intact.
4195:
3753:
3295:
3112:
2927:
2912:
2787:
2746:
2687:
2510:
2467:
2264:
2120:
2093:
2044:
2002:
1956:
1899:
1842:
1793:
1736:
1719:
1702:
1628:
1495:
1438:
1373:
930:
923:
919:
741:
718:
675:
567:
559:
539:
496:
338:
70:
2628:
2609:
2569:
2396:
1824:
1679:
1585:
1544:
1243:
964:, which retains its polymerase function but lacks 5'-exonuclease activity.
764:
in the lung which release excessive amount of proteolytic enzymes such as
391:
ubiquitin is released and reused, while the targeted protein is degraded.
4419:
4354:
4190:
3999:
3946:
3882:
3842:
3417:
3376:
3305:
3270:
3265:
3224:
3196:
3163:
3145:
3117:
2970:
2960:
2950:
2228:
1526:
903:
863:
761:
757:
563:
512:
417:
413:
295:
230:
160:
62:
58:
2778:
2761:
2161:
1930:
404:, which has a half-life of 11 minutes. In contrast, other proteins like
359:
3657:
3563:
3540:
3536:
3492:
3456:
3433:
3216:
3020:
2986:
2942:
2343:
2246:
1767:
1357:
1134:
1094:
968:
957:
883:
843:
839:
796:
698:
659:
655:
628:
582:
547:
532:
464:
448:
424:
384:
376:
278:
266:
220:
168:
164:
133:
125:
122:
66:
35:
2188:
73:
is extremely slow, taking hundreds of years. Proteolysis is typically
4393:
4367:
3732:
3686:
3599:
3409:
3328:
3275:
3239:
3178:
3155:
3102:
3033:
2965:
2388:
1671:
1620:
1197:
1144:
1082:
1076:
871:
855:
851:
749:
734:
647:
480:
456:
440:
380:
372:
262:
94:
74:
542:), these enzymes are secreted as inactive zymogen. The precursor of
269:. These proteins are cleaved to form their final active structures.
46:
of water (blue). The uncatalysed half-life is several hundred years.
30:
3736:
3674:
3670:
3666:
3603:
3576:
3518:
3469:
3465:
3363:
3310:
3132:
3074:
3056:
2326:
Bryan John Smith (2002). "Chapter 71-75". In John M. Walker (ed.).
1557:
1109:
1088:
1018:
1001:
980:
946:
915:
894:
Proteolysis is also used in research and diagnostic applications:
847:
765:
722:
717:
Abnormal proteolytic activity is associated with many diseases. In
704:
632:
575:
551:
528:
516:
500:
368:
82:
882:
may also form, which is of interest in the study of generation of
483:, proteins in food are broken down into smaller peptide chains by
351:
needed. The amino acids may then be reused for protein synthesis.
3634:
3626:
3607:
3580:
3391:
1912:
753:
683:
643:
624:
616:
555:
492:
452:
428:
299:
270:
258:
137:
54:
39:
3665:
1198:
P H Hirel; M J Schmitter; P Dessen; G Fayat; S Blanquet (1989).
153:) may be removed during translation of the nascent protein. For
121:
often occurs for many proteins. This may involve removal of the
4406:
4176:
3822:
3815:
3810:
3678:
3630:
3572:
3514:
3257:
3029:
2525:"Chemicals in Meat Cooked at High Temperatures and Cancer Risk"
769:
620:
571:
543:
520:
488:
436:
409:
225:
78:
2852:
27:
Breakdown of proteins into smaller polypeptides or amino acids
4380:
3857:
3852:
3785:
3780:
3323:
2994:
2201:
1806:
1131:
a proteomic technology for identifying proteolytic substrates
1069:
696:
FrpC self-processing domain, cleavage of the Asn-Pro bond in
405:
2229:
Brian Lyons; Ann H. Kwan; Roger J.W. Truscott (April 2016).
827:, which can be purified by treating crude extracts with hot
523:); chymotrypsin cleaves the bond after an aromatic residue (
394:
108:
88:
Proteolysis in organisms serves many purposes; for example,
2802:
Research on
Biological Roles and Variation of Snake Venoms.
2147:
1451:
1068:
Certain types of venom, such as those produced by venomous
934:
150:
4145:
2488:
2106:
1972:
1343:
674:
Autoproteolysis takes place in some proteins, whereby the
554:
secretes the precursors of a number of proteases such as
3616:
4-(p-hydroxybenzylidene)-5-imidazolinone (HBI) formation
412:
have a half-life of a month or more, while, in essence,
337:, but in many bacteria the food may be internalized via
949:
contaminants that may otherwise degrade the DNA or RNA.
878:
may start to form upon degradation. Above 500 °C,
241:, leading to two different lengths of peptidic chains (
2641:
2109:
International
Journal of Tuberculosis and Lung Disease
1968:
1966:
1700:
1649:
815:
can readily hydrolyse the peptide bonds in a protein (
791:
Other diseases linked to aberrant proteolysis include
2701:
Wernimont, A; Edwards, A (2009). Song, Haiwei (ed.).
842:. Similar methods may be used to specifically cleave
375:-dependent process that targets unwanted proteins to
113:
Limited proteolysis of a polypeptide during or after
2015:
1749:
1397:"Paradigms of protein degradation by the proteasome"
1105:
926:, so that only the targeted sequence may be cleaved.
2859:
2541:
2445:
1963:
997:
Increasing success rate of crystallisation projects
144:
85:, but may also occur by intra-molecular digestion.
3589:p-Hydroxybenzylidene-imidazolinone (HBI) formation
2824:
2280:
1558:Michael S. Brown; Joseph L. Goldstein (May 1997).
1395:Inobe, Tomonao; Matouschek, Andreas (2014-02-01).
1288:(2nd ed.). W H Freeman and Company. pp.
1277:
1173:(2nd ed.). W H Freeman and Company. pp.
1166:
566:, which is activated by a very specific protease,
503:, and into amino acids by various enzymes such as
237:in the mRNA that codes for the polypeptide causes
3731:
2287:(2nd ed.). W H Freeman and Company. p.
2174:
1856:Minamino, Tohru; Macnab, Robert M. (2000-09-01).
1606:
252:
174:
4438:
2700:
2582:
2325:
1319:(2nd ed.). John Wiley & Sons. pp.
646:are an important group of proteases involved in
149:The initiating methionine (and, in prokaryotes,
2202:Bernard Testa; Joachim M. Mayer (1 July 2003).
1394:
1312:
768:, such that they can no longer be inhibited by
2071:
1855:
4161:
3717:
2879:
2828:Proteins: Structures and Molecular Properties
2284:Proteins: Structures and Molecular Properties
2276:
2274:
1285:Proteins: Structures and Molecular Properties
1273:
1271:
1170:Proteins: Structures and Molecular Properties
3549:Tryptophan tryptophylquinone (TTQ) formation
1511:"Progress report. Peptide absorption in man"
756:tobacco. Smoking is thought to increase the
347:as well as in of soil organism communities.
233:. The latter name refers to the fact that a
2421:Journal of Analytical and Applied Pyrolysis
2133:: CS1 maint: numeric names: authors list (
1162:
1160:
886:in tobacco smoke and cooking at high heat.
712:
190:
4168:
4154:
3724:
3710:
2886:
2872:
2271:
1268:
889:
802:
354:
2831:(2nd ed.). W H Freeman and Company.
2777:
2759:
2736:
2726:
2677:
2667:
2618:
2608:
2559:
2254:
2205:Hydrolysis in Drug and Prodrug Metabolism
1946:
1889:
1832:
1783:
1718:
1575:
1534:
1485:
1428:
1233:
1223:
395:Rate of intracellular protein degradation
109:Post-translational proteolytic processing
2374:
2177:Journal of the American Chemical Society
1157:
933:, a broad-spectrum proteinase stable in
611:
358:
29:
3643:Methylidene-imidazolone (MIO) formation
1508:
973:liquid chromatography-mass spectrometry
786:tissue inhibitors of metalloproteinases
103:
14:
4439:
2542:Hilz H, Wiegers U, Adamietz P (1975).
967:Digestion of proteins in solution for
941:, is often used in the preparation of
619:are a group of proteins that activate
594:
320:
4149:
3705:
3527:Lysine tyrosylquinone (LTQ) formation
2867:
2334:(2 ed.). Humana Press. pp.
1401:Current Opinion in Structural Biology
416:lasts for the entire life-time of an
4094:Amyloid precursor protein secretase
3000:Glycosyl phosphatidylinositol (GPI)
1707:The Journal of Biological Chemistry
1012:
249:) at an approximately fixed ratio.
24:
2818:
2561:10.1111/j.1432-1033.1975.tb02211.x
975:(LC-MS). This may also be done by
669:
25:
4468:
3311:Oxidative deamination to aldehyde
2846:
2025:Molecular Genetics and Metabolism
838:cleaves the peptide bond after a
273:, for example, is synthesized as
4079:Proteasome endopeptidase complex
2548:European Journal of Biochemistry
1874:10.1128/JB.182.17.4906-4914.2000
1108:
880:polycyclic aromatic hydrocarbons
145:Removal of N-terminal methionine
4447:Post-translational modification
2899:posttranslational modifications
2794:
2753:
2694:
2635:
2583:Klenow H, Henningsen I (1970).
2576:
2535:
2517:
2482:
2439:
2411:
2368:
2319:
2305:
2222:
2208:. Wiley VCH. pp. 270–288.
2195:
2168:
2141:
2100:
2065:
2009:
1906:
1849:
1800:
1743:
1694:
1643:
1600:
1551:
1502:
902:so that the fusion partner and
678:is cleaved in a self-catalyzed
2330:The Protein Protocols Handbook
1445:
1388:
1337:
1306:
1259:
1250:
1191:
740:Proteases may be regulated by
253:Cleavage of precursor proteins
175:Removal of the signal sequence
13:
1:
3943:Serine type carboxypeptidases
3925:Angiotensin-converting enzyme
2503:10.1016/s0278-6915(00)00155-1
2433:10.1016/S0165-2370(02)00108-0
2037:10.1016/S1096-7192(02)00146-4
2016:Kathleen M. Sakamoto (2002).
1577:10.1016/S0092-8674(00)80213-5
1150:
858:peptide bonds. Acids such as
2728:10.1371/journal.pone.0005094
2669:10.1371/journal.pone.0046147
1975:Journal of Molecular Biology
1470:10.1016/j.celrep.2014.07.055
638:
602:protease-activated receptors
562:. The zymogen of trypsin is
474:
7:
4175:
3118:Topaquinone (TPQ) formation
2825:Thomas E Creighton (1993).
2281:Thomas E Creighton (1993).
1278:Thomas E Creighton (1993).
1167:Thomas E Creighton (1993).
1101:
627:and progress into the next
10:
4473:
2853:The Journal of Proteolysis
2589:Proc. Natl. Acad. Sci. USA
2086:10.1152/physrev.00023.2009
1280:"Chapter 10 - Degradation"
1016:
987:for the identification by
866:may be used for cleavage.
4332:
4324:Michaelis–Menten kinetics
4296:
4265:
4234:
4183:
4124:
4040:
4020:
3963:
3933:
3915:
3868:
3833:
3761:
3748:
3655:
3625:
3598:
3571:
3562:Crosslinks between three
3561:
3535:
3513:
3491:
3464:
3454:
3432:
3408:
3390:
3362:
3256:
3238:
3215:
3177:
3154:
3131:
3073:
3028:
3018:
2985:
2941:
2905:
2895:Protein primary structure
2529:National Cancer Institute
2460:10.1007/s00216-010-3563-5
1987:10.1016/j.jmb.2008.01.050
1413:10.1016/j.sbi.2014.02.002
1063:
782:matrix metalloproteinases
690:type D (VWD) domains and
4216:Diffusion-limited enzyme
3905:Tripeptidyl peptidase II
3656:Crosslinks between four
1313:Voet & Voet (1995).
1204:Proc Natl Acad Sci U S A
1058:Asparagine peptide lyase
713:Proteolysis and diseases
191:Cleavage of polyproteins
4074:Threonine endopeptidase
3900:Tripeptidyl peptidase I
3455:Crosslinks between two
2766:Journal of Biochemistry
1919:Journal of Bacteriology
1862:Journal of Bacteriology
1225:10.1073/pnas.86.21.8247
890:Laboratory applications
803:Non-enzymatic processes
680:intramolecular reaction
585:, which is produced by
402:ornithine decarboxylase
355:Lysosome and proteasome
327:extracellular digestion
239:ribosomal frameshifting
4064:Aspartic acid protease
3888:Dipeptidyl peptidase-4
3103:Porphyrin ring linkage
2811:Loma Linda University.
1720:10.1074/jbc.M210069200
876:heterocyclic compounds
693:Neisseria meningitidis
364:
307:blood clotting cascade
217:group-specific antigen
47:
4309:Eadie–Hofstee diagram
4242:Allosteric regulation
3895:Tripeptidyl peptidase
3164:Succinimide formation
2610:10.1073/pnas.65.1.168
2074:Physiological Reviews
1825:10.1110/ps.035733.108
688:von Willebrand factor
652:programmed cell death
612:Cell cycle regulation
362:
33:
4319:Lineweaver–Burk plot
4069:Metalloendopeptidase
3974:Metalloexopeptidases
3878:Dipeptidyl peptidase
2918:Protein biosynthesis
2315:. Protein Data Bank.
1527:10.1136/gut.15.6.494
983:after separation by
860:trifluoroacetic acid
731:rheumatoid arthritis
198:pro-opiomelanocortin
104:Biological functions
53:is the breakdown of
18:Proteolytic cleavage
4084:HslU—HslV peptidase
4028:Metalloexopeptidase
2719:2009PLoSO...4.5094W
2660:2012PLoSO...746147M
2601:1970PNAS...65..168K
2162:10.1021/ja00230a041
1931:10.1128/JB.01730-08
1756:Biochemical Journal
1713:(16): 13944–13951.
1664:1991Natur.349..132G
1216:1989PNAS...86.8247H
1124:The Proteolysis Map
1091:(muscle-destroying)
985:gel electrophoresis
945:to remove unwanted
746:protease inhibitors
595:Cellular regulation
321:Protein degradation
298:is cleaved to form
65:. Uncatalysed, the
44:nucleophilic attack
4278:Enzyme superfamily
4211:Enzyme promiscuity
3248:Transglutamination
2807:2019-09-15 at the
2760:Kohei Oda (2012).
2344:10.1385/1592591698
2247:10.1111/acel.12428
1768:10.1042/BJ20030753
1358:10.1002/prot.21773
1085:(blood-destroying)
1038:Threonine protease
908:protein expression
793:muscular dystrophy
570:, secreted by the
461:intrinsic disorder
365:
48:
4434:
4433:
4143:
4142:
4092:Other/ungrouped:
4059:Cysteine protease
4036:
4035:
3954:
3699:
3698:
3695:
3694:
3651:
3650:
3557:
3556:
3450:
3449:
3202:Polyglutamylation
3088:Dephosphorylation
3047:Dephosphorylation
2838:978-0-7167-2317-2
2779:10.1093/jb/mvr129
2491:Food Chem Toxicol
2448:Anal Bioanal Chem
2353:978-0-89603-940-7
2298:978-0-7167-2317-2
2215:978-3-906390-25-3
2189:10.1021/ja954077c
2183:(26): 6105–6109.
2156:(22): 7529–7534.
1925:(13): 4259–4267.
1868:(17): 4906–4914.
1819:(10): 1834–1843.
1762:(Pt 2): 477–488.
1615:(6801): 258–264.
1330:978-0-471-58651-7
1299:978-0-7167-2317-2
1184:978-0-7167-2317-2
1079:(cell-destroying)
1048:Glutamic protease
1043:Aspartic protease
1028:Cysteine protease
989:mass spectrometry
969:proteome analysis
821:hydrochloric acid
727:diabetes mellitus
588:Bacillus subtilis
485:digestive enzymes
451:and oxidation of
344:Neurospora crassa
311:complement system
235:slippery sequence
119:protein synthesis
90:digestive enzymes
16:(Redirected from
4464:
4314:Hanes–Woolf plot
4257:Enzyme activator
4252:Enzyme inhibitor
4226:Enzyme catalysis
4170:
4163:
4156:
4147:
4146:
4109:Beta-secretase 2
4104:Beta-secretase 1
3980:Carboxypeptidase
3976:
3952:
3759:
3758:
3726:
3719:
3712:
3703:
3702:
3663:
3662:
3569:
3568:
3505:Sulfilimine bond
3483:ADP-ribosylation
3462:
3461:
3382:ADP-ribosylation
3301:ADP-ribosylation
3192:ADP-ribosylation
3169:ADP-ribosylation
3093:ADP-ribosylation
3065:ADP-ribosylation
3026:
3025:
3019:Single specific
2888:
2881:
2874:
2865:
2864:
2842:
2812:
2800:Hayes WK. 2005.
2798:
2792:
2791:
2781:
2757:
2751:
2750:
2740:
2730:
2698:
2692:
2691:
2681:
2671:
2639:
2633:
2632:
2622:
2612:
2580:
2574:
2573:
2563:
2539:
2533:
2532:
2521:
2515:
2514:
2486:
2480:
2479:
2443:
2437:
2436:
2415:
2409:
2408:
2389:10.1038/310430a0
2372:
2366:
2365:
2333:
2323:
2317:
2316:
2313:"Ribonuclease A"
2309:
2303:
2302:
2278:
2269:
2268:
2258:
2226:
2220:
2219:
2199:
2193:
2192:
2172:
2166:
2165:
2150:J. Am. Chem. Soc
2145:
2139:
2138:
2132:
2124:
2104:
2098:
2097:
2069:
2063:
2062:
2060:
2059:
2053:
2047:. Archived from
2022:
2013:
2007:
2006:
1981:(4): 1130–1143.
1970:
1961:
1960:
1950:
1910:
1904:
1903:
1893:
1853:
1847:
1846:
1836:
1804:
1798:
1797:
1787:
1747:
1741:
1740:
1722:
1698:
1692:
1691:
1672:10.1038/349132a0
1647:
1641:
1640:
1621:10.1038/35025229
1604:
1598:
1597:
1579:
1555:
1549:
1548:
1538:
1509:Silk DB (1974).
1506:
1500:
1499:
1489:
1464:(6): 1832–1844.
1449:
1443:
1442:
1432:
1392:
1386:
1385:
1341:
1335:
1334:
1310:
1304:
1303:
1275:
1266:
1263:
1257:
1254:
1248:
1247:
1237:
1227:
1195:
1189:
1188:
1164:
1140:In-gel digestion
1118:
1113:
1112:
1013:Protease enzymes
977:in-gel digestion
954:DNA polymerase I
836:cyanogen bromide
505:carboxypeptidase
21:
4472:
4471:
4467:
4466:
4465:
4463:
4462:
4461:
4437:
4436:
4435:
4430:
4342:Oxidoreductases
4328:
4304:Enzyme kinetics
4292:
4288:List of enzymes
4261:
4230:
4201:Catalytic triad
4179:
4174:
4144:
4139:
4120:
4114:Gamma secretase
4099:Alpha secretase
4054:Serine protease
4032:
4021:Other/ungrouped
4016:
3972:
3959:
3955:-Transpeptidase
3929:
3911:
3864:
3829:
3744:
3730:
3700:
3691:
3647:
3621:
3594:
3553:
3531:
3509:
3487:
3446:
3442:C-mannosylation
3428:
3404:
3386:
3358:
3324:Imine formation
3252:
3234:
3211:
3207:Polyglycylation
3173:
3150:
3127:
3083:Phosphorylation
3069:
3042:Phosphorylation
3014:
2981:
2937:
2901:
2892:
2849:
2839:
2821:
2819:Further reading
2816:
2815:
2809:Wayback Machine
2799:
2795:
2758:
2754:
2699:
2695:
2640:
2636:
2581:
2577:
2540:
2536:
2531:. 2 April 2018.
2523:
2522:
2518:
2487:
2483:
2444:
2440:
2427:(1–2): 97–121.
2416:
2412:
2383:(5976): 430–2.
2373:
2369:
2354:
2324:
2320:
2311:
2310:
2306:
2299:
2279:
2272:
2227:
2223:
2216:
2200:
2196:
2173:
2169:
2146:
2142:
2126:
2125:
2105:
2101:
2070:
2066:
2057:
2055:
2051:
2020:
2014:
2010:
1971:
1964:
1911:
1907:
1854:
1850:
1813:Protein Science
1805:
1801:
1748:
1744:
1699:
1695:
1658:(6305): 132–8.
1648:
1644:
1605:
1601:
1556:
1552:
1507:
1503:
1450:
1446:
1393:
1389:
1342:
1338:
1331:
1311:
1307:
1300:
1276:
1269:
1264:
1260:
1255:
1251:
1210:(21): 8247–51.
1196:
1192:
1185:
1165:
1158:
1153:
1114:
1107:
1104:
1066:
1053:Metalloprotease
1033:Serine protease
1021:
1015:
962:Klenow fragment
892:
817:acid hydrolysis
805:
777:
715:
672:
670:Autoproteolysis
641:
614:
597:
477:
443:(the so-called
397:
357:
323:
315:immune response
287:Protein folding
283:disulfide bonds
277:, which yields
255:
193:
177:
147:
111:
106:
28:
23:
22:
15:
12:
11:
5:
4470:
4460:
4459:
4454:
4449:
4432:
4431:
4429:
4428:
4415:
4402:
4389:
4376:
4363:
4350:
4336:
4334:
4330:
4329:
4327:
4326:
4321:
4316:
4311:
4306:
4300:
4298:
4294:
4293:
4291:
4290:
4285:
4280:
4275:
4269:
4267:
4266:Classification
4263:
4262:
4260:
4259:
4254:
4249:
4244:
4238:
4236:
4232:
4231:
4229:
4228:
4223:
4218:
4213:
4208:
4203:
4198:
4193:
4187:
4185:
4181:
4180:
4173:
4172:
4165:
4158:
4150:
4141:
4140:
4138:
4137:
4135:Staphylokinase
4131:
4129:
4122:
4121:
4119:
4118:
4117:
4116:
4111:
4106:
4101:
4089:
4088:
4087:
4086:
4081:
4071:
4066:
4061:
4056:
4050:
4048:
4038:
4037:
4034:
4033:
4031:
4030:
4024:
4022:
4018:
4017:
4015:
4014:
4013:
4012:
4007:
4002:
3997:
3992:
3987:
3977:
3969:
3967:
3961:
3960:
3958:
3957:
3949:
3939:
3937:
3931:
3930:
3928:
3927:
3921:
3919:
3913:
3912:
3910:
3909:
3908:
3907:
3902:
3892:
3891:
3890:
3885:
3874:
3872:
3866:
3865:
3863:
3862:
3861:
3860:
3855:
3850:
3839:
3837:
3831:
3830:
3828:
3827:
3826:
3825:
3820:
3819:
3818:
3813:
3803:
3798:
3793:
3788:
3783:
3778:
3771:Aminopeptidase
3767:
3765:
3756:
3746:
3745:
3729:
3728:
3721:
3714:
3706:
3697:
3696:
3693:
3692:
3690:
3689:
3683:
3681:
3660:
3653:
3652:
3649:
3648:
3646:
3645:
3639:
3637:
3623:
3622:
3620:
3619:
3612:
3610:
3596:
3595:
3593:
3592:
3585:
3583:
3566:
3559:
3558:
3555:
3554:
3552:
3551:
3545:
3543:
3533:
3532:
3530:
3529:
3523:
3521:
3511:
3510:
3508:
3507:
3501:
3499:
3489:
3488:
3486:
3485:
3480:
3478:Disulfide bond
3474:
3472:
3459:
3452:
3451:
3448:
3447:
3445:
3444:
3438:
3436:
3430:
3429:
3427:
3426:
3421:
3414:
3412:
3406:
3405:
3403:
3402:
3396:
3394:
3388:
3387:
3385:
3384:
3379:
3374:
3372:Citrullination
3368:
3366:
3360:
3359:
3357:
3356:
3351:
3349:Propionylation
3346:
3341:
3336:
3331:
3326:
3321:
3319:-glycosylation
3313:
3308:
3303:
3298:
3293:
3291:Ubiquitination
3288:
3283:
3278:
3273:
3268:
3262:
3260:
3254:
3253:
3251:
3250:
3244:
3242:
3236:
3235:
3233:
3232:
3227:
3221:
3219:
3213:
3212:
3210:
3209:
3204:
3199:
3194:
3189:
3183:
3181:
3175:
3174:
3172:
3171:
3166:
3160:
3158:
3152:
3151:
3149:
3148:
3143:
3141:Palmitoylation
3137:
3135:
3129:
3128:
3126:
3125:
3123:Detyrosination
3120:
3115:
3113:Flavin linkage
3110:
3105:
3100:
3095:
3090:
3085:
3079:
3077:
3071:
3070:
3068:
3067:
3062:
3054:
3049:
3044:
3038:
3036:
3023:
3016:
3015:
3013:
3012:
3010:Detyrosination
3007:
3002:
2997:
2991:
2989:
2983:
2982:
2980:
2979:
2976:Myristoylation
2973:
2968:
2963:
2958:
2953:
2947:
2945:
2939:
2938:
2936:
2935:
2933:N–O acyl shift
2930:
2925:
2920:
2915:
2909:
2907:
2903:
2902:
2891:
2890:
2883:
2876:
2868:
2862:
2861:
2856:
2848:
2847:External links
2845:
2844:
2843:
2837:
2820:
2817:
2814:
2813:
2793:
2752:
2693:
2654:(10): e46147.
2634:
2595:(1): 168–175.
2575:
2554:(1): 103–108.
2534:
2516:
2497:(5): 499–505.
2481:
2438:
2410:
2367:
2352:
2318:
2304:
2297:
2270:
2241:(2): 237–244.
2221:
2214:
2194:
2167:
2140:
2099:
2064:
2031:(1–2): 44–56.
2008:
1962:
1905:
1848:
1799:
1742:
1693:
1642:
1599:
1570:(3): 331–340.
1550:
1521:(6): 494–501.
1501:
1444:
1387:
1352:(2): 903–909.
1336:
1329:
1305:
1298:
1267:
1258:
1249:
1190:
1183:
1155:
1154:
1152:
1149:
1148:
1147:
1142:
1137:
1132:
1126:
1120:
1119:
1116:Biology portal
1103:
1100:
1099:
1098:
1092:
1086:
1080:
1065:
1062:
1061:
1060:
1055:
1050:
1045:
1040:
1035:
1030:
1017:Main article:
1014:
1011:
1010:
1009:
1006:Lysogeny Broth
998:
995:
992:
965:
950:
927:
900:fusion protein
891:
888:
825:ribonuclease A
804:
801:
775:
752:brought on by
725:. People with
714:
711:
702:FlhB protein,
671:
668:
664:death receptor
640:
637:
613:
610:
596:
593:
509:aminopeptidase
476:
473:
396:
393:
356:
353:
322:
319:
254:
251:
192:
189:
181:signal peptide
176:
173:
146:
143:
130:signal peptide
110:
107:
105:
102:
26:
9:
6:
4:
3:
2:
4469:
4458:
4455:
4453:
4450:
4448:
4445:
4444:
4442:
4426:
4422:
4421:
4416:
4413:
4409:
4408:
4403:
4400:
4396:
4395:
4390:
4387:
4383:
4382:
4377:
4374:
4370:
4369:
4364:
4361:
4357:
4356:
4351:
4348:
4344:
4343:
4338:
4337:
4335:
4331:
4325:
4322:
4320:
4317:
4315:
4312:
4310:
4307:
4305:
4302:
4301:
4299:
4295:
4289:
4286:
4284:
4283:Enzyme family
4281:
4279:
4276:
4274:
4271:
4270:
4268:
4264:
4258:
4255:
4253:
4250:
4248:
4247:Cooperativity
4245:
4243:
4240:
4239:
4237:
4233:
4227:
4224:
4222:
4219:
4217:
4214:
4212:
4209:
4207:
4206:Oxyanion hole
4204:
4202:
4199:
4197:
4194:
4192:
4189:
4188:
4186:
4182:
4178:
4171:
4166:
4164:
4159:
4157:
4152:
4151:
4148:
4136:
4133:
4132:
4130:
4127:
4123:
4115:
4112:
4110:
4107:
4105:
4102:
4100:
4097:
4096:
4095:
4091:
4090:
4085:
4082:
4080:
4077:
4076:
4075:
4072:
4070:
4067:
4065:
4062:
4060:
4057:
4055:
4052:
4051:
4049:
4047:
4046:Endopeptidase
4043:
4039:
4029:
4026:
4025:
4023:
4019:
4011:
4008:
4006:
4003:
4001:
3998:
3996:
3993:
3991:
3988:
3986:
3983:
3982:
3981:
3978:
3975:
3971:
3970:
3968:
3966:
3962:
3956:
3950:
3948:
3944:
3941:
3940:
3938:
3936:
3932:
3926:
3923:
3922:
3920:
3918:
3914:
3906:
3903:
3901:
3898:
3897:
3896:
3893:
3889:
3886:
3884:
3881:
3880:
3879:
3876:
3875:
3873:
3871:
3867:
3859:
3856:
3854:
3851:
3849:
3846:
3845:
3844:
3841:
3840:
3838:
3836:
3832:
3824:
3821:
3817:
3814:
3812:
3809:
3808:
3807:
3804:
3802:
3799:
3797:
3794:
3792:
3789:
3787:
3784:
3782:
3779:
3777:
3774:
3773:
3772:
3769:
3768:
3766:
3764:
3760:
3757:
3755:
3751:
3747:
3742:
3738:
3734:
3727:
3722:
3720:
3715:
3713:
3708:
3707:
3704:
3688:
3685:
3684:
3682:
3680:
3676:
3672:
3668:
3664:
3661:
3659:
3654:
3644:
3641:
3640:
3638:
3636:
3632:
3628:
3624:
3618:(chromophore)
3617:
3614:
3613:
3611:
3609:
3605:
3601:
3597:
3591:(chromophore)
3590:
3587:
3586:
3584:
3582:
3578:
3574:
3570:
3567:
3565:
3560:
3550:
3547:
3546:
3544:
3542:
3538:
3534:
3528:
3525:
3524:
3522:
3520:
3516:
3512:
3506:
3503:
3502:
3500:
3498:
3497:Hydroxylysine
3494:
3490:
3484:
3481:
3479:
3476:
3475:
3473:
3471:
3467:
3463:
3460:
3458:
3453:
3443:
3440:
3439:
3437:
3435:
3431:
3425:
3424:Adenylylation
3422:
3419:
3416:
3415:
3413:
3411:
3407:
3401:
3400:Hydroxylation
3398:
3397:
3395:
3393:
3389:
3383:
3380:
3378:
3375:
3373:
3370:
3369:
3367:
3365:
3361:
3355:
3352:
3350:
3347:
3345:
3342:
3340:
3339:Succinylation
3337:
3335:
3334:Carbamylation
3332:
3330:
3327:
3325:
3322:
3320:
3318:
3314:
3312:
3309:
3307:
3304:
3302:
3299:
3297:
3294:
3292:
3289:
3287:
3286:Hydroxylation
3284:
3282:
3281:Adenylylation
3279:
3277:
3274:
3272:
3269:
3267:
3264:
3263:
3261:
3259:
3255:
3249:
3246:
3245:
3243:
3241:
3237:
3231:
3230:Glycosylation
3228:
3226:
3223:
3222:
3220:
3218:
3214:
3208:
3205:
3203:
3200:
3198:
3195:
3193:
3190:
3188:
3187:Carboxylation
3185:
3184:
3182:
3180:
3176:
3170:
3167:
3165:
3162:
3161:
3159:
3157:
3153:
3147:
3144:
3142:
3139:
3138:
3136:
3134:
3130:
3124:
3121:
3119:
3116:
3114:
3111:
3109:
3108:Adenylylation
3106:
3104:
3101:
3099:
3096:
3094:
3091:
3089:
3086:
3084:
3081:
3080:
3078:
3076:
3072:
3066:
3063:
3061:
3059:
3055:
3053:
3052:Glycosylation
3050:
3048:
3045:
3043:
3040:
3039:
3037:
3035:
3031:
3027:
3024:
3022:
3017:
3011:
3008:
3006:
3005:O-methylation
3003:
3001:
2998:
2996:
2993:
2992:
2990:
2988:
2984:
2977:
2974:
2972:
2969:
2967:
2964:
2962:
2959:
2957:
2956:Carbamylation
2954:
2952:
2949:
2948:
2946:
2944:
2940:
2934:
2931:
2929:
2926:
2924:
2921:
2919:
2916:
2914:
2911:
2910:
2908:
2904:
2900:
2896:
2889:
2884:
2882:
2877:
2875:
2870:
2869:
2866:
2860:
2857:
2854:
2851:
2850:
2840:
2834:
2830:
2829:
2823:
2822:
2810:
2806:
2803:
2797:
2789:
2785:
2780:
2775:
2771:
2767:
2763:
2756:
2748:
2744:
2739:
2734:
2729:
2724:
2720:
2716:
2712:
2708:
2704:
2697:
2689:
2685:
2680:
2675:
2670:
2665:
2661:
2657:
2653:
2649:
2645:
2638:
2630:
2626:
2621:
2616:
2611:
2606:
2602:
2598:
2594:
2590:
2586:
2579:
2571:
2567:
2562:
2557:
2553:
2549:
2545:
2538:
2530:
2526:
2520:
2512:
2508:
2504:
2500:
2496:
2492:
2485:
2477:
2473:
2469:
2465:
2461:
2457:
2454:(1): 309–17.
2453:
2449:
2442:
2434:
2430:
2426:
2422:
2414:
2406:
2402:
2398:
2394:
2390:
2386:
2382:
2378:
2371:
2363:
2359:
2355:
2349:
2345:
2341:
2337:
2332:
2331:
2322:
2314:
2308:
2300:
2294:
2290:
2286:
2285:
2277:
2275:
2266:
2262:
2257:
2252:
2248:
2244:
2240:
2236:
2232:
2225:
2217:
2211:
2207:
2206:
2198:
2190:
2186:
2182:
2178:
2171:
2163:
2159:
2155:
2151:
2144:
2136:
2130:
2122:
2118:
2114:
2110:
2103:
2095:
2091:
2087:
2083:
2080:(2): 465–94.
2079:
2075:
2068:
2054:on 2016-03-04
2050:
2046:
2042:
2038:
2034:
2030:
2026:
2019:
2012:
2004:
2000:
1996:
1992:
1988:
1984:
1980:
1976:
1969:
1967:
1958:
1954:
1949:
1944:
1940:
1936:
1932:
1928:
1924:
1920:
1916:
1909:
1901:
1897:
1892:
1887:
1883:
1879:
1875:
1871:
1867:
1863:
1859:
1852:
1844:
1840:
1835:
1830:
1826:
1822:
1818:
1814:
1810:
1803:
1795:
1791:
1786:
1781:
1777:
1773:
1769:
1765:
1761:
1757:
1753:
1746:
1738:
1734:
1730:
1726:
1721:
1716:
1712:
1708:
1704:
1697:
1689:
1685:
1681:
1677:
1673:
1669:
1665:
1661:
1657:
1653:
1646:
1638:
1634:
1630:
1626:
1622:
1618:
1614:
1610:
1603:
1595:
1591:
1587:
1583:
1578:
1573:
1569:
1565:
1561:
1554:
1546:
1542:
1537:
1532:
1528:
1524:
1520:
1516:
1512:
1505:
1497:
1493:
1488:
1483:
1479:
1475:
1471:
1467:
1463:
1459:
1455:
1448:
1440:
1436:
1431:
1426:
1422:
1418:
1414:
1410:
1406:
1402:
1398:
1391:
1383:
1379:
1375:
1371:
1367:
1363:
1359:
1355:
1351:
1347:
1340:
1332:
1326:
1322:
1318:
1317:
1309:
1301:
1295:
1291:
1287:
1286:
1281:
1274:
1272:
1262:
1253:
1245:
1241:
1236:
1231:
1226:
1221:
1217:
1213:
1209:
1205:
1201:
1194:
1186:
1180:
1176:
1172:
1171:
1163:
1161:
1156:
1146:
1143:
1141:
1138:
1136:
1133:
1130:
1127:
1125:
1122:
1121:
1117:
1111:
1106:
1096:
1093:
1090:
1087:
1084:
1081:
1078:
1075:
1074:
1073:
1071:
1059:
1056:
1054:
1051:
1049:
1046:
1044:
1041:
1039:
1036:
1034:
1031:
1029:
1026:
1025:
1024:
1020:
1007:
1003:
999:
996:
993:
990:
986:
982:
978:
974:
970:
966:
963:
959:
955:
951:
948:
944:
943:nucleic acids
940:
936:
932:
928:
925:
921:
917:
913:
909:
905:
901:
897:
896:
895:
887:
885:
881:
877:
873:
867:
865:
861:
857:
853:
849:
845:
841:
837:
832:
830:
829:sulfuric acid
826:
822:
818:
814:
813:mineral acids
809:
800:
798:
794:
789:
787:
783:
779:
771:
767:
763:
759:
755:
751:
747:
743:
742:antiproteases
738:
736:
732:
728:
724:
720:
710:
707:
706:
701:
700:
695:
694:
689:
685:
681:
677:
667:
665:
662:, or via the
661:
657:
653:
649:
645:
636:
634:
630:
626:
622:
618:
609:
605:
603:
592:
590:
589:
584:
579:
577:
573:
569:
565:
561:
557:
553:
549:
545:
541:
536:
534:
530:
526:
525:phenylalanine
522:
518:
514:
510:
506:
502:
498:
494:
490:
486:
482:
472:
468:
466:
462:
458:
454:
450:
446:
445:PEST proteins
442:
438:
434:
433:glutamic acid
430:
426:
421:
419:
415:
411:
407:
403:
392:
388:
386:
382:
378:
374:
370:
361:
352:
348:
346:
345:
340:
336:
332:
328:
318:
316:
312:
308:
303:
301:
297:
291:
288:
284:
280:
276:
275:preproinsulin
272:
268:
264:
260:
250:
248:
244:
240:
236:
232:
228:
227:
222:
218:
214:
210:
209:polycistronic
206:
201:
199:
188:
186:
182:
172:
170:
166:
162:
158:
157:
152:
142:
139:
135:
131:
127:
124:
120:
116:
101:
98:
96:
91:
86:
84:
80:
76:
72:
71:peptide bonds
68:
64:
60:
57:into smaller
56:
52:
45:
42:(red) by the
41:
37:
32:
19:
4420:Translocases
4417:
4404:
4391:
4378:
4365:
4355:Transferases
4352:
4339:
4196:Binding site
4010:Glutamate II
3805:
3754:Exopeptidase
3354:Butyrylation
3316:
3057:
2928:Racemization
2922:
2913:Peptide bond
2827:
2796:
2772:(1): 13–25.
2769:
2765:
2755:
2713:(4): e5094.
2710:
2706:
2696:
2651:
2647:
2637:
2592:
2588:
2578:
2551:
2547:
2537:
2528:
2519:
2494:
2490:
2484:
2451:
2447:
2441:
2424:
2420:
2413:
2380:
2376:
2370:
2329:
2321:
2307:
2283:
2238:
2234:
2224:
2204:
2197:
2180:
2176:
2170:
2153:
2149:
2143:
2129:cite journal
2115:(4): 361–7.
2112:
2108:
2102:
2077:
2073:
2067:
2056:. Retrieved
2049:the original
2028:
2024:
2011:
1978:
1974:
1922:
1918:
1908:
1865:
1861:
1851:
1816:
1812:
1802:
1759:
1755:
1745:
1710:
1706:
1696:
1655:
1651:
1645:
1612:
1608:
1602:
1567:
1563:
1553:
1518:
1514:
1504:
1461:
1458:Cell Reports
1457:
1447:
1404:
1400:
1390:
1349:
1345:
1339:
1316:Biochemistry
1315:
1308:
1284:
1261:
1252:
1207:
1203:
1193:
1169:
1067:
1022:
931:proteinase K
924:TEV protease
920:enterokinase
912:purification
898:Cleavage of
893:
868:
844:tryptophanyl
833:
810:
806:
790:
778:-antitrypsin
739:
719:pancreatitis
716:
703:
697:
691:
676:peptide bond
673:
642:
615:
606:
598:
586:
580:
568:enterokinase
560:chymotrypsin
540:pancreatitis
537:
497:chymotrypsin
478:
469:
422:
398:
389:
366:
349:
342:
339:phagocytosis
324:
304:
292:
256:
246:
242:
224:
221:retroviruses
212:
202:
194:
178:
154:
148:
112:
99:
87:
77:by cellular
59:polypeptides
50:
49:
4191:Active site
3947:Cathepsin A
3883:Cathepsin C
3843:Dipeptidase
3418:Diphthamide
3377:Methylation
3344:Lactylation
3306:Deamination
3296:Sumoylation
3271:Acetylation
3266:Methylation
3225:Deamidation
3197:Methylation
3146:Prenylation
2971:Methylation
2961:Formylation
2951:Acetylation
2923:Proteolysis
1407:: 156–164.
1095:hemorrhagic
960:yields the
904:protein tag
884:carcinogens
864:formic acid
856:asparaginyl
784:(MMPs) and
762:macrophages
758:neutrophils
564:trypsinogen
513:dipeptidase
418:erythrocyte
414:haemoglobin
296:trypsinogen
267:prehormones
231:Nidovirales
161:prokaryotes
115:translation
63:amino acids
51:Proteolysis
4452:Metabolism
4441:Categories
4394:Isomerases
4368:Hydrolases
4235:Regulation
3541:Tryptophan
3537:Tryptophan
3493:Methionine
3434:Tryptophan
3217:Asparagine
2987:C terminus
2943:N terminus
2235:Aging Cell
2058:2012-06-30
1151:References
1135:Proteasome
1097:(bleeding)
958:subtilisin
840:methionine
797:malignancy
699:Salmonella
666:pathways.
660:granzyme B
656:apoptosome
629:cell cycle
583:Subtilisin
548:pepsinogen
533:tryptophan
465:proteasome
449:asparagine
425:N-end rule
385:cathepsins
377:proteasome
279:proinsulin
263:proenzymes
169:N-end rule
165:eukaryotes
134:proprotein
126:methionine
123:N-terminal
67:hydrolysis
36:hydrolysis
4273:EC number
4128:: Unknown
3806:Methionyl
3737:proteases
3733:Hydrolase
3687:Desmosine
3600:Histidine
3420:formation
3410:Histidine
3329:Glycation
3276:Acylation
3240:Glutamine
3179:Glutamate
3156:Aspartate
3098:Sulfation
3034:Threonine
2995:Amidation
2966:Glycation
1995:1089-8638
1939:0021-9193
1882:1098-5530
1776:0264-6021
1729:0021-9258
1688:205003883
1478:2211-1247
1421:1879-033X
1366:1097-0134
1321:1010–1014
1145:Ubiquitin
1083:hemotoxic
1077:cytotoxic
872:pyrolysis
852:cysteinyl
788:(TIMPs).
750:emphysema
735:Alzheimer
682:. Unlike
648:apoptosis
639:Apoptosis
481:digestion
479:In human
475:Digestion
457:histidine
441:threonine
381:autophagy
373:ubiquitin
95:apoptosis
83:proteases
75:catalysed
4297:Kinetics
4221:Cofactor
4184:Activity
3801:Glutamyl
3791:Cystinyl
3786:Aspartyl
3675:Allysine
3671:Allysine
3667:Allysine
3604:Tyrosine
3577:Tyrosine
3519:Tyrosine
3470:Cysteine
3466:Cysteine
3364:Arginine
3133:Cysteine
3075:Tyrosine
2805:Archived
2788:22016395
2747:19352432
2707:PLOS ONE
2688:23056252
2648:PLOS ONE
2511:11313117
2476:33835929
2468:20213167
2265:26751411
2121:18371259
2094:20393191
2045:12359129
2003:18314133
1957:19395493
1900:10940035
1843:18662906
1794:12882646
1737:12582180
1629:11001069
1594:17882616
1496:25220455
1439:24632559
1382:13942948
1374:18004785
1346:Proteins
1129:PROTOMAP
1102:See also
1089:myotoxic
1019:Protease
1002:tryptone
981:proteins
947:nuclease
916:thrombin
906:used in
874:; small
848:aspartyl
772:such as
766:elastase
723:pancreas
705:Yersinia
684:zymogens
658:, or by
644:Caspases
633:anaphase
576:duodenum
552:pancreas
529:tyrosine
517:arginine
501:elastase
487:such as
369:lysosome
259:zymogens
185:membrane
55:proteins
4407:Ligases
4177:Enzymes
3781:Arginyl
3776:Alanine
3635:Glycine
3627:Alanine
3608:Glycine
3581:Glycine
3392:Proline
3060:-GlcNAc
2906:General
2738:2661377
2715:Bibcode
2679:3463568
2656:Bibcode
2629:4905667
2597:Bibcode
2570:1236799
2405:4315057
2397:6462230
2362:3692961
2256:4783340
1948:2698497
1834:2548358
1785:1223699
1680:1846030
1660:Bibcode
1637:4429634
1586:9150132
1545:4604970
1536:1413009
1487:4358326
1430:4010099
1290:463–473
1244:2682640
1212:Bibcode
811:Strong
770:serpins
754:smoking
625:mitosis
621:kinases
617:Cyclins
574:of the
556:trypsin
493:trypsin
453:cystein
429:proline
371:, or a
313:of the
300:trypsin
271:Insulin
205:viruses
156:E. coli
138:albumin
81:called
79:enzymes
40:protein
4457:EC 3.4
4381:Lyases
4126:3.4.99
4042:3.4.21
3965:3.4.17
3935:3.4.16
3917:3.4.15
3870:3.4.14
3835:3.4.13
3796:Leucyl
3763:3.4.11
3750:3.4.11
3679:Lysine
3631:Serine
3573:Serine
3515:Lysine
3258:Lysine
3030:Serine
2835:
2786:
2745:
2735:
2686:
2676:
2627:
2620:286206
2617:
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2092:
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1993:
1955:
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1937:
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1652:Nature
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1609:Nature
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1427:
1419:
1380:
1372:
1364:
1327:
1296:
1242:
1235:298257
1232:
1181:
1070:snakes
1064:Venoms
922:, and
854:, and
572:mucosa
544:pepsin
531:, and
521:lysine
511:, and
499:, and
489:pepsin
439:, and
437:serine
410:myosin
379:. The
331:organs
265:, and
226:ORF1ab
4333:Types
4044:-25:
3752:-19:
2978:(Gly)
2472:S2CID
2401:S2CID
2358:S2CID
2052:(PDF)
2021:(PDF)
1684:S2CID
1633:S2CID
1590:S2CID
1378:S2CID
1175:78–86
956:with
406:actin
219:) in
203:Many
38:of a
4425:list
4418:EC7
4412:list
4405:EC6
4399:list
4392:EC5
4386:list
4379:EC4
4373:list
4366:EC3
4360:list
4353:EC2
4347:list
4340:EC1
3743:3.4)
2897:and
2833:ISBN
2784:PMID
2743:PMID
2684:PMID
2625:PMID
2566:PMID
2507:PMID
2464:PMID
2393:PMID
2348:ISBN
2293:ISBN
2261:PMID
2210:ISBN
2135:link
2117:PMID
2090:PMID
2041:PMID
1999:PMID
1991:ISSN
1953:PMID
1935:ISSN
1896:PMID
1878:ISSN
1839:PMID
1790:PMID
1772:ISSN
1733:PMID
1725:ISSN
1676:PMID
1625:PMID
1582:PMID
1564:Cell
1541:PMID
1492:PMID
1474:ISSN
1435:PMID
1417:ISSN
1370:PMID
1362:ISSN
1325:ISBN
1294:ISBN
1240:PMID
1179:ISBN
937:and
935:urea
910:and
862:and
760:and
558:and
519:and
423:The
408:and
335:guts
245:and
223:and
163:and
151:fMet
34:The
3658:AAs
3564:AAs
3457:AAs
3021:AAs
2774:doi
2770:151
2733:PMC
2723:doi
2674:PMC
2664:doi
2615:PMC
2605:doi
2556:doi
2499:doi
2456:doi
2452:397
2429:doi
2385:doi
2381:310
2340:doi
2336:485
2251:PMC
2243:doi
2185:doi
2181:118
2158:doi
2154:110
2082:doi
2033:doi
1983:doi
1979:377
1943:PMC
1927:doi
1923:191
1886:PMC
1870:doi
1866:182
1829:PMC
1821:doi
1780:PMC
1764:doi
1760:375
1715:doi
1711:278
1668:doi
1656:349
1617:doi
1613:407
1572:doi
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1482:PMC
1466:doi
1425:PMC
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1354:doi
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