The Enzyme Database

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EC 3.4.22.1     
Accepted name: cathepsin B
Reaction: Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg┼ bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides
Other name(s): cathepsin B1 (obsolete); cathepsin II
Comments: An intracellular (lysosomal) enzyme in peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9047-22-7
References:
1.  Bond, J.S. and Barrett, A.J. Degradation of fructose-1,6-bisphosphate aldolase by cathepsin B. A further example of peptidyldipeptidase activity of this proteinase. Biochem. J. 189 (1980) 17–25. [PMID: 7458901]
2.  Barrett, A.J. and Kirschke, H. Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. 80 (1981) 535–561. [PMID: 7043200]
3.  Polgár, L. and Csoma, C. Dissociation of ionizing groups in the binding cleft inversely controls the endo- and exopeptidase activities of cathepsin B. J. Biol. Chem. 262 (1987) 14448–14453. [PMID: 3312190]
4.  Barrett, A.J., Buttle, D.J. and Mason, R.W. Lysosomal cysteine proteinases. ISI Atlas of Science. Biochemistry 1 (1988) 256–260.
5.  Kirschke, H., Wikstrom, P. and Shaw, E. Active center differences between cathepsins L and B: the S1 binding region. FEBS Lett. 228 (1988) 128–130. [DOI] [PMID: 3342870]
[EC 3.4.22.1 created 1972]
 
 
EC 3.4.22.2     
Accepted name: papain
Reaction: Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1′
Other name(s): papayotin; summetrin; velardon; papaine; Papaya peptidase I
Comments: Type example of peptidase family C1 from latex of the papaya (Carica papaya) fruit. Inhibited by compound E-64 and proteins of the cystatin family.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9001-73-4
References:
1.  Kamphuis, I.G., Drenth, J. and Baker, E.N. Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain. J. Mol. Biol. 182 (1985) 317–329. [DOI] [PMID: 3889350]
2.  Ménard, R. and Storer, A.C. Papain. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 555–557.
[EC 3.4.22.2 created 1961 as EC 3.4.4.10, transferred 1972 to EC 3.4.22.2, modified 1976, modified 2000]
 
 
EC 3.4.22.3     
Accepted name: ficain
Reaction: Similar to that of papain
Other name(s): ficin; debricin; higueroxyl delabarre
Comments: The major proteolytic component of the latex of fig, Ficus glabrata. Cysteine endopeptidases with similar properties are present in other members of the large genus Ficus. In peptidase family C1 (papain family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9001-33-6
References:
1.  Liener, I.E. and Friedenson, B. Ficin. Methods Enzymol. 19 (1970) 261–273.
2.  Brocklehurst, K., Willenbrock, F. and Salih, E. Cysteine proteinases. In: Neuberger, A. and Brocklehurst, K. (Eds), New Comprehensive Biochemistry: Hydrolytic Enzymes, Elsevier, Amsterdam, 1987, pp. 39–158.
[EC 3.4.22.3 created 1961 as EC 3.4.4.12, transferred 1972 to EC 3.4.22.3]
 
 
EC 3.4.22.4      
Transferred entry: bromelain (stem). Now EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain)
[EC 3.4.22.4 created 1972, deleted 1992 [EC 3.4.22.5 created 1972, incorporated 1978]]
 
 
EC 3.4.22.5      
Transferred entry: bromelain (juice). Now EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain)
[EC 3.4.22.5 created 1972, deleted 1978]
 
 
EC 3.4.22.6     
Accepted name: chymopapain
Reaction: Similar to that of papain
Other name(s): chymopapain A; chymopapain B; chymopapain S
Comments: The major endopeptidase of papaya (Carica papaya) latex. It has multiple chromatographic forms. In peptidase family C1 (papain family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9001-09-6
References:
1.  Brocklehurst, K., Willenbrock, F. and Salih, E. Cysteine proteinases. In: Neuberger, A. and Brocklehurst, K. (Eds), New Comprehensive Biochemistry: Hydrolytic Enzymes, Elsevier, Amsterdam, 1987, pp. 39–158.
2.  Jacquet, A., Kleinschmidt, T., Schnek, A.G., Looze, Y. and Braunitzer, G. The thiol proteinases from the latex of Carica papaya L. III. The primary structure of chymopapain. Biol. Chem. Hoppe-Seyler 370 (1989) 425–434. [PMID: 2500950]
3.  Buttle, D.J., Dando, P.M., Coe, P.F., Sharp, S.L., Shepherd, S.T. and Barrett, A.J. The preparation of fully active chymopapain free of contaminating proteinases. Biol. Chem. Hoppe-Seyler 371 (1990) 1083–1088. [PMID: 2085414]
[EC 3.4.22.6 created 1961 as EC 3.4.4.11, transferred 1972 to EC 3.4.22.6]
 
 
EC 3.4.22.7     
Accepted name: asclepain
Reaction: Similar to that of papain
Comments: From the latex of milkweed, Asclepias syriaca. It has multiple forms, and is in peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 37288-80-5
References:
1.  Brockbank, W.J. and Lynn, K.R. Purification and preliminary characterization of two asclepains from the latex of Asclepias syriaca L. (milkweed). Biochim. Biophys. Acta 578 (1979) 13–22. [DOI] [PMID: 36921]
[EC 3.4.22.7 created 1972]
 
 
EC 3.4.22.8     
Accepted name: clostripain
Reaction: Preferential cleavage: Arg┼, including Arg┼Pro, but not Lys-
Other name(s): clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase
Comments: From the bacterium Clostridium histolyticum. It requires Ca2+ ions and is inhibited by EDTA. Type example of peptidase family C11.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9028-00-6
References:
1.  Mitchell, W.M. Cleavage at arginine residues by clostripain. Methods Enzymol. 47 (1977) 165–170. [DOI] [PMID: 927173]
2.  Gilles, A.-M., Imhoff, J.-M. and Keil, B. α-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain. J. Biol. Chem. 254 (1979) 1462–1468. [PMID: 762145]
3.  Gilles, A.-M., Lecroisey, A. and Keil, B. Primary structure of α-clostripain light chain. Eur. J. Biochem. 145 (1984) 469–476. [DOI] [PMID: 6391922]
[EC 3.4.22.8 created 1961 as EC 3.4.4.20, transferred 1972 to EC 3.4.22.8]
 
 
EC 3.4.22.9      
Transferred entry: yeast proteinase B. Now EC 3.4.21.48, cerevisin
[EC 3.4.22.9 created 1972, deleted 1981]
 
 
EC 3.4.22.10     
Accepted name: streptopain
Reaction: Preferential cleavage with hydrophobic residues at P2, P1 and P1′
Other name(s): Streptococcus peptidase A; streptococcal cysteine proteinase; Streptococcus protease
Comments: From the bacterium, group A Streptococcus. Formed from the proenzyme by limited proteolysis. Type example of peptidase family C10.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-51-8
References:
1.  Elliott, S.D. and Liu, T.-Y. Streptococcal proteinase. Methods Enzymol. 19 (1970) 252–261.
2.  Liu, T.-Y. and Elliott, S.D. Streptococcal proteinase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, Academic Press, New York, 1971, pp. 609–647.
3.  Tai, J. Y., Kortt, A.A., Liu, T.-Y. and Elliott, S.D. Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain. J. Biol. Chem. 251 (1976) 1955–1959. [PMID: 1270417]
4.  Lo, S.-S., Fraser, B.A. and Liu, T.-Y. The mixed disulphide in the zymogen of streptococcal proteinase. Characterization and implication for its biosynthesis. J. Biol. Chem. 259 (1984) 11041–11045. [PMID: 6381494]
[EC 3.4.22.10 created 1961 as EC 3.4.4.18, transferred 1972 to EC 3.4.22.10]
 
 
EC 3.4.22.11      
Transferred entry: insulinase. Now EC 3.4.24.56, insulysin
[EC 3.4.22.11 created 1976, deleted 1978 [transferred to EC 3.4.99.45, deleted 1993]]
 
 
EC 3.4.22.12      
Transferred entry: γ-glutamyl hydrolase. Now EC 3.4.19.9, γ-glutamyl hydrolase
[EC 3.4.22.12 created 1978, deleted 1992]
 
 
EC 3.4.22.13      
Deleted entry:  staphylococcal cysteine proteinase
[EC 3.4.22.13 created 1978, modified 1981, deleted 1992]
 
 
EC 3.4.22.14     
Accepted name: actinidain
Reaction: Similar to that of papain
Other name(s): actinidin; Actinidia anionic protease; proteinase A2 of Actinidia chinensis
Comments: From the kiwi fruit or Chinese gooseberry (Actinidia chinensis). In peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 39279-27-1
References:
1.  Baker, E.N., Boland, M.J., Calder, P.C. and Hardman, M.J. The specificity of actinidin and its relationship to the structure of the enzyme. Biochim. Biophys. Acta 616 (1980) 30–34. [DOI] [PMID: 7002215]
2.  Kamphuis, I.G., Drenth, J. and Baker, E.N. Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain. J. Mol. Biol. 182 (1985) 317–329. [DOI] [PMID: 3889350]
3.  Baker, E.N. and Drenth, J. The thiol proteases: stucture and mechanism. In: Jurnak, F.A. and McPherson, A. (Eds), Biological Macromolecules and Assemblies: Active Sites of Enzymes, vol. 3, John Wiley and Sons, New York, 1987, pp. 314–368.
[EC 3.4.22.14 created 1978]
 
 
EC 3.4.22.15     
Accepted name: cathepsin L
Reaction: Similar to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity
Other name(s): Aldrichina grahami cysteine proteinase
Comments: A lysosomal enzyme in peptidase family C1 (papain family) that is readily inhibited by the diazomethane inhibitor Z-Phe-Phe-CHN2 or the epoxide inhibitor E-64
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 60616-82-2
References:
1.  Barrett, A.J. and Kirschke, H. Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. 80 (1981) 535–561. [PMID: 7043200]
2.  Barrett, A.J., Buttle, D.J. and Mason, R.W. Lysosomal cysteine proteinases. ISI Atlas of Science. Biochemistry 1 (1988) 256–260.
3.  Joseph, L.J., Chang, L.C., Stamenkovich, D. and Sukhatme, V.P. Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts. J. Clin. Invest. 81 (1988) 1621–1629. [DOI] [PMID: 2835398]
4.  Kirschke, H., Wikstrom, P. and Shaw, E. Active center differences between cathepsins L and B: the S1 binding region. FEBS Lett. 228 (1988) 128–130. [DOI] [PMID: 3342870]
[EC 3.4.22.15 created 1978 (EC 3.4.99.19 created 1972, incorporated 1981)]
 
 
EC 3.4.22.16     
Accepted name: cathepsin H
Reaction: Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg┼ bonds) as well as an endopeptidase
Other name(s): cathepsin B3; benzoylarginine-naphthylamide (BANA) hydrolase (obsolete); cathepsin Ba, aleurain; N-benzoylarginine-β-naphthylamide hydrolase
Comments: Present in lysosomes of mammalian cells. In peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 60748-73-4
References:
1.  Barrett, A.J. and Kirschke, H. Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. 80 (1981) 535–561. [PMID: 7043200]
2.  Brömme, D., Bescherer, K., Kirschke, H. and Fittkau, S. Enzyme-substrate interactions in the hydrolysis of peptides by cathepsins B and H from rat liver. Biochem. J. 245 (1987) 381–385. [PMID: 3663163]
3.  Fuchs, R., Machleidt, W. and Gassen, H.G. Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H. Biol. Chem. Hoppe-Seyler 369 (1988) 469–475. [PMID: 2849458]
[EC 3.4.22.16 created 1981, modified 1989]
 
 
EC 3.4.22.17      
Transferred entry: calpain. Now EC 3.4.22.53, calpain-2
[EC 3.4.22.17 created 1981 [EC 3.4.24.5 created 1978, part incorporated 1989], deleted 2003]
 
 
EC 3.4.22.18      
Transferred entry: prolyl endopeptidase (thiol-dependent). Now EC 3.4.21.26, prolyl oligopeptidase
[EC 3.4.22.18 created 1981, deleted 1992]
 
 
EC 3.4.22.19      
Transferred entry: endo-oligopeptidase. Now EC 3.4.24.15, thimet oligopeptidase
[EC 3.4.22.19 created 1989, deleted 1992]
 
 
EC 3.4.22.20      
Deleted entry:  dinorphin-converting enzyme
[EC 3.4.22.20 created 1989, deleted 1992]
 
 
EC 3.4.22.21      
Transferred entry: yeast cysteine proteinase E. Now EC 3.4.25.1, proteasome endopeptidase complex
[EC 3.4.22.21 created 1989, deleted 1992]
 
 
EC 3.4.22.22      
Transferred entry: yeast cysteine proteinase D. Now EC 3.4.24.37, saccharolysin
[EC 3.4.22.22 created 1989, deleted 1992]
 
 
EC 3.4.22.23      
Transferred entry: yeast cysteine proteinase F. Now EC 3.4.21.61, kexin
[EC 3.4.22.23 created 1989, deleted 1992]
 
 
EC 3.4.22.24     
Accepted name: cathepsin T
Reaction: Interconversion of the three forms of tyrosine aminotransferase, EC 2.6.1.5
Comments: Degrades azocasein and denatured hemoglobin; the only native protein on which it has been shown to act is tyrosine aminotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77464-86-9
References:
1.  Gohda, E. and Pitot, H.C. Purification and characterization of a new thiol proteinase from rat kidney. Biochim. Biophys. Acta 659 (1981) 114–122. [DOI] [PMID: 7248311]
2.  Gohda, E. and Pitot, H.C. A new thiol proteinase from rat liver. J. Biol. Chem. 256 (1981) 2567–2572. [PMID: 6780567]
3.  Pitot, H.C. and Gohda, E. Cathepsin T. Methods Enzymol. 142 (1987) 279–289. [PMID: 2885716]
[EC 3.4.22.24 created 1990]
 
 
EC 3.4.22.25     
Accepted name: glycyl endopeptidase
Reaction: Preferential cleavage: Gly┼, in proteins and small molecule substrates
Other name(s): papaya peptidase B; papaya proteinase IV; glycine-specific proteinase; chymopapain; Papaya proteinase 4; PPIV; chymopapain M
Comments: From the papaya plant, Carica papaya. Not inhibited by chicken cystatin, unlike most other homologues of papain, but in peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 149719-24-4
References:
1.  Polgár, L. Isolation of highly active papaya peptidases A and B from commercial chymopapain. Biochim. Biophys. Acta 658 (1981) 262–269. [DOI] [PMID: 7018581]
2.  Buttle, D.J., Kembhavi, A.A., Sharp, S.L., Shute, R.E., Rich, D.H. and Barrett, A.J. Affinity purification of the novel cysteine proteinase papaya proteinase IV and papain from papaya latex. Biochem. J. 261 (1989) 469–476. [PMID: 2505761]
3.  Ritonja, A., Buttle, D.J., Rawlings, N.D., Turk, V. and Barrett, A.J. Papaya proteinase IV amino acid sequence. FEBS Lett. 258 (1989) 109–112. [DOI] [PMID: 2591528]
4.  Buttle, D.J., Ritonja, A., Pearl, L.H., Turk, V. and Barrett, A.J. Selective cleavage of glycyl bonds by papaya proteinase IV. FEBS Lett. 260 (1990) 195–197. [DOI] [PMID: 2404797]
5.  Buttle, D.J., Ritonja, A., Dando, P.M., Abrahamson, M., Shaw, E.N., Wikstrom, P., Turk, V. and Barrett, A.J. Interaction of papaya proteinase IV with inhibitors. FEBS Lett. 262 (1990) 58–60. [DOI] [PMID: 1690669]
[EC 3.4.22.25 created 1992]
 
 
EC 3.4.22.26     
Accepted name: cancer procoagulant
Reaction: Specific cleavage of Arg┼Ile bond in Factor X to form Factor Xa
Comments: Apparently produced only by malignant and fetal cells
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 109456-80-6
References:
1.  Falanga, A. and Gordon, S.G. Isolation and characterization of cancer procoagulant: a cysteine proteinase from malignant tissue. Biochemistry 24 (1985) 5558–5567. [PMID: 3935163]
2.  Falanga, A., Shaw, E., Donati, M.B., Consonni, R., Barbui, T. and Gordon, S. Inhibition of cancer procoagulant by peptidyl diazomethyl ketones and peptidyl sulfonium salts. Thromb. Res. 54 (1989) 389–398. [DOI] [PMID: 2772865]
[EC 3.4.22.26 created 1992]
 
 
EC 3.4.22.27     
Accepted name: cathepsin S
Reaction: Similar to cathepsin L, but with much less activity on Z-Phe-Arg┼NHMec, and more activity on the Z-Val-Val-Arg┼ compound
Comments: A lysosomal cysteine endopeptidase that is unusual amongst such enzymes for its stability to neutral pH. In peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 71965-46-3
References:
1.  Turnšek, T., Kregar, I. and Lebez, D. Acid sulphydryl protease from calf lymph nodes. Biochim. Biophys. Acta 403 (1975) 514–520. [DOI] [PMID: 1182153]
2.  Brömme, D., Steinert, A., Friebe, S., Fittkau, S., Wiederanders, B. and Kirschke, H. The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B. Biochem. J. 264 (1989) 475–485. [PMID: 2604727]
3.  Kirschke, H., Wiederanders, B., Brömme, D. and Rinne, A. Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins. Biochem. J. 264 (1989) 467–473. [PMID: 2690828]
[EC 3.4.22.27 created 1992]
 
 
EC 3.4.22.28     
Accepted name: picornain 3C
Reaction: Selective cleavage of Gln┼Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly
Other name(s): picornavirus endopeptidase 3C; poliovirus protease 3C; rhinovirus protease 3C; foot-and-mouth protease 3C; poliovirus proteinase 3C; rhinovirus proteinase 3C; coxsackievirus 3C proteinase; foot-and-mouth-disease virus proteinase 3C; 3C protease; 3C proteinase; cysteine proteinase 3C; hepatitis A virus 3C proteinase; protease 3C; tomato ringspot nepovirus 3C-related protease
Comments: From entero-, rhino-, aphto- and cardioviruses. Larger than the homologous virus picornain 2A. Type example of peptidase family C3
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 97162-88-4
References:
1.  Ivanoff, L.A., Towatari, T., Ray, J., Korant, B.D. and Petteway, S.R. Expression and site-specific mutagenesis of the poliovirus 3C protease in Escherichia coli. Proc. Natl Acad. Sci. USA 83 (1986) 5392–5396. [DOI] [PMID: 3016701]
2.  Bazan, J.F. and Fletterick, R.J. Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. Proc. Natl Acad. Sci. USA 85 (1988) 7872–7876. [DOI] [PMID: 3186696]
3.  Kräusslich, H.-G. and Wimmer, E. Viral proteinases. Annu. Rev. Biochem. 57 (1988) 701–754. [DOI] [PMID: 3052288]
4.  Nicklin, M.J.H., Harris, K.S., Pallai, P.V. and Wimmer, E. Poliovirus proteinase 3C: large-scale expression, purification, and specific cleavage activity on natural and synthetic substrates in vitro. J. Virol. 62 (1988) 4586–4593. [PMID: 2846872]
[EC 3.4.22.28 created 1992]
 
 
EC 3.4.22.29     
Accepted name: picornain 2A
Reaction: Selective cleavage of Tyr┼Gly bond in picornavirus polyprotein
Other name(s): picornavirus endopeptidase 2A; poliovirus protease 2A; rhinovirus protease 2A; 2A protease; 2A proteinase; protease 2A; proteinase 2Apro; picornaviral 2A proteinase; Y-G proteinase 2A; poliovirus proteinase 2A; poliovirus protease 2Apro; picornaviral 2A proteinase
Comments: From entero-, rhino-, aphto- and cardioviruses. Smaller than the homologous picornain 3C, which is also in peptidase family C3 (picornain 3C family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 103406-62-8
References:
1.  Bazan, J.F. and Fletterick, R.J. Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. Proc. Natl Acad. Sci. USA 85 (1988) 7872–7876. [DOI] [PMID: 3186696]
2.  König, H. and Rosenwirth, B. Purification and partial characterization of poliovirus protease 2A by means of a functional assay. J. Virol. 62 (1988) 1243–1250. [PMID: 2831385]
3.  Kräusslich, H.-G. and Wimmer, E. Viral proteinases. Annu. Rev. Biochem. 57 (1988) 701–754. [DOI] [PMID: 3052288]
[EC 3.4.22.29 created 1992]
 
 
EC 3.4.22.30     
Accepted name: caricain
Reaction: Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
Other name(s): papaya peptidase A; papaya peptidase II; papaya proteinase ; papaya proteinase III; papaya proteinase 3; proteinase ω; papaya proteinase A; chymopapain S; Pp
Comments: From papaya plant, Carica papaya. In peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 39307-22-7
References:
1.  Schack, P. Fractionation of proteolytic enzymes of dried papaya latex. Isolation and preliminary characterization of a new proteolytic enzyme. C. R. Trav. Carlesberg 36 (1967) 67–83. [PMID: 6043136]
2.  Robinson, G.W. Isolation and characterization of papaya peptidase A from commercial chymopapain. Biochemistry 16 (1975) 3695–3700. [PMID: 240390]
3.  Polgár, L. Problems of classification of papaya latex proteinases. Biochem. J. 221 (1984) 555–556. [PMID: 6383350]
4.  Brocklehurst, K., Salih, E., McKee, R. and Smith, H. Fresh non-fruit latex of Carica papaya contains papain, multiple forms of chymopapain A and papaya proteinase . Biochem. J. 228 (1985) 525–527. [PMID: 4015629]
5.  Zucker, S., Buttle, D.J., Nicklin, M.J.H. and Barrett, A.J. Proteolytic activities of papain, chymopapain and papaya proteinase III. Biochim. Biophys. Acta 828 (1985) 196–204. [DOI] [PMID: 3919769]
6.  Dubois, T., Kleinschmidt, T., Schnek, A.G., Looze, Y. and Braunitzer, G. The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase . Biol. Chem. Hoppe-Seyler 369 (1988) 741–754. [PMID: 3063283]
[EC 3.4.22.30 created 1992]
 
 
EC 3.4.22.31     
Accepted name: ananain
Reaction: Hydrolysis of proteins with broad specificity for peptide bonds. Best reported small molecule substrate Bz-Phe-Val-Arg┼NHMec, but broader specificity than fruit bromelain
Other name(s): stem bromelain; fruit bromelain
Comments: From stem of pineapple plant, Ananas comosus. Differs from stem and fruit bromelains in being inhibited by chicken cystatin. In peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 119129-70-3
References:
1.  Rowan, A.D., Buttle, D.J. and Barrett, A.J. Ananain: a novel cysteine proteinase found in pineapple stem. Arch. Biochem. Biophys. 267 (1988) 262–270. [DOI] [PMID: 3196029]
2.  Rowan, A.D., Buttle, D.J. and Barrett, A.J. The cysteine proteinases of the pineapple plant. Biochem. J. 266 (1990) 869–875. [PMID: 2327970]
[EC 3.4.22.31 created 1992]
 
 
EC 3.4.22.32     
Accepted name: stem bromelain
Reaction: Broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg┼NHMec amongst small molecule substrates
Other name(s): bromelain; pineapple stem bromelain
Comments: The most abundant of the cysteine endopeptidases of the stem of the pineapple plant, Ananas comosus. Distinct from the bromelain found in the pineapple fruit (EC 3.4.22.33). Scarcely inhibited by chicken cystatin and also very slowly inactivated by E-64. In peptidase family C1 (papain family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 37189-34-7
References:
1.  Brocklehurst, K., Willenbrock, F. and Salih, E. Cysteine proteinases. In: Neuberger, A. and Brocklehurst, K. (Eds), New Comprehensive Biochemistry: Hydrolytic Enzymes, Elsevier, Amsterdam, 1987, pp. 39–158.
2.  Rowan, A.D., Buttle, D.J. and Barrett, A.J. Ananain: a novel cysteine proteinase found in pineapple stem. Arch. Biochem. Biophys. 267 (1988) 262–270. [DOI] [PMID: 3196029]
3.  Ritonja, A., Rowan, A.B., Buttle, D.J., Rawlings, N.D., Turk, V. and Barrett, A.J. Stem bromelain: amino acid sequence and implications for weak binding to cystatin. FEBS Lett. 247 (1989) 419–429. [DOI] [PMID: 2714443]
4.  Rowan, A.D., Buttle, D.J. and Barrett, A.J. The cysteine proteinases of the pineapple plant. Biochem. J. 266 (1990) 869–875. [PMID: 2327970]
[EC 3.4.22.32 created 1965 as EC 3.4.4.24, transferred 1972 to EC 3.4.22.4, part transferred 1992 to EC 3.4.22.32]
 
 
EC 3.4.22.33     
Accepted name: fruit bromelain
Reaction: Hydrolysis of proteins with broad specificity for peptide bonds. Bz-Phe-Val-Arg┼NHMec is a good synthetic substrate, but there is no action on Z-Arg-Arg-NHMec (c.f. stem bromelain)
Other name(s): juice bromelain; ananase; bromelase; bromelin; extranase; juice bromelain; pinase; pineapple enzyme; traumanase; fruit bromelain FA2
Comments: From the pineapple plant, Ananas comosus. Scarcely inhibited by chicken cystatin. Another cysteine endopeptidase, with similar action on small molecule substrates, pinguinain, is obtained from the related plant, Bromelia pinguin, but pinguinain differs from fruit bromelain in being inhibited by chicken cystatin [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9001-00-7
References:
1.  Sasaki, M., Kato, T. and Iida, S. Antigenic determinant common to four kinds of thiol proteases of plant origin. J. Biochem. (Tokyo) 74 (1973) 635–637. [PMID: 4127920]
2.  Yamada, F., Takahashi, N. and Murachi, T. Purification and characterization of a proteinase from pineapple fruit, fruit bromelain FA2. J. Biochem. (Tokyo) 79 (1976) 1223–1234. [PMID: 956152]
3.  Ota, S., Muta, E., Katanita, Y. and Okamoto, Y. Reinvestigation of fractionation and some properties of the proteolytically active components of stem and fruit bromelains. J. Biochem. (Tokyo) 98 (1985) 219–228. [PMID: 4044551]
4.  Rowan, A.D., Buttle, D.J. and Barrett, A.J. The cysteine proteinases of the pineapple plant. Biochem. J. 266 (1990) 869–875. [PMID: 2327970]
[EC 3.4.22.33 created 1965 as EC 3.4.4.24, transferred 1972 to EC 3.4.22.4, part transferred 1992 to EC 3.4.22.33]
 
 
EC 3.4.22.34     
Accepted name: legumain
Reaction: Hydrolysis of proteins and small molecule substrates at -Asn┼Xaa- bonds
Other name(s): asparaginyl endopeptidase; citvac; proteinase B (ambiguous); hemoglobinase (ambiguous); PRSC1 gene product (Homo sapiens); vicilin peptidohydrolase; bean endopeptidase; vicilin peptidohydrolase
Comments: Best known from legume seeds, the trematode Schistosoma mansoni and mammalian lysosomes. Not inhibited by compound E-64. Type example of peptidase family C13
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 149371-18-6
References:
1.  Hara-Nishimura, I. Asparaginyl endopeptidase. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 746–749.
2.  Dalton, J.P. and Brindley, P.J. Schistosome legumain. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 749–754.
3.  Chen, J.-M., Rawlings, N.D., Stevens, R.A.E. and Barrett, A.J. Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases. FEBS Lett. 441 (1998) 361–365. [DOI] [PMID: 9891971]
[EC 3.4.22.34 created 1992, modified 2000]
 
 
EC 3.4.22.35     
Accepted name: histolysain
Reaction: Hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg┼ in small molecule substrates including Z-Arg-Arg┼NHMec
Other name(s): histolysin; histolysin; Entamoeba histolytica cysteine proteinase; amebapain; Entamoeba histolytica cysteine protease; Entamoeba histolytica neutral thiol proteinase
Comments: From the protozoan, Entamoeba histolytica. In peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 92228-52-9
References:
1.  Lushbaugh, W.B., Hofbauer, A.F. and Pittman, F.E. Entamoeba histolytica: purification of cathepsin B. Exp. Parasitol. 59 (1985) 328–336. [PMID: 2860002]
2.  Luaces, A.L. and Barrett, A.J. Affinity purification and biochemical characterization of histolysin: the major cysteine proteinase of Entamoeba histolytica. Biochem. J. 250 (1988) 903–909. [PMID: 2898937]
[EC 3.4.22.35 created 1992]
 
 
EC 3.4.22.36     
Accepted name: caspase-1
Reaction: Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp┼
Other name(s): interleukin 1β-converting enzyme; protease VII; protease A; interleukin 1β precursor proteinase; interleukin 1 converting enzyme; interleukin 1β-converting endopeptidase; interleukin-1β convertase; interleukin-1β converting enzyme; interleukin-1β precursor proteinase; prointerleukin 1β protease; precursor interleukin-1β converting enzyme; pro-interleukin 1β proteinase; ICE
Comments: From mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation [6,7]. Cleaves pro-interleukin-1β (pro-IL-1β) to form mature IL-1β, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-γ-inducing factor [6]. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mice, whereas caspase-4 enhances its activation in humans [7]. Belongs in peptidase family C14.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 122191-40-6
References:
1.  Howard, A., Kostura, M.J., Thornberry, N., Ding, G.J.., Limjuco, G., Weidner, J., Salley, J.P., Hogquist, K.A., Chaplin, D.D., Mumford, R.A., Schmidt, J.A. and Tocci, M.J. IL-1 converting enzyme requires aspartic acid residues for processing of the IL-1β precursor at two distinct sites and does not cleave 31-kDa IL-1α. J. Immunol. 147 (1991) 2964–2969. [PMID: 1919001]
2.  Thornberry, N.A., Bull, H.G., Calaycay, J.R., Chapman, K.T., Howard, A.D., Kostura, M.J., Miller, D.K., Molineaux, S.M., Weidner, J.R., Aunins, J., Elliston, K.O., Ayala, J.M., Casano, F J., Chin, J., Ding, G.J.-F., Egger, L.A., Gaffney, E.P., Limjuco, G., Palyha, O.C., Raju, S.M., Rolando, A.M., Salley, J.P., Yamin, T.-T. and Tocci, M.J. A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes. Nature 356 (1992) 768–774. [DOI] [PMID: 1574116]
3.  Thornberry, N.A. Interleukin-1β converting enzyme. Methods Enzymol. 244 (1994) 615–631. [PMID: 7845238]
4.  Alnemri, E.S., Livingston, D.J., Nicholson, D.W., Salvesen, G., Thornberry, N.A., Wong, W.W. and Yuan, J.Y. Human ICE/CED-3 protease nomenclature. Cell 87 (1996) 171. [DOI] [PMID: 8861900]
5.  Margolin, N., Raybuck, S.A., Wilson, K.P., Chen, W.Y., Fox, T., Gu, Y. and Livingston, D.J. Substrate and inhibitor specificity of interleukin-1β-converting enzyme and related caspases. J. Biol. Chem. 272 (1997) 7223–7228. [DOI] [PMID: 9054418]
6.  Martinon, F. and Tschopp, J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 117 (2004) 561–574. [DOI] [PMID: 15163405]
7.  Chang, H.Y. and Yang, X. Proteases for cell suicide: functions and regulation of caspases. Microbiol. Mol. Biol. Rev. 64 (2000) 821–846. [PMID: 11104820]
[EC 3.4.22.36 created 1993, modified 1997, modified 2007]
 
 
EC 3.4.22.37     
Accepted name: gingipain R
Reaction: Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1
Other name(s): Arg-gingipain; gingipain-1; argingipain; Arg-gingivain-55 proteinase; Arg-gingivain-70 proteinase; Arg-gingivain-75 proteinase; arginine-specific cysteine protease; arginine-specific gingipain; arginine-specific gingivain; RGP-1; RGP
Comments: A secreted endopeptidase from the bacterium Porphyromonas gingivalis. Strongly activated by glycine [1], and stabilized by Ca2+. Precursor molecule contains a hemagglutinin domain [2,3]. Misleadingly described in some literature as "trypsin-like", being a cysteine peptidase, type example of family C25
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 159745-71-8
References:
1.  Chen, Z., Potempa, J., Polanowski, A., Wikstrom, M. and Travis, J. Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis. J. Biol. Chem. 267 (1992) 18896–18901. [PMID: 1527017]
2.  Kirszbaum, L., Sotiropoulos, C., Jackson, C., Cleal, S., Slakeski, N. and Reynolds, E.C. Complete nucleotide sequence of a gene prtR of Porphyromonas gingivalis W50 encoding a 132 kDa protein that contains an arginine-specific thiol endopeptidase domain and a haemagglutinin domain. Biochem. Biophys. Res. Commun. 207 (1995) 424–431. [DOI] [PMID: 7857299]
3.  Pavloff, N., Potempa, J., Pike, R.N., Prochazka, V., Kiefer, M.C., Travis, J. and Barr, P.J. Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein. J. Biol. Chem. 270 (1995) 1007–1010. [DOI] [PMID: 7836351]
[EC 3.4.22.37 created 1996]
 
 
EC 3.4.22.38     
Accepted name: cathepsin K
Reaction: Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg
Other name(s): cathepsin O and cathepsin X (both misleading, having been used for other enzymes); cathepsin O2
Comments: Prominently expressed in mammalian osteoclasts, and believed to play a role in bone resorption. In peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 94716-09-3
References:
1.  Inaoka, T., Bilbe, G., Ishibashi, O., Tezuka, K., Kumegawa, M. and Kokubo, T. Molecular cloning of human cDNA for cathepsin K: Novel cysteine proteinase predominantly expressed in bone. Biochem. Biophys. Res. Commun. 206 (1995) 89–96. [DOI] [PMID: 7818555]
2.  Bossard, M.J., Tomaszek, T.A., Thompson, S.K., Amegadzie, B.Y., Hanning, C.R., Jones, C., Kurdyla, J.T., McNulty, D.E., Drake, F.H., Gowen, M. and Levy, M.A. Proteolytic activity of human osteoclast cathepsin K - Expression, purification, activation, and substrate identification. J. Biol. Chem. 271 (1996) 12517–12524. [DOI] [PMID: 8647860]
3.  Bromme, D., Klaus, J.L., Okamoto, K., Rasnick, D. and Palmer, J.T. Peptidyl vinyl sulphones: A new class of potent and selective cysteine protease inhibitors - S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L. Biochem. J. 315 (1996) 85–89. [PMID: 8670136]
4.  Zhao, B.G., Janson, C.A., Amegadzie, B.Y., D'Alessio, K., Griffin, C., Hanning, C.R., Jones, C., Kurdyla, J., McQueney, M., Qiu, X.Y., Smith, W.W. and Abdel-Meguid, S.S. Crystal structure of human osteoclast cathepsin K complex with E-64. Nature Struct. Biol. 4 (1997) 109–111. [PMID: 9033588]
5.  McGrath, M.E., Klaus, J.L., Barnes, M.G. and Brömme, D. Crystal structure of human cathepsin K complexed with a potent inhibitor. Nature Struct. Biol. 4 (1997) 105–109. [PMID: 9033587]
[EC 3.4.22.38 created 1997]
 
 
EC 3.4.22.39     
Accepted name: adenain
Reaction: Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly┼Xaa- and -Yaa-Xaa-Gly-Xaa┼Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid)
Comments: A cysteine endopeptidase from adenoviruses, the type example of peptidase family C5, with a protein fold unlike that known for any other peptidase [2]. Activity is greatly stimulated by the binding to the enzyme of an 11-residue peptide from the adenovirus capsid protein pre-VI at a site separate from the active site [1]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 369652-03-9
References:
1.  Webster, A., Hay, R.T. and Kemp, G. The adenovirus protease is activated by a virus-coded disulphide-linked peptide. Cell 72 (1993) 274–275. [DOI] [PMID: 8422686]
2.  Ding, J.Z., McGrath, W.J., Sweet, R.M. and Mangel, W.F. Crystal structure of the human adenovirus proteinase with its 11 residue cofactor. EMBO J. 15 (1996) 1778–1783. [PMID: 8617222]
3.  Weber, J.M. Adenovirus protease. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 741–743.
[EC 3.4.22.39 created 2000]
 
 
EC 3.4.22.40     
Accepted name: bleomycin hydrolase
Reaction: Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of β-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred [1]
Other name(s): aminopeptidase C (Lactococcus lactis) [4]
Comments: The molecule is a homohexamer in which the monomers have a papain-like tertiary structure (in peptidase family C1). The active sites are on the walls of a central channel through the molecule, and access of substrate molecules to them is obstructed by this and by the C-terminus of each polypeptide chain [3]. Bleomycin can scarcely be the natural substrate, and there are reports of limited endopeptidase activity. Known from bacteria as well as eukaryotic organisms. Hydrolase H from chicken muscle has many similarities to bleomycin hydrolase, but hydrolyses Ph-CO-Arg-2-naphthylamine as well as aminopeptidase substrates [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 53096-17-6
References:
1.  Brömme, D., Rossi, A.B., Smeekens, S.P., Anderson, D.C. & Payan, D.G. Human bleomycin hydrolase: molecular cloning, sequencing, functional expression, and enzymatic characterization. Biochemistry 35 (1996) 6706–6714. [DOI] [PMID: 8639621]
2.  Adachi, H., Tsujimoto, M., Fukasawa, M., Sato, Y., Arai, H., Inoue, K. and Nishimura, T. cDNA cloning and expression of chicken aminopeptidase H, possessing endopeptidase as well as aminopeptidase activity. Eur. J. Biochem. 245 (1997) 283–288. [DOI] [PMID: 9151954]
3.  Zheng, W., Johnston, S.A. & Joshua-Tor, L. The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase. Cell 93 (1998) 103–109. [DOI] [PMID: 9546396]
4.  Mistou, M.Y. & Gripon, J.C. Catalytic properties of the cysteine aminopeptidase PepC, a bacterial bleomycin hydrolase. Biochim. Biophys. Acta 1383 (1998) 63–70. [DOI] [PMID: 9546047]
[EC 3.4.22.40 created 2000]
 
 
EC 3.4.22.41     
Accepted name: cathepsin F
Reaction: The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (kcat/Km) comparable to that of cathepsin L
Comments: Cathepsin F is a lysosomal cysteine endopeptidase of family C1 (papain family), most active at pH 5.9. The enzyme is unstable at neutral pH values and is inhibited by compound E-64. Cathepsin F is expressed in most tissues of human, mouse and rat. Human gene locus: 11q13.1-13.3
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 65997-74-2
References:
1.  Santamaría, I., Velasco, G., Pendás, A.M., Paz, A. and López-Otín, C. Molecular cloning and structural and functional chararcterization of cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J. Biol. Chem. 274 (1999) 13800–13809. [DOI] [PMID: 10318784]
2.  Nägler, D.K. Sulea, T. and Ménard, R. Full length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen. Biochem. Biophys. Res. Commun. 257 (1999) 313–318. [DOI] [PMID: 10198209]
3.  Wex, T., Levy, B., Wex, H. and Brömme, D. Human cathepsins F and W: A new subgroup of cathepsins. Biochem. Biophys. Res. Commun. 259 (1999) 401–407. [DOI] [PMID: 10362521]
4.  Wang, B., Shi, G.-P., Yao, P.M., Li, Z., Chapman, H.A. and Brömme, D. Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. J. Biol. Chem. 273 (1998) 32000–32008. [DOI] [PMID: 9822672]
[EC 3.4.22.41 created 2000]
 
 
EC 3.4.22.42     
Accepted name: cathepsin O
Reaction: The recombinant human enzyme hydrolyses synthetic endopeptidase substrates including Z-Phe-Arg-NHMec and Z-Arg-Arg-NHMec
Comments: Cathepsin O is a lysosomal cysteine peptidase of family C1 (papain family). The recombinant human enzyme is catalytically active at pH 6.0 and is inhibited by compound E-64. Cathepsin O is ubiquitously expressed in human tissues and the human gene locus is 4q31-32
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 162032-86-2
References:
1.  Santamaría, I., Pendás, A.M. and López-Otín, C. Genomic structure and chromosomal localization of a human cathepsin O gene (CTSO). Genomics 53 (1998) 231–234. [DOI] [PMID: 9790772]
2.  Velasco, G., Ferrando, A.A., Puente, X.S., Sanchez, L.M. and López-Otín, C. Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in human tissues. J. Biol. Chem. 269 (1994) 27136–27142. [PMID: 7929457]
[EC 3.4.22.42 created 2000]
 
 
EC 3.4.22.43     
Accepted name: cathepsin V
Reaction: The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec)
Other name(s): Cathepsin L2; cathepsin U
Comments: Cathepsin V is a human lysosomal cysteine endopeptidase of family C1 (papain family) that is maximally active at pH 5.7 and unstable at neutral pH. Compound E-64, leupeptin and chicken cystatin are inhibitors. Human cathepsin V shows expression restricted to thymus, testis, corneal epithelium and some colon and breast carcinomas. Human gene locus: 9q22.2
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 223670-00-6
References:
1.  Brömme, D., Li, Z., Barnes, M. and Mehler, E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry 38 (1999) 2377–2385. [DOI] [PMID: 10029531]
2.  Adachi, W., Kawamoto, S., Ohno, I., Nishida, K., Kinoshita, S., Matsubara, K. and Okubo, K. Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium. Invest. Ophthalmol. Vis. Sci. 39 (1998) 1789–1796. [PMID: 9727401]
3.  Santamaría, I., Velasco, G., Cazorla, M., Fueyo, A., Campo, E. and López-Otín, C. Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer Res. 58 (1998) 1624–1630. [PMID: 9563472]
[EC 3.4.22.43 created 2000]
 
 
EC 3.4.22.44     
Accepted name: nuclear-inclusion-a endopeptidase
Reaction: Hydrolyses glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1′ that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln┼(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
Other name(s): potyvirus NIa protease
Comments: The potyviruses cause diseases in plants, and inclusion bodies appear in the host cell nuclei; protein a of the inclusion bodies is the endopeptidase. The enzyme finds practical use when encoded in vectors for the artificial expression of recombinant fusion proteins, since it can confer on them the capacity for autolytic cleavage. It is also reported that transgenic plants expressing the enzyme are resistant to viral infection. Type example of peptidase family C4.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 139946-51-3
References:
1.  Fellers, J.P., Collins, G.B. and Hunt, A.G. The NIa-proteinase of different plant potyviruses provides specific resistance to viral infection. Crop Sci. 38 (1998) 1309–1319.
2.  Kim, D.-H. and Choi, K.Y. Potyvirus NIa protease. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 721–723.
3.  Takahashi, T., Nakanishi, M., Yao, Y., Uyeda, I. and Serizawa, N. Direct formation of human interleukin-11 by cis-acting system of plant virus protease in Escherichia coli. Biosci. Biotechnol. Biochem. 62 (1998) 953–958. [PMID: 9648226]
4.  Kim, D.H., Hwang, D.C., Kang, B.H., Lew, J., Han, J.S., Song, B.O.D. and Choi, K.Y. Effects of internal cleavages and mutations in the C-terminal region of NIa protease of turnip mosaic potyvirus on the catalytic activity. Virology 226 (1996) 183–190. [DOI] [PMID: 8955037]
[EC 3.4.22.44 created 2000]
 
 
EC 3.4.22.45     
Accepted name: helper-component proteinase
Reaction: Hydrolyses a Gly┼Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly┼Gly, in the processing of the potyviral polyprotein
Other name(s): HC-Pro
Comments: Known from many potyviruses. The helper component-proteinase of the tobacco etch virus is a multifunctional protein with several known activities: the N-terminal region is required for aphid transmission and efficient genome amplification, the central region is required for long-distance movement in plants, and the C-terminal domain has cysteine endopeptidase activity. Type example of peptidase family C6.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 124566-20-7
References:
1.  Kasschau, K.D. and Carrington, J.C. Requirement for HC-Pro processing during genome amplification of tobacco etch potyvirus. Virology 209 (1995) 268–273. [DOI] [PMID: 7747479]
2.  Verchot, J. Potyvirus helper component proteinase. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds), Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes, London, 1998, pp. 677–679.
[EC 3.4.22.45 created 2001]
 
 
EC 3.4.22.46     
Accepted name: L-peptidase
Reaction: Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys┼Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly┼Arg- and -Lys┼Arg-
Comments: Best known from foot-and-mouth disease virus, but occurs in other aphthoviruses and cardioviruses. Destruction of initiation factor eIF-4G has the effect of shutting off host-cell protein synthesis while allowing synthesis of viral proteins to continue. The tertiary structure reveals a distant relationship to papain and, consistent with this, compound E-64 is inhibitory. Type example of peptidase family C28.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Piccone, M.E., Zellner, M., Kumosinski, T.F., Mason, P.W. and Grubman, M.J. Identification of the active-site residues of the L proteinase of foot-and-mouth disease virus. J. Virol. 69 (1995) 4950–4956. [PMID: 7609064]
2.  Guarné, A., Hampoelz, B., Glaser, W., Carpena, X., Torma, J., Fita, I. and Skern, T. Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes. J. Mol. Biol. 302 (2000) 1227–1240. [DOI] [PMID: 11183785]
[EC 3.4.22.46 created 2001]
 
 
EC 3.4.22.47     
Accepted name: gingipain K
Reaction: Endopeptidase with strict specificity for lysyl bonds
Other name(s): Lys-gingipain; PrtP proteinase
Comments: Activity is stimulated by glycine. Known from the bacterium Porphyromonas gingivalis and contributes to the pathogenicity of the organism. In peptidase family C25.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, SWISSPROT, CAS registry number: 159745-69-4
References:
1.  Pike, R., McGraw, W., Potempa, J. and Travis, J. Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins. J. Biol. Chem. 269 (1994) 406–411. [PMID: 8276827]
2.  Curtis, M.A., Aduse, O.J., Rangarajan, M., Gallagher, A., Sterne, J.A., Reid, C.R., Evans, H.E. and Samuelsson, B. Attenuation of the virulence of Porphyromonas gingivalis by using a specific synthetic Kgp protease inhibitor 2. Infect. Immun. 70 (2002) 6968–6975. [DOI] [PMID: 12438376]
[EC 3.4.22.47 created 2003]
 
 
EC 3.4.22.48     
Accepted name: staphopain
Reaction: Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate
Other name(s): staphylopain
Comments: Known from species of Staphylococcus. Type example of peptidase family C47.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, SWISSPROT, CAS registry number: 347841-89-8
References:
1.  Hofmann, B., Hecht, H.J., Kiess, M. and Schomburg, D. Crystal structure of a thiol proteinase from Staphylococcus aureus V8 in the E-64 inhibitor complex. Acta Crystallogr. Sect. A (Suppl.) 49 (1993) 102.
2.  Potempa, J., Dubin, A. and Travis, J. Staphylopain. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds), Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes, London, 1998, pp. 669–671.
3.  Dubin, G., Chmiel, D., Mak, P., Rakwalska, M., Rzychon, M. and Dubin, A. Molecular cloning and biochemical characterisation of proteases from Staphylococcus epidermidis. Biol. Chem. 382 (2001) 1575–1582. [DOI] [PMID: 11767947]
[EC 3.4.22.48 created 2003]
 
 
EC 3.4.22.49     
Accepted name: separase
Reaction: All bonds known to be hydrolysed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage
Other name(s): separin
Comments: In both budding yeast and human cells, cleavage of the cohesin subunit Scc1 by separase is required for sister chromatid separation in mitosis. Budding yeast separase is also known to cleave the Rec8 subunit of a meiotic cohesin complex and the kinetochore protein Slk19. Type example of peptidase family C50.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, SWISSPROT, CAS registry number: 351527-77-0
References:
1.  Waizenegger, I., Gimenez-Abian, J., Wernic, D. and Peters, J. Regulation of human separase by securin binding and autocleavage. Curr. Biol. 12 (2002) 1368–1378. [DOI] [PMID: 12194817]
[EC 3.4.22.49 created 2003]
 
 
EC 3.4.22.50     
Accepted name: V-cath endopeptidase
Reaction: Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B
Other name(s): AcNPV protease; BmNPV protease; NPV protease; baculovirus cathepsin; nucleopolyhedrosis virus protease; viral cathepsin
Comments: In peptidase family C1. Contributes to the liquefaction of the tissues of the insect host in the late stages of infection by the baculovirus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, SWISSPROT, CAS registry number: 316365-69-2
References:
1.  Slack, J.M., Kuzio, J. and Faulkner, P. Characterization of V-cath, a cathepsin L-like proteinase expressed by the baculovirus Autographa californica multiple nuclear polyhedrosis-virus. J. Gen. Virol. 76 (1995) 1091–1098. [DOI] [PMID: 7730794]
2.  Hawtin, R.E., Zarkowska, T., Arnold, K., Thomas, C.J., Gooday, G.W., King, L.A., Kuzio, J.A. and Possee, R.D. Liquefaction of Autographa californica nucleopolyhedrovirus-infected insects is dependent on the integrity of virus-encoded chitinase and cathepsin genes. Virology 238 (1997) 243–253. [DOI] [PMID: 9400597]
[EC 3.4.22.50 created 2003]
 
 


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