The Enzyme Database

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EC 3.4.24.1     
Accepted name: atrolysin A
Reaction: Cleavage of Asn3┼Gln, His5┼Leu, His10┼Leu, Ala14┼Leu and Tyr16┼Leu in insulin B chain; removes C-terminal Leu from small peptides
Other name(s): Crotalus atrox metalloendopeptidase a; hemorrhagic toxin a; Crotalus atrox α-proteinase; Crotalus atrox proteinase; bothropasin
Comments: A hemorrhagic endopeptidase of 68 kDa, one of six hemorrhagic toxins in the venom of western diamondback rattlesnake. The 60 kDa hemorrhagic toxin 1 of Crotalus ruber ruber shows identical specificity [2]. In peptidase family M12 (astacin family). Related metalloendopeptidases from rattlesnake venoms are EC 3.4.24.41 (atrolysin B), EC 3.4.24.42 (atrolysin C), EC 3.4.24.43 (atroxase), EC 3.4.24.44 (atrolysin E), EC 3.4.24.45 (atrolysin F), EC 3.4.24.46 (adamalysin), EC 3.4.24.47 (horrilysin), and EC 3.4.24.48 (ruberlysin)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 37288-82-7
References:
1.  Bjarnason, J.B. and Tu, A.T. Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e. Biochemistry 17 (1978) 3395–3404. [PMID: 210790]
2.  Mori, N., Nikai, T., Sugihara, H. and Tu, A.T. Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom. Arch. Biochem. Biophys. 253 (1987) 108–121. [DOI] [PMID: 2949699]
3.  Bjarnason, J.B., Hamilton, D. and Fox, J.W. Studies on the mechanism of hemorrhage production by five proteolytic hemorrhagic toxins from Crotalus atrox venom. Biol. Chem. Hoppe-Seyler 369 (1988) 121–129. [PMID: 3060135]
4.  Bjarnason, J.B. and Fox, J.W. Hemorrhagic toxins from snake venoms. J. Toxicol. Toxin Rev. 7 (1989) 121–209.
[EC 3.4.24.1 created 1972, modified 1986]
 
 
EC 3.4.24.2      
Deleted entry: Sepia proteinase
[EC 3.4.24.2 created 1972, deleted 1992]
 
 
EC 3.4.24.3     
Accepted name: microbial collagenase
Reaction: Digestion of native collagen in the triple helical region at ┼Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1′, Pro and Ala at P2 and P2′, and hydroxyproline, Ala or Arg at P3′
Other name(s): Clostridium histolyticum collagenase; clostridiopeptidase A; collagenase A; collagenase I; Achromobacter iophagus collagenase; collagenase; aspergillopeptidase C; nucleolysin; azocollase; metallocollagenase; soycollagestin; Clostridium histolyticum proteinase A; clostridiopeptidase II; MMP-8; clostridiopeptidase I; collagen peptidase; collagen protease; collagenase MMP-1; metalloproteinase-1; kollaza; matrix metalloproteinase-1; MMP-1; matrix metalloproteinase-8; matirx metalloproteinase-18; interstitial collagenase
Comments: Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. Class I has forms α (68 kDa), β (115 kDa) and γ (79 kDa); class II has δ (100 kDa), ε (110 kDa) and ζ (125 kDa). The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. The enzymes also act as peptidyl-tripeptidases. Variants of the enzyme have been purified from Bacillus cereus [10], Empedobacter collagenolyticum [4], Pseudomonas marinoglutinosa [1], and species of Vibrio, Vibrio B-30 (ATCC 21250) [2] and V. alginolyticus (previously Achromobacter iophagus) [3,8]. Also known from Streptomyces sp. [9]. The Vibrio enzyme is the type example of peptidase family M9.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9001-12-1
References:
1.  Hanada, K., Mizutani, T., Yamagishi, M., Tsuji, H., Misaki, T. Sawada, J. The isolation of collagenase and its enzymological and physico-chemical properties. Agric. Biol. Chem. 37 (1973) 1771–1781.
2.  Merkel, J.R. and Dreisbach, J.H. Purification and characterization of a marine bacterial collagenase. Biochemistry 17 (1978) 2857–2863. [PMID: 210785]
3.  Heindl, M.-C., Fermandjian, S. and Keil, B. Circular dichroism comparative studies of two bacterial collagenases and thermolysin. Biochim. Biophys. Acta 624 (1980) 51–59. [DOI] [PMID: 6250633]
4.  Labadie, J. and Montel, M..-C. Purification et étude de quelques propriétés d’une collagénase produite par Empedobacter collagenolyticum. Biochimie 64 (1982) 49–54. [PMID: 6530724]
5.  Bond, M.D and Van Wart, H.D. Characterization of the individual collagenases from Clostridium histolyticum. Biochemistry 23 (1984) 3085–3091. [PMID: 6087888]
6.  Bond, M.D. and Van Wart, H.D. Relationship between the individual collagenases of Clostridium histolyticum: evidience for evolution by gene duplication. Biochemistry 23 (1984) 3092–3099. [PMID: 6087889]
7.  Van Wart, H.D. and Steinbrink, D.R. Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum. Biochemistry 24 (1985) 6520–6526. [PMID: 3002445]
8.  Tong, N.T., Tsugita, A. and Keil-Dlouha, V. Purification and characterization of two high-molecular-mass forms of Achromobacter collagenase. Biochim. Biophys. Acta 874 (1986) 296–304.
9.  Endo, A., Murakawa, S., Shimizu, H. and Shiraishi, Y. Purification and properties of collagenase from a Streptomyces species. J. Biochem. (Tokyo) 102 (1987) 163–170. [PMID: 2822678]
10.  Makinen, K.K. and Makinen, P.-L. Purification and properties of an extracellular collagenolytic protease produced by the human oral bacterium Bacillus cereus (strain Soc 67). J. Biol. Chem. 262 (1987) 12488–12495. [PMID: 3040751]
[EC 3.4.24.3 created 1961 as EC 3.4.4.19, transferred 1972 to EC 3.4.24.3 (EC 3.4.24.8 created 1978, incorporated 1992, EC 3.4.99.5 created 1972, incorporated 1978)]
 
 
EC 3.4.24.4      
Transferred entry: now EC 3.4.24.40 serralysin
[EC 3.4.24.4 created 1972 [EC 3.4.99.13 and EC 3.4.99.22 both created 1972, incorporated 1978], deleted 1992]
 
 
EC 3.4.24.5      
Deleted entry:  lens neutral proteinase. Now included with EC 3.4.22.53 (calpain-2) and EC 3.4.25.1 (proteasome endopeptidase complex)
[EC 3.4.24.5 created 1978, deleted 1989]
 
 
EC 3.4.24.6     
Accepted name: leucolysin
Reaction: Cleavage of Phe1┼Val, His5┼Leu, Ala14┼Leu, Gly20┼Glu, Gly23┼Phe and Phe24┼Phe bonds in insulin B chain as well as N-blocked dipeptides
Other name(s): Leucostoma neutral proteinase; Leucostoma peptidase A
Comments: From the venom of the western cottonmouth moccasin snake (Agkistrodon piscivorus leucostoma).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72561-03-6
References:
1.  Wagner, F.W., Spiekerman, A.M. and Prescott, J.M. Leucostoma peptidase A. Isolation and physical properties. J. Biol. Chem. 243 (1968) 4486–4493. [PMID: 5684005]
2.  Spiekerman, A.M., Fredericks, K.K., Wagner, F.W. and Prescott, J.M. Leucostoma peptidase A: a metalloprotease from snake venom. Biochim. Biophys. Acta 293 (1973) 464–475. [DOI] [PMID: 4711816]
[EC 3.4.24.6 created 1978]
 
 
EC 3.4.24.7     
Accepted name: interstitial collagenase
Reaction: Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at Gly775┼Ile in the α1(I) chain. Cleaves synthetic substrates and α-macroglobulins at bonds where P1′ is a hydrophobic residue
Other name(s): vertebrate collagenase; matrix metalloproteinase 1
Comments: The enzyme takes its name from substrates of the interstitial collagen group - types I, II and III, all of which are cleaved in the helical domain. However, α-macroglobulins are cleaved much more rapidly. The enzyme is widely distributed in vertebrate animals. Type example of peptidase family M10
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9001-12-1
References:
1.  Goldberg, G.I., Wilhelm, S.M., Kronberger, A., Bauer, E.A., Grant, G.A. and Eisen, A.Z. Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein. J. Biol. Chem. 261 (1986) 6600–6605. [PMID: 3009463]
2.  Birkedal-Hansen, H. Catabolism and turnover of collagens: collagenases. Methods Enzymol. 144 (1987) 140–171. [DOI] [PMID: 3041177]
3.  Fields, G.B., Van Wart, H.E. and Birkedal-Hansen, H. Sequence specificity of human skin fibroblast collagenase. Evidence for the role of collagen structure in determining the collagenase cleavage site. J. Biol. Chem. 262 (1987) 6221–6226. [PMID: 3032960]
4.  Sottrup-Jensen, L. and Birkedal-Hansen, H. Human fibroblast collagenase-α-macroglobulin interactions. Localization of cleavage sites in the bait regions of five mammalian α-macroglobulins. J. Biol. Chem. 264 (1989) 393–401. [PMID: 2462561]
[EC 3.4.24.7 created 1978]
 
 
EC 3.4.24.8      
Transferred entry: Achromobacter iophagus collagenase. Now EC 3.4.24.3, microbial collagenase
[EC 3.4.24.8 created 1978, deleted 1992]
 
 
EC 3.4.24.9      
Deleted entry:  Trichophyton schoenleinii collagenase
[EC 3.4.24.9 created 1978, deleted 1992]
 
 
EC 3.4.24.10      
Deleted entry: Trichophyton mentagrophytes keratinase
[EC 3.4.24.10 created 1972 as EC 3.4.99.12, transferred 1978 to EC 3.4.24.10, deleted 1992]
 
 
EC 3.4.24.11     
Accepted name: neprilysin
Reaction: Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1′
Other name(s): neutral endopeptidase; endopeptidase 24.11; kidney-brush-border neutral peptidase; enkephalinase (misleading); endopeptidase-2; CALLA (common acute lymphoblastic leukemia-associated) antigens; CALLA antigen; endopeptidase; membrane metalloendopeptidase; kidney-brush-border neutral endopeptidase; kidney-brush-border neutral proteinase; endopeptidase-2; CALLA glycoprotein; CALLA; common acute lymphoblastic leukemia antigen; CALLA glycoproteins; common acute lymphoblastic leukemia-associated antigens; neutral metallendopeptidase; membrane metalloendopeptidase; NEP; neutral endopeptidase 24.11; CD10; neutral endopeptidase; acute lymphoblastic leukemia antigen
Comments: A membrane-bound glycoprotein widely distributed in animal tissues. Inhibited by phosphoramidon and thiorphan. Common acute lymphoblastic leukemia antigen (CALLA). Type example of peptidase family M13
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 82707-54-8
References:
1.  Matsas, R., Fulcher, I.S., Kenny, A.J. and Turner, A.J. Substance P and [Leu]enkephalin are hydrolyzed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli. Proc. Natl Acad. Sci. USA 80 (1983) 3111–3115. [DOI] [PMID: 6190172]
2.  Malfroy, B., Schofield, P.R., Kuang, W.-J., Seeburg, P.H., Mason, A.J. Henzel, W.J. Molecular cloning and amino acid sequence of rat enkephalinase. Biochem. Biophys. Res. Commun. 144 (1987) 59–66. [DOI] [PMID: 3555489]
3.  Letarte, M., Vera, S., Tran, R., Addis, J.B.L., Onizuka, R.J., Quackenbush, E J., Jongneel, C.V. and McInnes, R.R. Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase. J. Exp. Med. 168 (1988) 1247–1253. [PMID: 2971756]
4.  Erdös, E.G. and Skidgel, R.A. Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones. FASEB J. 3 (1989) 145–151. [PMID: 2521610]
[EC 3.4.24.11 created 1978, modified 1989]
 
 
EC 3.4.24.12     
Accepted name: envelysin
Reaction: Hydrolysis of proteins of the fertilization envelope and dimethylcasein
Other name(s): sea-urchin-hatching proteinase; hatching enzyme; chorionase; chorion-digesting proteinase; chymostrypsin; sea urchin embryo hatching enzyme
Comments: A glycoprotein from various members of the class Echinoidea. Extracellular enzyme requiring Ca2+. In peptidase family M10 (interstitial collagenase family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 50812-13-0
References:
1.  Barrett, D. and Edwards, B.F. Hatching enzyme of the sea urchin Strongylocentrotus purpuratus. Methods Enzymol. 45 (1976) 354–373. [DOI] [PMID: 1012003]
2.  Lepage, T. and Gache, C. Purification and characterization of the sea urchin embryo hatching enzyme. J. Biol. Chem. 264 (1989) 4787–4793. [PMID: 2925668]
3.  Lepage, T. and Gache, C. Early expression of a collagenase-like hatching enzyme gene in the sea urchin embryo. EMBO J. 9 (1990) 3003–3012. [PMID: 2167841]
4.  Nomura, K., Tanaka, H., Kikkawa, Y., Yamaguchi, M. and Suzuki, N. The specificity of sea urchin hatching enzyme (envelysin) places it in the mammalian matrix metalloproteinase family. Biochemistry 30 (1991) 6115–6123. [PMID: 1711895]
[EC 3.4.24.12 created 1978]
 
 
EC 3.4.24.13     
Accepted name: IgA-specific metalloendopeptidase
Reaction: Cleavage of Pro┼Thr bond in the hinge region of the heavy chain of human IgA
Other name(s): immunoglobulin A1 proteinase; IgA protease; IgA1-specific proteinase; IgA1 protease; IgA1 proteinase
Comments: A 190 kDa enzyme found in several pathogenic species of Streptococcus such as sanguis and pneumoniae. Type example of peptidase family M26. There is also an IgA-specific prolyl endopeptidase of the serine-type (see EC 3.4.21.72, IgA-specific serine endopeptidase)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 72231-73-3
References:
1.  Kornfeld, S.J. and Plaut, A.G. Secretory immunity and the bacterial IgA proteases. Rev. Infect. Dis. 3 (1981) 521–534. [PMID: 6792682]
2.  Gilbert, J.V., Plaut, A.G. and Wright, A. Analysis of the immunoglobulin A protease gene of Streptococcus sanguis. Infect. Immun. 59 (1991) 7–17. [PMID: 1987065]
3.  Gilbert, J.V., Plaut, A.G., Fishman, Y. and Wright, A. Cloning of the gene encoding streptococcal immunoglobulin A protease and its expression in Escherichia coli. Infect. Immun. 56 (1988) 1961–1966. [PMID: 3294181]
[EC 3.4.24.13 created 1984]
 
 
EC 3.4.24.14     
Accepted name: procollagen N-endopeptidase
Reaction: Cleaves the N-propeptide of collagen chain α1(I) at Pro┼Gln and of α1(II) and α2(I) at Ala┼Gln
Other name(s): procollagen N-terminal peptidase; procollagen aminopeptidase; aminoprocollagen peptidase; aminoterminal procollagen peptidase; procollagen aminoterminal protease; procollagen N-terminal proteinase; type I/II procollagen N-proteinase; type III procollagen
Comments: Removes the propeptides of type I and II collagens prior to fibril assembly. Does not act on type III collagen. In peptidase family M12 (astacin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 68651-94-5
References:
1.  Kohn, L.D., Iserky, C., Zupnik, J., Lenaers, A., Lee, G. and Lapiére, C.M. Calf tendon procollagen peptidase: its purification and endopeptidase mode of action. Proc. Natl. Acad. Sci. USA 71 (1974) 40–44. [DOI] [PMID: 4204204]
2.  Hojima, Y., McKenzie, J., van der Rest, M. and Prockop, D.J. Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptides. J. Biol. Chem. 264 (1989) 11336–11345. [PMID: 2500439]
[EC 3.4.24.14 created 1984]
 
 
EC 3.4.24.15     
Accepted name: thimet oligopeptidase
Reaction: Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3′ and a small residue at P1′ in substrates of 5-15 residues
Other name(s): Pz-peptidase; soluble metalloendopeptidase; endo-oligopeptidase A; tissue-endopeptidase degrading collagenase-synthetic-substrate
Comments: Thiol compounds activate at low concentrations. Type example of peptidase family M3.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 110639-28-6
References:
1.  Cicilini, M.A., Ribeiro, M.J.F., de Oliveira, E.B., Mortara, R.A. and de Camargo, A.C.M. Endooligopeptidase A activity in rabbit heart: generation of enkephalin from enkephalin containing peptides. Peptides (Fayetteville) 9 (1988) 945–955. [DOI] [PMID: 3244563]
2.  Orlowski, M., Reznik, S., Ayala, J. and Pierotti, A.R. Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptides, including enkephalin-containing peptides. Biochem. J. 261 (1989) 951–958. [PMID: 2803255]
3.  Barrett, A.J. and Brown, M.A. Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase. Biochem. J. 271 (1990) 701–706. [PMID: 2123097]
4.  Pierotti, A., Dong, K.W., Glucksman, M.J., Orlowski, M. and Roberts, J.L. Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15. Biochemistry 29 (1990) 10323–10329. [PMID: 2261476]
5.  Tisljar, U. and Barrett, A.J. Thiol-dependent metallo-endopeptidase characteristics of Pz-peptidase in rat and rabbit. Biochem. J. 267 (1990) 531–533. [PMID: 2185743]
[EC 3.4.24.15 created 1984 (EC 3.4.22.19 created 1989 and EC 3.4.99.31 created 1978 both incorporated 1992)]
 
 
EC 3.4.24.16     
Accepted name: neurolysin
Reaction: Preferential cleavage in neurotensin: Pro10┼Tyr
Other name(s): neurotensin endopeptidase; endopeptidase 24.16; endo-oligopeptidase B (proline-endopeptidase)
Comments: No absolute requirement for a prolyl bond: the enzyme acts on some peptides, such as dynorphin 1-8, that do not contain proline, and does not act on some others that do. In peptidase family M3 (thimet oligopeptidase family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 149371-24-4
References:
1.  Checler, F., Vincent, J.P. and Kitabgi, P. Purification and characterization of a novel neurotensin-degrading peptidase from rat brain synaptic membranes. J. Biol. Chem. 261 (1986) 11274–11281. [PMID: 3525564]
2.  Barelli, H., Vincent, J.-P. and Checler, F. Peripheral inactivation of neurotensin. Isolation and characterization of a metallopeptidase from rat ileum. Eur. J. Biochem. 175 (1988) 481–489. [DOI] [PMID: 3409880]
3.  Checler, F., Barelli, H. and Vincent, J.-P. Tissue distribution of a novel neurotensin-degrading metallopeptidase. An immunological approach using monospecific polyclonal antibodies. Biochem. J. 257 (1989) 549–554. [PMID: 2649078]
[EC 3.4.24.16 created 1989]
 
 
EC 3.4.24.17     
Accepted name: stromelysin 1
Reaction: Preferential cleavage where P1′, P2′ and P3′ are hydrophobic residues
Other name(s): matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein
Comments: An extracellular endopeptidase of vertebrate tissues homologous with interstitial collagenase. Digests proteoglycan, fibronectin, collagen types III, IV, V, IX, and activates procollagenase. In peptidase family M10 (interstitial collagenase family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 79955-99-0
References:
1.  Chin, J.R., Murphy, G. and Werb, Z. Stromelysin, a connective tissue-degrading metalloendopeptidase secreted by stimulated rabbit synovial fibroblasts in parallel with collagenase. Biosynthesis, isolation, characterization, and substrates. J. Biol. Chem. 260 (1985) 12367–12376. [PMID: 2995374]
2.  Okada, Y., Nagase, H. and Harris, E.D., Jr. A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization. J. Biol. Chem. 261 (1986) 14245–14255. [PMID: 3095317]
3.  Docherty, A.J.P. and Murphy, G. The tissue metalloproteinase family and the inhibitor TIMP: a study using cDNAs and recombinant proteins. Ann. Rheum. Dis. 49 (1990) 469–479. [PMID: 2197998]
4.  Emonard, H. and Grimaud, J.-A. Matrix metalloproteinase. A review. Cell. Mol. Biol. 36 (1990) 131–153. [PMID: 2165861]
[EC 3.4.24.17 created 1990]
 
 
EC 3.4.24.18     
Accepted name: meprin A
Reaction: Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues
Other name(s): endopeptidase-2; meprin-a; meprin; N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase; PABA-peptide hydrolase; PPH
Comments: A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts. Differences from neprilysin (EC 3.4.24.11 (astacin family). Formerly included in EC 3.4.24.11
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 148938-24-3
References:
1.  Beynon, R.J., Shannon, J.D. and Bond, J.S. Purification and characterization of a metallo-endoproteinase from mouse kidney. Biochem. J. 199 (1981) 591–598. [PMID: 7041888]
2.  Butler, P.E., McKay, M.J. and Bond, J.S. Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney. Biochem. J. 241 (1987) 229–235. [PMID: 3105525]
3.  Stephenson, S.L. and Kenny, A.J. The metabolism of neuropeptides. Hydrolysis of peptides by the phosphoramidon-insensitive rat kidney enzyme 'endopeptidase-2′ and by rat microvillar membranes. Biochem. J. 255 (1988) 45–51. [PMID: 2461706]
4.  Sterchi, E.E., Naim, H.Y., Lentze, M.J., Hauri, H.-P. Fransen, J.A.M. N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides. Arch. Biochem. Biophys. 265 (1988) 105–118. [DOI] [PMID: 3261961]
5.  Barnes, K., Ingram, J. and Kenny, A.J. Proteins of the kidney microvillar membrane. Structural and immunochemical properties of rat endopeptidase-2 and its immunohistochemical localization in tissues of rat and mouse. Biochem. J. 264 (1989) 335–346. [PMID: 2690825]
[EC 3.4.24.18 created 1992]
 
 
EC 3.4.24.19     
Accepted name: procollagen C-endopeptidase
Reaction: Cleavage of the C-terminal propeptide at Ala┼Asp in type I and II procollagens and at Arg┼Asp in type III
Other name(s): procollagen C-terminal proteinase; carboxyprocollagen peptidase; procollagen C-terminal peptidase; procollagen C-proteinase; procollagen C-terminal proteinase; procollagen carboxypeptidase; procollagen carboxy-terminal proteinase; procollagen peptidase
Comments: A 100 kDa endopeptidase the activity of which is increased by Ca2+ and by an enhancer glycoprotein. In peptidase family M12 (astacin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 68651-95-6
References:
1.  Hojima, Y., van der Rest, M. and Prockop, D.J. Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization. J. Biol. Chem. 260 (1985) 15996–16003. [PMID: 3905801]
2.  Kessler, E. and Adar, R. Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55-kDa enhancer glycoprotein. Eur. J. Biochem. 186 (1989) 115–121. [PMID: 2689170]
[EC 3.4.24.19 created 1992]
 
 
EC 3.4.24.20     
Accepted name: peptidyl-Lys metalloendopeptidase
Reaction: Preferential cleavage in proteins: -Xaa┼Lys- (in which Xaa may be Pro)
Other name(s): Armillaria mellea neutral proteinase; peptidyllysine metalloproteinase
Comments: From the honey fungus Armillaria mellea. In peptidase family M35 (deuterolysin family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 65979-41-1
References:
1.  Doonan S, Doonan HJ, Hanford R, Vernon CA, Walker JM, da Airold LP, Bossa F, Barra D, Carloni M, Fasella P, Riva F. The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues. Biochem. J. 149 (1975) 497–506. [PMID: 1239277]
2.  Lewis, W.G., Basford, J.M. and Walton, P.L. Specificity and inhibition studies of Armillaria mellea protease. Biochim. Biophys. Acta 522 (1978) 551–560. [DOI] [PMID: 23849]
[EC 3.4.24.20 created 1978 as EC 3.4.99.32, transferred 1992 to EC 3.4.24.20 (EC 3.4.99.30 created 1978, incorporated 1992)]
 
 
EC 3.4.24.21     
Accepted name: astacin
Reaction: Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1′, and Pro in P2′
Other name(s): Astacus proteinase; crayfish small-molecule proteinase
Comments: A 22.6 kDa digestive endopeptidase from the cardia of the crayfish Astacus fluviatilis. Type example of peptidase family M12.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 143179-21-9
References:
1.  Krauhs, E., Dörsam, H., Little, M., Zwilling, R. and Ponstingl, H. A protease from Astacus fluviatilis as an aid in protein sequencing. Anal. Biochem. 119 (1982) 153–157. [DOI] [PMID: 7041692]
2.  Titani, K., Torff, H.-J., Hormel, S., Kumar, S., Walsh, K.A., Rödl, J., Neurath, H. and Zwilling, R. Amino acid sequence of a unique protease from the crayfish Astacus fluviatilis. Biochemistry 26 (1987) 222–226. [PMID: 3548817]
3.  Stöcker, W., Wolz, R.L., Zwilling, R., Strydom, D.J. and Auld, D.S. Astacus protease, a zinc metalloenzyme. Biochemistry 27 (1988) 5026–5032.
4.  Stöcker, W., Ng, M. and Auld, D.S. Fluorescent oligopeptide substrates for kinetic characterization of the specificity of Astacus protease. Biochemistry 29 (1990) 10418–10425. [PMID: 2261483]
[EC 3.4.24.21 created 1972 as EC 3.4.99.6, transferred 1992 to EC 3.4.24.21]
 
 
EC 3.4.24.22     
Accepted name: stromelysin 2
Reaction: Similar to stromelysin 1, but action on collagen types III, IV and V is weak
Other name(s): matrix metalloproteinase 10; transin 2; proteoglycanase 2
Comments: In peptidase family M10 (interstitial collagenase family). Digests gelatin types I, III, IV, V, fibronectin and proteoglycan
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 140610-48-6
References:
1.  Breathnach, R., Matrisian, L.M., Gesnel, M.-C. and Leroy, P. Sequences coding for part of oncogene-induced transin are highly conserved in a related rat gene. Nucleic Acids Res. 15 (1987) 1139–1151. [DOI] [PMID: 3547333]
2.  Muller, D., Quantin, B., Gesnel, M.-C., Millon-Collard, R., Abecassis, J. and Breathnach, R. The collagenase gene family in humans consists of at least four members. Biochem. J. 253 (1988) 187–192. [PMID: 2844164]
3.  Nicholson, R., Murphy, G. and Breathnach, R. Human and rat malignant-tumor-associated mRNAs encode stromelysin-like metalloproteinases. Biochemistry 28 (1989) 5195–5203. [PMID: 2548603]
[EC 3.4.24.22 created 1992]
 
 
EC 3.4.24.23     
Accepted name: matrilysin
Reaction: Cleavage of Ala14┼Leu and Tyr16┼Leu in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain α2(I) > α1(I)
Other name(s): matrin; uterine metalloendopeptidase; matrix metalloproteinase 7; putative (or punctuated) metalloproteinase-1; matrix metalloproteinase pump 1; MMP 7; PUMP-1 proteinase; PUMP; metalloproteinase pump-1; putative metalloproteinase; MMP
Comments: Found in rat uterus; at 19 kDa, the smallest member of peptidase family M10 (interstitial collagenase family). Similar in specificity to stromelysin, but more active on azocoll
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 141256-52-2
References:
1.  Muller, D., Quantin, B., Gesnel, M.-C., Millon-Collard, R., Abecassis, J. and Breathnach, R. The collagenase gene family in humans consists of at least four members. Biochem. J. 253 (1988) 187–192. [PMID: 2844164]
2.  Woessner, J.F., Jr. and Taplin, C.J. Purification and properties of a small latent matrix metalloproteinase of the rat uterus. J. Biol. Chem. 263 (1988) 16918–16925. [PMID: 3182822]
3.  Quantin, B., Murphy, G. and Breathnach, R. Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Biochemistry 28 (1989) 5327–5334. [PMID: 2550050]
4.  Miyazaki, K., Hattori, Y., Umenishi, F., Yasumitsu, H. and Umeda, M. Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line. Cancer Res. 50 (1990) 7758–7764. [PMID: 2253219]
[EC 3.4.24.23 created 1992]
 
 
EC 3.4.24.24     
Accepted name: gelatinase A
Reaction: Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly┼Ile-Ala-Gly-Gln
Other name(s): 72-kDa gelatinase; matrix metalloproteinase 2; type IV collagenase (ambiguous); 3/4 collagenase (obsolete); matrix metalloproteinase 5 (obsolete); 72 kDa gelatinase type A; collagenase IV (ambiguous); collagenase type IV (ambiguous); MMP 2; type IV collagen metalloproteinase (ambiguous); type IV collagenase/gelatinase (ambiguous)
Comments: A secreted endopeptidase in peptidase family M10 (interstitial collagenase family), but possessing an additional fibronectin-like domain
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 146480-35-5
References:
1.  Murphy, G., McAlpine, C.G., Poll, C.T. and Reynolds, J.J. Purification and characterization of a bone metalloproteinase that degrades gelatin and types IV and V collagen. Biochim. Biophys. Acta 831 (1985) 49–58. [DOI] [PMID: 2994741]
2.  Collier, I.E., Wilhelm, S.M., Eisen, A.Z., Marmer, B.L., Grant, G.A., Seltzer, J.L., Kronberger, A., He, C., Bauer, E.A. and Goldberg, G.I. H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. J. Biol. Chem. 263 (1988) 6579–6587. [PMID: 2834383]
3.  Okada, Y., Morodomi, T., Enghild, J.J., Suzuki, K., Yasui, A., Nakanishi, I., Salvesen, G. and Nagase, H. Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts-purification and activation of the precursor and enzymic properties. Eur. J. Biochem. 194 (1990) 721–730. [DOI] [PMID: 2269296]
[EC 3.4.24.24 created 1992]
 
 
EC 3.4.24.25     
Accepted name: vibriolysin
Reaction: Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1′. Phe at P1′ is the most favoured residue, which distinguished this enzyme from thermolysin
Other name(s): Aeromonas proteolytica neutral proteinase; aeromonolysin
Comments: Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica). Specificity related to, but distinct from, those of thermolysin and bacillolysin [1]. A zinc metallopeptidase in family M4 (thermolysin family). Formerly included in EC 3.4.24.4
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 69598-88-5
References:
1.  Holmquist, B. and Vallee, B.L. Esterase activity of zinc neutral proteases. Biochemistry 15 (1976) 101–107. [PMID: 2276]
2.  Wilkes, S.H. and Prescott, J.M. Aeromonas neutral protease. Methods Enzymol. 45 (1976) 404–415. [DOI] [PMID: 1012006]
3.  Bayliss, M.E., Wilkes, S.H. and Prescott, J.M. Aeromonas neutral protease: specificity toward extended substrates. Arch. Biochem. Biophys. 204 (1980) 214–219. [DOI] [PMID: 7000005]
4.  Wilkes, S.H., Bayliss, M.E. and Prescott, J.M. Critical ionizing groups in Aeromonas neutral protease. J. Biol. Chem. 263 (1988) 1821–1825. [PMID: 3123480]
5.  David, V.A., Deutch, A.H., Sloma, A., Pawlyk, D., Ally, A. and Durham, D.R. Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus. Gene 112 (1992) 107–112. [DOI] [PMID: 1551587]
[EC 3.4.24.25 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.25, modified 1997]
 
 
EC 3.4.24.26     
Accepted name: pseudolysin
Reaction: Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1′. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects
Other name(s): Pseudomonas elastase; Pseudomonas aeruginosa neutral metalloproteinase
Comments: In peptidase family M4 (thermolysin family). From the pathogenic bacteria Pseudomonas aeruginosa and Legionella pneumophila, and causes tissue damage.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 171715-23-4
References:
1.  Morihara, K. and Tsuzuki, H. Pseudomonas aeruginosa elastase: affinity chromatography and some properties as a metallo-neutral proteinase. Agric. Biol. Chem. 39 (1975) 1123–1128.
2.  Nishino, N. and Powers, J.C. Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand. J. Biol. Chem. 255 (1980) 3482–3486. [PMID: 6767718]
3.  Dreyfus, L.A. and Iglewski, B.H. Purification and characterization of an extracellular protease of Legionella pneumophila. Infect. Immun. 70 (1986) 736–743. [PMID: 3512431]
4.  Bever, R.A. and Iglewski, B.H. Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene. J. Bacteriol. 170 (1988) 4309–4314. [DOI] [PMID: 2842313]
5.  Black, W.J., Quinn, F.D. and Tompkins, L.S. Legionella pneumophila zinc metalloprotease is structurally and functionally homologous to Pseudomonas aeruginosa elastase. J. Bacteriol. 172 (1990) 2608–2613. [DOI] [PMID: 2110146]
[EC 3.4.24.26 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.26]
 
 
EC 3.4.24.27     
Accepted name: thermolysin
Reaction: Preferential cleavage: ┼Leu > ┼Phe
Other name(s): Bacillus thermoproteolyticus neutral proteinase; thermoase; thermoase Y10; TLN
Comments: A thermostable extracellular metalloendopeptidase containing four calcium ions. Enzymes that may be species variants of thermolysin are reported from Micrococcus caseolyticus [4] and Aspergillus oryzae [5]. Type example of peptidase family M4. Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9073-78-3
References:
1.  Ohta, Y. Ogura, Y. and Wada, A. Thermostable protease from thermophilic bacteria. I. Thermostability, physicochemical properties, and amino acid composition. J. Biol. Chem. 241 (1966) 5919–5925. [PMID: 5954368]
2.  Morihara, K., Tsuzuki, H. and Oka, T. Comparison of the specificities of various neutral proteinases from microorganisms. Arch. Biochem. Biophys. 123 (1968) 572–588. [DOI] [PMID: 4967801]
3.  Latt, S. A., Holmquist, B. and Vallee, B. L. Thermolysin: a zinc metalloenzyme. Biochem. Biophys. Res. Commun. 37 (1969) 333–339. [DOI] [PMID: 5823940]
4.  Desmazeaud, M. J. and Hermier, J. H. Spécificité de la protéase neutre de Micrococcus caseolyticus. Eur. J. Biochem. 19 (1971) 51–55. [DOI] [PMID: 5551628]
5.  Morihara, K. and Tsuzuki, H. Comparative study of various neutral proteinases from microorganisms: specificity with oligopeptides. Arch. Biochem. Biophys. 146 (1971) 291–296. [DOI] [PMID: 5004124]
6.  Titani, K., Hermodson, M. A., Ericson, L. H., Walsh, K. A. and Neurath, H. Amino-acid sequence of thermolysin. Nature New Biol. 238 (1972) 35–37. [PMID: 18663848]
7.  Matthews, B. W. Structural basis of the action of thermolysin and related zinc peptidases. Acc. Chem. Res. 21 (1988) 333–340.
[EC 3.4.24.27 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.27]
 
 
EC 3.4.24.28     
Accepted name: bacillolysin
Reaction: Similar, but not identical, to that of thermolysin
Other name(s): Bacillus metalloendopeptidase; Bacillus subtilis neutral proteinase; anilozyme P 10; Bacillus metalloproteinase; Bacillus neutral proteinase; megateriopeptidase
Comments: Variants of this enzyme have been found in species of Bacillus including B. subtilis [1,6], B. amyloliquefaciens [5], B. megaterium (megateriopeptidase, [2]), B. mesentericus [10], B. cereus [3,8,9] and B. stearothermophilus [7]. In peptidase family M4 (thermolysin family). Formerly included in EC 3.4.24.4
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9080-56-2
References:
1.  Morihara, K., Tsuzuki, H. and Oka, T. Comparison of the specificities of various neutral proteinases from microorganisms. Arch. Biochem. Biophys. 123 (1968) 572–588. [DOI] [PMID: 4967801]
2.  Millet, J. and Acher, R. Spécificité de la mégatériopeptidase: une amino-endopeptidase à caractère hydrophobe. Eur. J. Biochem. 9 (1969) 456–462. [DOI] [PMID: 4980359]
3.  Feder, J., Keay, L., Garrett, L.R., Cirulis, N., Moseley, M.H. and Wildi, B.S. Bacillus cereus neutral protease. Biochim. Biophys. Acta 251 (1971) 74–78. [DOI] [PMID: 5002444]
4.  Holmquist, B. and Vallee, B.L. Esterase activity of zinc neutral proteases. Biochemistry 15 (1976) 101–107. [PMID: 2276]
5.  Vasantha, N., Thompson, L.D., Rhodes, C., Banner, C., Nagle, J. and Filpula, D. Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein. J. Bacteriol. 159 (1984) 811–819. [PMID: 6090391]
6.  Yang, M.Y., Ferrari, E. and Henner, D.J. Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro-derived deletion mutation. J. Bacteriol. 160 (1984) 15–21. [PMID: 6090407]
7.  Takagi, M., Imanaka, T. and Aiba, S. Nucleotide sequence and promoter region for the neutral protease gene from Bacillus stearothermophilus. J. Bacteriol. 163 (1985) 824–831. [PMID: 2993245]
8.  Sidler, W., Niederer, E., Suter, F. and Zuber, H. The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral proteinase. Biol. Chem. Hoppe-Seyler 367 (1986) 643–657. [PMID: 3092843]
9.  Pauptit, R.A., Karlson, R., Picot, D., Jenkins, J.A., Niklaus-Reimer, A.-S. and Jansonius, J.N. Crystal structure of neutral protease from Bacillus cereus refined at 3.0 Å resolution and comparison with the homologous but more thermostable enzyme thermolysin. J. Mol. Biol. 199 (1988) 525–537. [DOI] [PMID: 3127592]
10.  Stoeva, S., Kleinschmidt, T., Mesrob, B. and Braunitzer, G. Primary structure of a zinc protease from Bacillus mesentericus strain 76. Biochemistry 29 (1990) 527–534. [PMID: 2302386]
[EC 3.4.24.28 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.28]
 
 
EC 3.4.24.29     
Accepted name: aureolysin
Reaction: Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1′ residue. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus
Other name(s): Staphylococcus aureus neutral proteinase; Staphylococcus aureus neutral protease
Comments: A metalloenzyme from S. aureus earlier confused with staphylokinase (a non-enzymic activator of plasminogen).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 39335-13-2
References:
1.  Arvidson, S. Studies on extracellular proteolytic enzymes from Staphylococcus aureus. II. Isolation and characterization of an EDTA-sensitive protease. Biochim. Biophys. Acta 302 (1973) 149–157. [DOI] [PMID: 4632563]
2.  Saheb, S.A. Purification et caractérisation d’une protéase extracellulaire de Staphylococcus aureus inhibée par l’E.D.T.A. Biochimie 58 (1976) 793–804. [DOI] [PMID: 823980]
3.  Drapeau, G.R. Role of a metalloprotease in activation of the precursor of staphylococcal protease. J. Bacteriol. 136 (1978) 607–613. [PMID: 711676]
4.  Potempa, J., Porwit-Bohr, Z. and Travis, J. Stabilization vs. degradation of Staphylococcus aureus metalloproteinase. Biochim. Biophys. Acta 993 (1989) 301–304. [DOI] [PMID: 2512988]
[EC 3.4.24.29 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.29]
 
 
EC 3.4.24.30     
Accepted name: coccolysin
Reaction: Preferential cleavage: ┼Leu, ┼Phe, ┼Tyr, ┼Ala
Other name(s): Streptococcus thermophilus intracellular proteinase; EM 19000
Comments: A 30 kDa endopeptidase found intracellularly in S. thermophilus [1] and S. diacetilactis [2] and in the medium of S. faecalis [3,4]. In peptidase family M4 (thermolysin family). Formerly included in EC 3.4.24.4
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 156859-08-4
References:
1.  Desmazeaud, M.J. Propriétés générales et spécificité d’action d’une endopeptidase neutre intracellulaire de Streptococcus thermophilus. Biochimie 56 (1974) 1173–1181. [DOI] [PMID: 4451671]
2.  Desmazeaud, M.J. and Zevaco, C. General properties and substrate specificity of an intracellular neutral protease from Streptococcus diacetilactis. Ann. Biol. Anim. Biochem. Biophys. 16 (1976) 851–868.
3.  Smith, R.A.G., Green, J. and Kopper, P.H. The purification and properties of a fibrinolytic neutral metalloendopeptidase from Streptococcus faecalis. Arch. Biochem. Biophys. 202 (1980) 629–638. [DOI] [PMID: 6779709]
4.  Mäkinen, P.-L., Clewell, D.B., An, F., Mäkinen, K.K. Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain 0G1-10). J. Biol. Chem. 264 (1989) 3325–3334. [PMID: 2536744]
[EC 3.4.24.30 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.30]
 
 
EC 3.4.24.31     
Accepted name: mycolysin
Reaction: Preferential cleavage of bonds with hydrophobic residues in P1′
Other name(s): pronase component; Streptomyces griseus neutral proteinase; actinase E; SGNPI
Comments: From Streptomyces griseus, S. naraensis, and S. cacaoi. Specificity similar to that of thermolysin, but much more sensitive to inhibition by mercaptoacetyl-Phe-Leu. Little structural similarity to other bacterial metalloendopeptidases. Type example of peptidase family M5. Formerly included in EC 3.4.24.4
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 153190-34-2
References:
1.  Morihara, K., Tsuzuki, H. and Oka, T. Comparison of the specificities of various neutral proteinases from microorganisms. Arch. Biochem. Biophys. 123 (1968) 572–588. [DOI] [PMID: 4967801]
2.  Hiramatsu, A. and Ouchi, T. A neutral proteinase from Streptomyces naraensis. J. Biochem. (Tokyo) 71 (1972) 767–781. [PMID: 5073323]
3.  Blumberg, S. and Tauber, Z. Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides. Eur. J. Biochem. 136 (1983) 151–154. [DOI] [PMID: 6413206]
4.  Chang, P.C., Kue, T-C., Tsugita, A. and Lee, Y.H.W. Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product. Gene 88 (1990) 87–95. [DOI] [PMID: 2341042]
[EC 3.4.24.31 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.31]
 
 
EC 3.4.24.32     
Accepted name: β-lytic metalloendopeptidase
Reaction: Cleavage of N-acetylmuramoyl┼Ala, and of the insulin B chain at Gly23┼Phe > Val18┼Cya
Other name(s): Myxobacter β-lytic proteinase; achromopeptidase component; β-lytic metalloproteinase; β-lytic protease; Myxobacterium sorangium β-lytic proteinase; Myxobacter495 β-lytic proteinase
Comments: From Achromobacter lyticus and Lysobacter enzymogenes. Digests bacterial cell walls. Type example of peptidase family M23.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 37288-92-9
References:
1.  Whitaker, D.R., Roy, C., Tsai, C.S. and Juraöek, L. Lytic enzymes of Sorangium sp. A comparison of the proteolytic properties of the α- and β-lytic proteases. Can. J. Biochem. 43 (1965) 1961–1970. [PMID: 5880182]
2.  Whitaker, D.R. and Roy, C. Concerning the nature of the α- and β-lytic proteases of Sorangium sp. Can. J. Biochem. 45 (1967) 911. [PMID: 6034704]
3.  Li, S. L., Norioka, S. and Sakiyama, F. Molecular cloning and nucleotide sequence of the β-lytic protease gene from Achromobacter lyticus. J. Bacteriol. 172 (1990) 6506–6511. [DOI] [PMID: 2228973]
[EC 3.4.24.32 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.32]
 
 
EC 3.4.24.33     
Accepted name: peptidyl-Asp metalloendopeptidase
Reaction: Cleavage of Xaa┼Asp, Xaa┼Glu and Xaa┼cysteic acid bonds
Other name(s): endoproteinase Asp-N; peptidyl-Asp metalloproteinase
Comments: A metalloenzyme isolated from Pseudomonas fragi. Useful in protein sequencing applications because of its limited specificity. In peptidase family M72.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 55576-49-3
References:
1.  Porzio, M.A. and Pearson, A.M. Isolation of an extracellular neutral proteinase from Pseudomonas fragi. Biochim. Biophys. Acta 384 (1975) 235–241. [DOI] [PMID: 236771]
2.  Drapeau, G.R. Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi. J. Biol. Chem. 255 (1980) 839–840. [PMID: 7188696]
3.  Ingrosso, D., Fowler, A.V., Bleibaum, J. and Clarke, S. Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at glutamyl residues in two proteins. Biochem. Biophys. Res. Commun. 162 (1989) 1528–1534. [DOI] [PMID: 2669754]
[EC 3.4.24.33 created 1992]
 
 
EC 3.4.24.34     
Accepted name: neutrophil collagenase
Reaction: Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, interstitial collagenase, this enzyme cleaves type III collagen more slowly than type I
Other name(s): matrix metalloproteinase 8; PMNL collagenase; MMP-8
Comments: Similar to interstitial collagenase in specificity, but the product of a different gene and highly glycosylated. Stored in the specific granules of neutrophil leukocytes. In peptidase family M10 (interstitial collagenase family). Formerly included in EC 3.4.24.7
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9001-12-1
References:
1.  Hasty, K. A., Jeffrey, J. J., Hibbs, M. S. and Welgus, H. G. The collagen substrate specificity of human neutrophil collagenase. J. Biol. Chem. 262 (1987) 10048–10052. [PMID: 3038863]
2.  Hasty, K. A., Pourmotabbed, T. F., Goldberg, G. I., Thompson, J. P., Spinella, D. G., Stevens, R. M. and Mainardi, C. L. Human Neutrophil Collagenase. A distinct gene product with homology to other matrix metalloproteinases. J. Biol. Chem. 265 (1990) 11421–11424. [PMID: 2164002]
3.  Knäuper, V., Krämer, S., Reinke, H. and Tschesche, H. Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence and determination of the proenzyme and various proteolytically activated forms. Eur. J. Biochem. 189 (1990) 295–300. [DOI] [PMID: 2159879]
[EC 3.4.24.34 created 1992]
 
 
EC 3.4.24.35     
Accepted name: gelatinase B
Reaction: Cleavage of gelatin types I and V and collagen types IV and V
Other name(s): 92-kDa gelatinase; matrix metalloproteinase 9; type V collagenase; 92-kDa type IV collagenase; macrophage gelatinase; 95 kDa type IV collagenase/gelatinase; collagenase IV (ambiguous); collagenase type IV (ambiguous); gelatinase MMP 9; MMP 9; type IV collagen metalloproteinase (ambiguous)
Comments: Similar to gelatinase A, but possesses a further domain . In peptidase family M10 (interstitial collagenase family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 146480-36-6
References:
1.  Hibbs, M.S., Hoidal, J.R. and Kang, A.H. Expression of a metalloproteinase that degrades native type V collagen and denatured collagens by cultured human alveolar macrophages. J. Clin. Invest. 80 (1987) 1644–1650. [DOI] [PMID: 3680518]
2.  Wilhelm, S.M., Collier, I.E., Marmer, B.L., Eisen, A.Z., Grant, G.A. and Goldberg, G.I. SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J. Biol. Chem. 264 (1989) 17213–17221. [PMID: 2551898]
3.  Mainardi, C. L. and Hasty, K. A. Secretion and glycosylation of rabbit macrophage type V collagenase. Matrix 10 (1990) 84–90. [PMID: 2165210]
[EC 3.4.24.35 created 1992]
 
 
EC 3.4.24.36     
Accepted name: leishmanolysin
Reaction: Preference for hydrophobic residues at P1 and P1′ and basic residues at P2′ and P3′. A model nonapeptide is cleaved at -Ala-Tyr┼Leu-Lys-Lys-
Other name(s): promastigote surface endopeptidase; glycoprotein gp63; Leishmania metalloproteinase; surface acid proteinase; promastigote surface protease
Comments: A membrane-bound glycoprotein found on the promastigote of various species of Leishmania protozoans. Contains consensus sequence for a zinc-binding site; Z-Tyr-Leu-NHOH is a strong inhibitor. The enzyme can activate its proenzyme by cleavage of the Val100┼Val bond. An acid pH optimum is found with certain protein substrates. Type example of peptidase family M8
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 161052-06-8
References:
1.  Button, L.L. and McMaster, W.R. Molecular cloning of the major surface antigen of Leishmania. J. Exp. Med. 167 (1988) 724–729. [PMID: 3346625]
2.  Bouvier, J., Cordier, C., Vogel, H., Reichelt, R. and Etges, R. Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase. Mol. Biochem. Parasitol. 37 (1989) 235–246. [DOI] [PMID: 2608099]
3.  Chaudhuri, G., Chaudhuri, M., Pan, A. and Chang, K.-P. Surface acid proteinase (gp63) of Leishmania mexicana. A metalloenzyme capable of protecting liposome-encapsulated proteins from phagolysosomal degradation by macrophages. J. Biol. Chem. 264 (1989) 7483–7489. [PMID: 2708373]
4.  Bouvier, J., Schneider, P., Etges, R. and Bordier, C. Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania. Biochemistry 29 (1990) 10113–10119. [PMID: 2271643]
[EC 3.4.24.36 created 1992]
 
 
EC 3.4.24.37     
Accepted name: saccharolysin
Reaction: Cleavage of Pro┼Phe and Ala┼Ala bonds
Other name(s): proteinase yscD; yeast cysteine proteinase D (Misleading); Saccharomyces cerevisiae proteinase yscD
Comments: An 83 kDa cytoplasmic thiol-dependent metalloendopeptidase from Saccharomyces cerevisiae. In peptidase family M3 (thimet oligopeptidase family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 96779-48-5
References:
1.  Achstetter, T., Ehmann, C. and Wolf, D.H. Proteinase yscD. Purification and characterization of a new yeast peptidase. J. Biol. Chem. 260 (1985) 4584–4590. [PMID: 3886641]
2.  Garcia-Alvarez, N., Teichert, U. and Wolf, D.H. Proteinase yscD mutants of yeast. Isolation and characterization. Eur. J. Biochem. 163 (1987) 339–346. [DOI] [PMID: 3545833]
[EC 3.4.24.37 created 1989 as EC 3.4.22.22, transferred 1992 to EC 3.4.24.37]
 
 
EC 3.4.24.38     
Accepted name: gametolysin
Reaction: Cleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met┼Arg-Phe-Ala
Other name(s): autolysin, Chlamydomonas cell wall degrading protease; lysin; Chlamydomonas reinhardtii metalloproteinase; gamete lytic enzyme; gamete autolysin
Comments: A glycoprotein found in the periplasmic space of Chlamydomonas reinhardtii gametes in a 62 kDa inactive form; decreased to 60 kDa upon activation. A zinc enzyme, inhibited by phosphoramidon, but also thiol activated. Type example of peptidase family M11
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 97089-74-2
References:
1.  Jaenicke, L., Kunhe, W., Spessert, R., Wahle, U. and Waffenschmidt, S. Cell-wall lytic enzymes (autolysins) of Chlamydomonas reinhardtii are (hydroxy)proline-specific proteases. Eur. J. Biochem. 170 (1987) 485–491. [PMID: 3319620]
2.  Buchanan, M.J., Imam, S.H., Eskue, W.A. and Snell, W.J. Activation of the cell wall degrading protease, lysin, during sexual signalling in Chlamydomonas: the enzyme is stored as an inactive, higher relative molecular mass precursor in the periplasm. J. Cell. Biol. 108 (1989) 199–207. [PMID: 2910877]
3.  Matsuda, Y. Gametolysin. In: Barrett, A.J., Rawlings, N.D. & Woessner, J.F. (Eds), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 1140–1143.
[EC 3.4.24.38 created 1992, modified 2000]
 
 
EC 3.4.24.39     
Accepted name: deuterolysin
Reaction: Preferential cleavage of bonds with hydrophobic residues in P1&prime
also Asn3┼Gln and Gly8┼Ser bonds in insulin B chain
Other name(s): Penicillium roqueforti protease II; microbial neutral proteinase II; acid metalloproteinase; neutral proteinase II; Penicillium roqueforti metalloproteinase
Comments: Proteolytic activity found in Penicillium roqueforti [4], P. caseicolum [4], Aspergillus sojae [3] and A. oryzae [1,5]. Optimum pH of 5 for digesting various proteins. Strong action on protamine and histones. Insensitive to phosphoramidon. About 20 kDa. A distinct Aspergillus sojae endopeptidase is larger and has a neutral pH optimum. Type example of peptidase family M35. Formerly included in EC 3.4.24.4
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 247028-11-1
References:
1.  Nakadai, T., Nasuno, S. and Iguchi, N. Purification and properties of neutral proteinase II from Aspergillus oryzae. Agric. Biol. Chem. 37 (1973) 2703–2708.
2.  Gripon, J.-C. and Hermier, J. Le système protéolytique de Penicillium roqueforti. III. Purification, propriétés et spécificité d’une protéase inhibée par l’E.D.T.A. Biochimie 56 (1974) 1324–1332. [PMID: 4219726]
3.  Sekine, H. , Neutral proteinases I and II of Aspergillus sojae action on various substrates. Agric. Biol. Chem. 40 (1976) 703–709.
4.  Gripon, J.C., Auberger, B. and Lenoir, J. Metalloproteases from Penicillium caseicolum and P. roqueforti: comparision of specificity and chemical characterization. Int. J. Biochem. 12 (1980) 451–455. [PMID: 6998789]
5.  Vaganova, T.I., Ivanova, N.M. and Stepanov, V.M. Isolation and properties of the "acid" metalloproteinase from Aspergillus oryzae. Biochemistry (Mosc) 53 (1988) 1171–1178.
[EC 3.4.24.39 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.39]
 
 
EC 3.4.24.40     
Accepted name: serralysin
Reaction: Preferential cleavage of bonds with hydrophobic residues in P1′
Other name(s): Pseudomonas aeruginosa alkaline proteinase; Escherichia freundii proteinase; Serratia marcescens extracellular proteinase; Serratia marcescens metalloproteinase; Pseudomonas aeruginosa alk. protease; Serratia marcescens metalloprotease
Comments: A 50 kDa extracellular endopeptidase from Pseudomonas aeruginosa [1,2,6], Escherichia freundii [3], Serratia marcescens [4,5,6] and Erwinia chrysanthemi [7]. There is broad specificity in cleavage of the insulin B chain, with some species variations. The pH optimum for digesting various proteins is about 9 - 10. In peptidase family M10 (interstitial collagenase family). Formerly included in EC 3.4.24.4
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 70851-98-8
References:
1.  Morihara, K., Tsuzuki, H. and Oka, T. Comparison of the specificities of various neutral proteinases from microorganisms. Arch. Biochem. Biophys. 123 (1968) 572–588. [DOI] [PMID: 4967801]
2.  Morihara, K., Tsuzuki, H. and Oka, T. On the specificity of Pseudomonas aeruginosa alkaline proteinase with synthetic peptides. Biochim. Biophys. Acta 309 (1973) 414–429. [DOI] [PMID: 4199986]
3.  Nakajima, M., Mizusawa, K. and Yoshida, F. Purification and properties of an extracellular proteinase of psychrophilic Escherichia freundii. Eur. J. Biochem. 44 (1974) 87–96. [DOI] [PMID: 4212288]
4.  Decedue, C.J., Broussard, E.A., II, L arson, A.D. and Braymer, H.D. Purification and characterization of the extracellular proteinase of Serratia marcescens. Biochim. Biophys. Acta 569 (1979) 293–301. [DOI] [PMID: 383155]
5.  Doerr, M. and Traub, W.H. Purification and characterization of two Serratia marcescens proteases. Zentralbl. Bakteriol., Mikrobiol. Hyg. Ser. A 257 (1984) 6–19. [PMID: 6380155]
6.  Nakahama, K., Yoshimura, K., Marumoto, R., Kikuchi, M., Lee, I.S., Hase, T. and Matsubara, H. Cloning and sequencing of Serratia protease gene. Nucleic Acids Res. 14 (1986) 5843–5856. [DOI] [PMID: 3016665]
7.  Dahler, G.S., Barras, F. and Keen, N.T. Cloning of genes encoding extracellular metalloproteases from Erwinia chrysanthemi EC16. J. Bacteriol. 172 (1990) 5803–5815. [DOI] [PMID: 2211513]
8.  Okuda, K., Morihara, K., Atsumi, Y., Takeuchi, H., Kawamoto, S., Kawasaki, H., Suzuki, K. and Fukushima, J. Complete nucleotide sequence of the structural gene for alkaline proteinase from Pseudomonas aeruginosa IFO 3455. Infect. Immun. 58 (1990) 4083–4088. [PMID: 2123832]
[EC 3.4.24.40 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.40]
 
 
EC 3.4.24.41     
Accepted name: atrolysin B
Reaction: Cleavage of His5┼Leu, His10┼Leu, Ala14┼Leu, Tyr16┼Leu and Gly23┼Phe of insulin B chain; identical to the cleavage of insulin B chain by atrolysin C. Also cleaves ┼Ser bonds in glucagon
Other name(s): Crotalus atrox metalloendopeptidase b; hemorrhagic toxin b; Ht-b
Comments: From the venom of the western diamondback rattlesnake (Crotalus atrox). In peptidase family M12 (astacin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 172306-48-8
References:
1.  Bjarnason, J.B. and Tu, A.T. Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e. Biochemistry 17 (1978) 3395–3404. [PMID: 210790]
2.  Bjarnason, J.B., Hamilton, D. and Fox, J.W. Studies on the mechanism of hemorrhage production by five proteolytic hemorrhagic toxins from Crotalus atrox venom. Biol. Chem. Hoppe-Seyler 369 (1988) 121–129. [PMID: 3060135]
[EC 3.4.24.41 created 1992]
 
 
EC 3.4.24.42     
Accepted name: atrolysin C
Reaction: Cleavage of His5┼Leu, His10┼Leu, Ala14┼Leu, Tyr16┼Leu and Gly23┼Phe bonds in B chain of insulin. With small molecule substrates prefers hydrophobic residue at P2′ and small residue such as Ala, Gly at P1
Other name(s): Crotalus atrox metalloendopeptidase c; hemorrhagic toxin c and d
Comments: A 24 kDa hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox) that digests type IV collagen, and exists as two forms, c and d. Phosphoramidon inhibits in the 0.1 mM range. In peptidase family M12 (astacin family). Hemorrhagic toxin-2 of C. ruber ruber has the same Mr and specificity and is a homologue [4,6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 158886-17-0
References:
1.  Bjarnason, J.B. and Tu, A.T. Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e. Biochemistry 17 (1978) 3395–3404. [PMID: 210790]
2.  Fox, J.W., Campbell, R., Beggerly, L. and Bjarnason, J.B. Substrate specificities and inhibition of two hemorrhagic zinc proteases Ht-c and Ht-d from Crotalus atrox venom. Eur. J. Biochem. 156 (1986) 65–72. [DOI] [PMID: 3514216]
3.  Bjarnason, J.B. and Fox, J.W. Characterization of two hemorrhagic zinc proteinases, toxin c and toxin d, from western diamondback rattlesnake (Crotalus atrox) venom. Biochim. Biophys. Acta 911 (1987) 356–363. [DOI] [PMID: 3101740]
4.  Mori, N., Nikai, T., Sugihara, H. and Tu, A.T. Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom. Arch. Biochem. Biophys. 253 (1987) 108–121. [DOI] [PMID: 2949699]
5.  Shannon, J.D., Baramova, E.N., Bjarnason, J.B. and Fox, F.W. Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin. J. Biol. Chem. 264 (1989) 11575–11583. [PMID: 2745407]
6.  Takeya, H., Onikura, A., Nikai, T., Sugihara, H. and Iwanaga, S. Primary structure of a hemorrhagic metalloproteinase, HT- 2, isolated from the venom of Crotalus ruber ruber. J. Biochem. (Tokyo) 108 (1990) 711–719. [PMID: 2081731]
[EC 3.4.24.42 created 1992]
 
 
EC 3.4.24.43     
Accepted name: atroxase
Reaction: Cleavage of His5┼Leu, Ser9┼His, His10┼Leu, Ala14┼Leu and Tyr16┼Leu of insulin B chain
Comments: A nonhemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox) that cleaves fibrinogen. In peptidase family M12 (astacin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 181186-94-7
References:
1.  Willis, T.W. and Tu, A.T. Purification and biochemical characterization of atroxase, a nonhemorrhagic fibrinolytic protease from western diamondback rattlesnake venom. Biochemistry 27 (1988) 4769–4777. [PMID: 3167016]
[EC 3.4.24.43 created 1992]
 
 
EC 3.4.24.44     
Accepted name: atrolysin E
Reaction: Cleavage of Asn3┼Gln, Ser9┼His and Ala14┼Leu bonds in insulin B chain and Tyr14┼Gln and Thr8┼Ser in A chain. Cleaves type IV collagen at Ala73┼Gln in α1(IV) and at Gly7┼Leu in α2(IV)
Other name(s): Crotalus atrox metalloendopeptidase e; hemorrhagic toxin e
Comments: A 25.7 kDa hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox) that digests basement membrane components, including the triple helix of type IV collagen. Such action is believed to contribute to the hemorrhagic property by weakening capillary walls. In peptidase family M12 (astacin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 172306-51-3
References:
1.  Bjarnason, J.B. and Tu, A.T. Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e. Biochemistry 17 (1978) 3395–3404. [PMID: 210790]
2.  Bjarnason, J.B. and Fox, J.W. Proteolytic specificity and cobalt exchange of hemorrhagic toxin e, a zinc protease isolated from the venom of the western diamondback rattlesnake (Crotalus atrox). Biochemistry 22 (1983) 3770–3778. [PMID: 6351911]
3.  Baramova, E.N., Shannon, J.D., Bjarnason, J.B. and Fox, J.W. Identification of the cleavave sites by a hemorrhagic metalloproteinase in type IV collagen. Matrix 10 (1990) 91–97. [PMID: 2374521]
[EC 3.4.24.44 created 1992]
 
 
EC 3.4.24.45     
Accepted name: atrolysin F
Reaction: Cleavage of Val2┼Asn, Gln4┼His, Leu6┼Cys, His10┼Leu, Ala14┼Leu and Tyr16┼Leu bonds in insulin B chain
Other name(s): Crotalus atrox metalloendopeptidase; hemorrhagic toxin f; Crotalus atrox metalloendopeptidase f
Comments: A 64 kDa hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox) that digests the γ chain of fibrinogen. Immunologically distinct from EC 3.4.24.1, atrolysin A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 172306-52-4
References:
1.  Nikai, T., Mori, N., Kishida, M., Sugihara, H. and Tu, A.T. Isolation and biochemical characterization of hemorrhagic toxin f from the venom of Crotalus atrox (western diamondback rattlesnake). Arch. Biochem. Biophys. 231 (1984) 309–319. [DOI] [PMID: 6375570]
[EC 3.4.24.45 created 1992]
 
 
EC 3.4.24.46     
Accepted name: adamalysin
Reaction: Cleavage of Phe1┼Val, His5┼Leu, His10┼Leu, Ala14┼Leu, Leu15┼Tyr, and Tyr16┼Leu of insulin B chain
Other name(s): Crotalus adamanteus metalloendopeptidase; proteinase I and II; Crotalus adamanteus venom proteinase II; adamalysin II
Comments: From the venom of the eastern diamondback rattlesnake (Crotalus adamanteus). Two isoenzymes of approx. 24 kDa that inactivate α1-proteinase inhibitor by a single cleavage. In peptidase family M12 (astacin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 74812-51-4
References:
1.  Kurecki, T., Laskowski, M., Sr. and Kress, L.F. Purification and some properties of two proteinases from Crotalus adamanteus venom that inactivate human α1-proteinase inhibitor. J. Biol. Chem. 253 (1978) 8340–8345. [PMID: 309470]
[EC 3.4.24.46 created 1992]
 
 
EC 3.4.24.47     
Accepted name: horrilysin
Reaction: Cleavage of only the single bond Ala14┼Leu in the insulin B chain, Ser12┼Leu in the A chain, and Ile┼Gly, Pro┼Ala, and Ser┼Trp in melittin
Other name(s): Crotalus horridus metalloendopeptidase; hemorrhagic proteinase IV; Crotalus horridus horridus venom hemorrhagic proteinase
Comments: A 56 kDa hemorrhagic endopeptidase from the venom of the timber rattlesnake (Crotalus horridus horridus) that cleaves basement membrane, hide powder and fibrinogen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 84056-81-5
References:
1.  Civello, D.J., Duong, H.L. and Geren, C.R. Isolation and characterization of a hemorrhagic proteinase from timber rattlesnake venom. Biochemistry 22 (1983) 749–755. [PMID: 6340728]
2.  Civello, D.J., Moran, J.B. and Geren, C.R. Substrate specificity of a hemorrhagic proteinase from timber rattlesnake venom. Biochemistry 22 (1983) 755–762. [PMID: 6340729]
[EC 3.4.24.47 created 1992]
 
 
EC 3.4.24.48     
Accepted name: ruberlysin
Reaction: Cleavage of His10┼Leu, Ala14┼Leu, Tyr16┼Leu and Gly23┼Phe bonds in the B chain of insulin; His┼Pro, Pro┼Phe, and Trp┼Ser of angiotensin I; and Gly┼Phe of Met enkephalin
Other name(s): Crotalus ruber metalloendopeptidase II; hemorrhagic toxin II
Comments: A 25 kDa hemorrhagic endopeptidase from the venom of the red rattlesnake (Crotalus ruber ruber) that cleaves fibrinogen. In peptidase family M12 (astacin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 846020-01-7
References:
1.  Mori, N., Nikai, T., Sugihara, H. and Tu, A.T. Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom. Arch. Biochem. Biophys. 253 (1987) 108–121. [DOI] [PMID: 2949699]
2.  Takeya, H., Onikura, A., Nikai, T., Sugihara, H. and Iwanaga, S. Primary structure of a hemorrhagic metalloproteinase, HT- 2, isolated from the venom of Crotalus ruber ruber. J. Biochem. (Tokyo) 108 (1990) 711–719. [PMID: 2081731]
[EC 3.4.24.48 created 1992]
 
 
EC 3.4.24.49     
Accepted name: bothropasin
Reaction: Cleavage of His5┼Leu, His10┼Leu, Ala14┼Leu, Tyr16┼Leu and Phe24┼Phe in insulin B chain
Other name(s): Bothrops jararaca venom metalloproteinase
Comments: Caseinolytic endopeptidase of jararaca snake (Bothrops jararaca) venom; 48 kDa. In peptidase family M12
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 84788-89-6
References:
1.  Mandelbaum, F.J., Reichel, A.P. and Assakura, M.T. Isolation and characterization of a proteolytic enzyme from the venom of the snake Bothrops jararaca (jararaca). Toxicon 20 (1982) 955–972. [PMID: 6819660]
[EC 3.4.24.49 created 1992]
 
 
EC 3.4.24.50     
Accepted name: bothrolysin
Reaction: Cleavage of Gln4┼His, Ser9┼His and Ala14┼Leu of insulin B chain and Pro┼Phe of angiotensin I
Other name(s): Bothrops metalloendopeptidase J; J protease
Comments: A 22.5 kDa endopeptidase from the venom of the jararaca snake (Bothrops jararaca), insensitive to phosphoramidon at 0.5 mM. In peptidase family M12 (astacin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 443890-65-1
References:
1.  Tanizaki, M.M., Zingali, R.B., Kawazaki, H., Imajoh, S., Yamazaki, S. and Suzuki, K. Purification and some characteristics of a zinc metalloprotease from the venom of Bothrops jararaca (jararaca). Toxicon 27 (1989) 747–755. [PMID: 2781574]
[EC 3.4.24.50 created 1992]
 
 


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