The Enzyme Database

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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, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9001-12-1
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]
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