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.
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. [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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