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Microbial collagenase
| Field | Value |
|---|---|
| Name | Microbial collagenase |
| EC_number | 3.4.24.3 |
| CAS_number | 2593923 |
Microbial collagenase (, 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, matrix metalloproteinase-8, matirx metalloproteinase-18, interstitial collagenase) is an enzyme. This enzyme catalyses the following chemical 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'
Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum.
References
References
- Tong, N.T.. (1986). "Purification and characterization of two high-molecular-mass forms of ''Achromobacter collagenase''". Biochim. Biophys. Acta.
- (July 1987). "Purification and properties of collagenase from a Streptomyces species". Journal of Biochemistry.
- (September 1987). "Purification and properties of an extracellular collagenolytic protease produced by the human oral bacterium Bacillus cereus (strain Soc 67)". The Journal of Biological Chemistry.
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