Belongs to peptidase family M9.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
Also known from Streptomyces sp.,
Belongs to peptidase family M9.,
Class I has forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class II has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa).,
Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum.,
The enzymes also act as peptidyl-tripeptidases.,
The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary.,
Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V.alginolyticus (previously Achromobacter iophagus).
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| rdfs:subClassOf | |
| skos:broaderTransitive | |
| uniprot:name |
Clostridiopeptidase A,
Clostridium histolyticum collagenase,
Collagenase A,
Collagenase I,
Microbial collagenase
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| uniprot:replaces | |
| uniprot:activity |
Digestion of native collagen in the triple helical region at Xaa-|-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'.
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| uniprot:cofactor |
Zinc
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