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ENZYME entry: EC

Accepted Name
microbial collagenase.
Alternative Name(s)
clostridiopeptidase A.
Clostridium histolyticum collagenase.
collagenase A.
collagenase I.
Reaction catalysed
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'
  • Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum.
  • 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).
  • 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, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V.alginolyticus (previously Achromobacter iophagus).
  • Also known from Streptomyces sp.
  • Belongs to peptidase family M9.
  • Formerly EC, EC and EC
PRIAM enzyme-specific profiles3.4.24.3
KEGG Ligand Database for Enzyme Nomenclature3.4.24.3
IUBMB Enzyme Nomenclature3.4.24.3
MEDLINEFind literature relating to
Rhea expert-curated reactions3.4.24.3

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