ENZYME entry: EC 3.4.24.3

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'
Cofactor(s)
Zn(2+).
Comment(s)
  • 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 3.4.4.19, EC 3.4.24.8 and EC 3.4.99.5.
Cross-references
BRENDA3.4.24.3
EC2PDB3.4.24.3
ExplorEnz3.4.24.3
PRIAM enzyme-specific profiles3.4.24.3
KEGG Ligand Database for Enzyme Nomenclature3.4.24.3
IUBMB Enzyme Nomenclature3.4.24.3
IntEnz3.4.24.3
MEDLINEFind literature relating to 3.4.24.3
MetaCyc3.4.24.3
UniProtKB/Swiss-Prot
P43153, COLA_CLOPE;  P43154, COLA_VIBAL;  Q9KRJ0, COLA_VIBCH;  
Q56696, COLA_VIBPA;  Q8D4Y9, COLA_VIBVU;  

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