ENZYME entry: EC 3.4.24.7

Accepted Name
Interstitial collagenase.
Alternative Name(s)
Matrix metalloproteinase 1.
Vertebrate collagenase.
Reaction catalysed
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue
Cofactor(s)
Zn(2+).
Comment(s)
  • The enzyme takes its name from substrates of the interstitial collagen group - types I, II and III, all of which are cleaved in the helical domain.
  • Alpha-macroglobulins are cleaved much more rapidly.
  • The enzyme is widely distributed in vertebrate animals.
  • Belongs to peptidase family M10B.
Cross-references
PROSITEPDOC00129
BRENDA3.4.24.7
EC2PDB3.4.24.7
ExplorEnz3.4.24.7
PRIAM enzyme-specific profiles3.4.24.7
KEGG Ligand Database for Enzyme Nomenclature3.4.24.7
IUBMB Enzyme Nomenclature3.4.24.7
IntEnz3.4.24.7
MEDLINEFind literature relating to 3.4.24.7
MetaCyc3.4.24.7
UniProtKB/Swiss-Prot
P34156, COG4_CHIOP;  Q9EPL5, MMP1A_MOUSE;  Q9EPL6, MMP1B_MOUSE;  
P28053, MMP1_BOVIN;  Q9XSZ5, MMP1_HORSE;  P03956, MMP1_HUMAN;  
Q11133, MMP1_LITCT;  P21692, MMP1_PIG;  P13943, MMP1_RABIT;  
P81563, MMP1_RAT;  

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