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ENZYME

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 alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue
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
BRENDA3.4.24.7
EC2PDB3.4.24.7
ExplorEnz3.4.24.7
KEGG Ligand Database for Enzyme Nomenclature3.4.24.7
IUBMB Enzyme Nomenclature3.4.24.7
MEDLINEFind literature relating to 3.4.24.7
MetaCyc3.4.24.7
Rhea expert-curated reactions3.4.24.7
UniProtKB/Swiss-Prot
P34156, COG4_CHIOPQ9EPL5, MMP1A_MOUSEQ9EPL6, MMP1B_MOUSE
Q11133, MMP1_AQUCTP28053, MMP1_BOVINQ9XSZ5, MMP1_HORSE
P03956, MMP1_HUMANP21692, MMP1_PIGP13943, MMP1_RABIT
P81563, MMP1_RAT

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.24.-
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