Ile in the α1(I) chain. Cleaves synthetic substrates and α-macroglobulins at bonds where P1' is a hydrophobic residue
Reaction: Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at Gly775Ile in the α1(I) chain. Cleaves synthetic substrates and α-macroglobulins at bonds where P1' is a hydrophobic residue
Other names: vertebrate collagenase; matrix metalloproteinase 1
Comments: 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. However, α-macroglobulins are cleaved much more rapidly. The enzyme is widely distributed in vertebrate animals. Type example of peptidase family M10
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 9001-12-1
References:
1. Goldberg, G.I., Wilhelm, S.M., Kronberger, A., Bauer, E.A., Grant, G.A. and Eisen, A.Z. Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein. J. Biol. Chem. 261 (1986) 6600-6605. [PMID: 3009463]
2. Birkedal-Hansen, H. Catabolism and turnover of collagens: collagenases. Methods Enzymol. 144 (1987) 140-171. [PMID: 3041177]
3. Fields, G.B., Van Wart, H.E. and Birkedal-Hansen, H. Sequence specificity of human skin fibroblast collagenase. Evidence for the role of collagen structure in determining the collagenase cleavage site. J. Biol. Chem. 262 (1987) 6221-6226. [PMID: 3032960]
4. Sottrup-Jensen, L. and Birkedal-Hansen, H. Human fibroblast collagenase-α-macroglobulin interactions. Localization of cleavage sites in the bait regions of five mammalian α-macroglobulins. J. Biol. Chem. 264 (1989) 393-401. [PMID: 2462561]