Interstitial collagenase

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Interstitial collagenase
collagenase monomer, Human fibroblast
EC no.
CAS no.2593923
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

Interstitial collagenase (EC, vertebrate collagenase, matrix metalloproteinase 1) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at Gly775-Ile in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue

This enzyme belongs to the peptidase family M10.

See also[edit]


  1. ^ Goldberg GI, Wilhelm SM, Kronberger A, Bauer EA, Grant GA, Eisen AZ (May 1986). "Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein". The Journal of Biological Chemistry. 261 (14): 6600–5. PMID 3009463.
  2. ^ Birkedal-Hansen H (1987). "Catabolism and turnover of collagens: collagenases". Methods in Enzymology. 144: 140–71. doi:10.1016/0076-6879(87)44177-3. PMID 3041177.
  3. ^ Fields GB, Van Wart HE, Birkedal-Hansen H (May 1987). "Sequence specificity of human skin fibroblast collagenase. Evidence for the role of collagen structure in determining the collagenase cleavage site". The Journal of Biological Chemistry. 262 (13): 6221–6. PMID 3032960.
  4. ^ Sottrup-Jensen L, Birkedal-Hansen H (January 1989). "Human fibroblast collagenase-alpha-macroglobulin interactions. Localization of cleavage sites in the bait regions of five mammalian alpha-macroglobulins". The Journal of Biological Chemistry. 264 (1): 393–401. PMID 2462561.

External links[edit]