Interstitial collagenase

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Interstitial collagenase
1hfc.jpg
collagenase monomer, Human fibroblast
Identifiers
EC number 3.4.24.7
CAS number 2593923
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Interstitial collagenase (EC 3.4.24.7, 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]

References[edit]

  1. ^ Goldberg, G.I.; Wilhelm, S.M.; Kronberger, A.; Bauer, E.A.; Grant, G.A.; Eisen, A.Z. (1986). "Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein". J. Biol. Chem. 261: 6600–6605. PMID 3009463. 
  2. ^ Birkedal-Hansen, H. (1987). "Catabolism and turnover of collagens: collagenases". Methods Enzymol. 144: 140–171. PMID 3041177. doi:10.1016/0076-6879(87)44177-3. 
  3. ^ Fields, G.B.; Van Wart, H.E.; Birkedal-Hansen, H. (1987). "Sequence specificity of human skin fibroblast collagenase. Evidence for the role of collagen structure in determining the collagenase cleavage site". J. Biol. Chem. 262: 6221–6226. PMID 3032960. 
  4. ^ Sottrup-Jensen, L.; Birkedal-Hansen, H. (1989). "Human fibroblast collagenase-α-macroglobulin interactions. Localization of cleavage sites in the bait regions of five mammalian α-macroglobulins". J. Biol. Chem. 264: 393–401. PMID 2462561. 

External links[edit]