The Enzyme Database

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Accepted name: stromelysin 1
Reaction: Preferential cleavage where P1′, P2′ and P3′ are hydrophobic residues
Other name(s): matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein
Comments: An extracellular endopeptidase of vertebrate tissues homologous with interstitial collagenase. Digests proteoglycan, fibronectin, collagen types III, IV, V, IX, and activates procollagenase. In peptidase family M10 (interstitial collagenase family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 79955-99-0
1.  Chin, J.R., Murphy, G. and Werb, Z. Stromelysin, a connective tissue-degrading metalloendopeptidase secreted by stimulated rabbit synovial fibroblasts in parallel with collagenase. Biosynthesis, isolation, characterization, and substrates. J. Biol. Chem. 260 (1985) 12367–12376. [PMID: 2995374]
2.  Okada, Y., Nagase, H. and Harris, E.D., Jr. A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization. J. Biol. Chem. 261 (1986) 14245–14255. [PMID: 3095317]
3.  Docherty, A.J.P. and Murphy, G. The tissue metalloproteinase family and the inhibitor TIMP: a study using cDNAs and recombinant proteins. Ann. Rheum. Dis. 49 (1990) 469–479. [PMID: 2197998]
4.  Emonard, H. and Grimaud, J.-A. Matrix metalloproteinase. A review. Cell. Mol. Biol. 36 (1990) 131–153. [PMID: 2165861]
[EC created 1990]

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