EC |
3.4.24.17 |
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, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 79955-99-0 |
References: |
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] |
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[EC 3.4.24.17 created 1990] |
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