Stromelysin 1
Stromelysin 1 | |||||||||
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Identifiers | |||||||||
EC number | 3.4.24.17 | ||||||||
CAS number | 79955-99-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Stromelysin 1 (EC 3.4.24.17, matrix metalloproteinase 3, proteoglycanase, collagenase activating protein, procollagenase activator, transin, MMP-3, neutral proteoglycanase, stromelysin, collagen-activating protein) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Preferential cleavage where P1', P2' and P3' are hydrophobic residues
This extracellular endopeptidase is present in vertebrate tissues.
References
- ↑ Chin, J.R.; Murphy, G.; Werb, Z. (1985). "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: 12367–12376. PMID 2995374.
- ↑ Okada, Y.; Nagase, H.; Harris, E.D. Jr. (1986). "A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization". J. Biol. Chem. 261: 14245–14255. PMID 3095317.
- ↑ Docherty, A.J.P.; Murphy, G. (1990). "The tissue metalloproteinase family and the inhibitor TIMP: a study using cDNAs and recombinant proteins". Ann. Rheum. Dis. 49: 469–479. PMID 2197998.
- ↑ Emonard, H.; Grimaud, J.A. (1990). "Matrix metalloproteinase. A review". Cell. Mol. Biol. 36: 131–153. PMID 2165861.
External links
- Stromelysin 1 at the US National Library of Medicine Medical Subject Headings (MeSH)
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