Biology:Stromelysin 1
From HandWiki
| Stromelysin 1 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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
- ↑ "Stromelysin, a connective tissue-degrading metalloendopeptidase secreted by stimulated rabbit synovial fibroblasts in parallel with collagenase. Biosynthesis, isolation, characterization, and substrates". The Journal of Biological Chemistry 260 (22): 12367–76. October 1985. PMID 2995374.
- ↑ "A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization". The Journal of Biological Chemistry 261 (30): 14245–55. October 1986. PMID 3095317.
- ↑ "The tissue metalloproteinase family and the inhibitor TIMP: a study using cDNAs and recombinant proteins". Annals of the Rheumatic Diseases 49 Suppl 1: 469–79. June 1990. PMID 2197998.
- ↑ "Matrix metalloproteinases. A review". Cellular and Molecular Biology 36 (2): 131–53. 1990. PMID 2165861.
External links
- Stromelysin+1 at the US National Library of Medicine Medical Subject Headings (MeSH)
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