Matrilysin
| Matrilysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.23 | ||||||||
| CAS number | 141256-52-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Matrilysin (EC 3.4.24.23, matrin, uterine metalloendopeptidase, matrix metalloproteinase 7, putative (or punctuated) metalloproteinase-1, matrix metalloproteinase pump 1, MMP 7, PUMP-1 proteinase, PUMP, metalloproteinase pump-1, putative metalloproteinase, MMP) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Cleavage of Ala14-Leu and Tyr16-Leu in B chain of insulin. No action on collagen types I, II, IV, V.
This enzyme is present in rat uterus.
References
- ↑ Muller, D.; Quantin, B.; Gesnel, M.-C.; Millon-Collard, R.; Abecassis, J.; Breathnach, R. (1988). "The collagenase gene family in humans consists of at least four members". Biochem. J. 253 (1): 187–192. PMC 1149273
. PMID 2844164. - ↑ Woessner, J.F.; Jr.; Taplin, C.J. (1988). "Purification and properties of a small latent matrix metalloproteinase of the rat uterus". J. Biol. Chem. 263 (32): 16918–16925. PMID 3182822.
- ↑ Quantin, B.; Murphy, G.; Breathnach, R. (1989). "Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members". Biochemistry. 28 (13): 5327–5334. doi:10.1021/bi00439a004. PMID 2550050.
- ↑ Miyazaki, K.; Hattori, Y.; Umenishi, F.; Yasumitsu, H.; Umeda, M. (1990). "Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line". Cancer Res. 50 (24): 7758–7764. PMID 2253219.
External links
- Matrilysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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