The Enzyme Database

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Accepted name: matrilysin
Reaction: Cleavage of Ala14┼Leu and Tyr16┼Leu in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain α2(I) > α1(I)
Other name(s): 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
Comments: Found in rat uterus; at 19 kDa, the smallest member of peptidase family M10 (interstitial collagenase family). Similar in specificity to stromelysin, but more active on azocoll
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 141256-52-2
1.  Muller, D., Quantin, B., Gesnel, M.-C., Millon-Collard, R., Abecassis, J. and Breathnach, R. The collagenase gene family in humans consists of at least four members. Biochem. J. 253 (1988) 187–192. [PMID: 2844164]
2.  Woessner, J.F., Jr. and Taplin, C.J. Purification and properties of a small latent matrix metalloproteinase of the rat uterus. J. Biol. Chem. 263 (1988) 16918–16925. [PMID: 3182822]
3.  Quantin, B., Murphy, G. and Breathnach, R. Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Biochemistry 28 (1989) 5327–5334. [PMID: 2550050]
4.  Miyazaki, K., Hattori, Y., Umenishi, F., Yasumitsu, H. and Umeda, M. Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line. Cancer Res. 50 (1990) 7758–7764. [PMID: 2253219]
[EC created 1992]

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