IUBMB Enzyme Nomenclature


Accepted name: matrilysin

Reaction: Cleavage of Ala14Leu and Tyr16Leu in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain α2(I) > α1(I)

Other names: 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, MEROPS, Metacyc, 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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