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

  1. ↑ Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J, Breathnach R (July 1988). "The collagenase gene family in humans consists of at least four members". The Biochemical Journal. 253 (1): 187–92. PMC 1149273. PMID 2844164.
  2. ↑ Woessner JF, Taplin CJ (November 1988). "Purification and properties of a small latent matrix metalloproteinase of the rat uterus". The Journal of Biological Chemistry. 263 (32): 16918–25. PMID 3182822.
  3. ↑ Quantin B, Murphy G, Breathnach R (June 1989). "Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members". Biochemistry. 28 (13): 5327–34. doi:10.1021/bi00439a004. PMID 2550050.
  4. ↑ Miyazaki K, Hattori Y, Umenishi F, Yasumitsu H, Umeda M (December 1990). "Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line". Cancer Research. 50 (24): 7758–64. PMID 2253219.
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