Matriptase

Matriptase
Identifiers
EC number 3.4.21.109
CAS number 241475-96-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Matriptases (EC 3.4.21.109) are an enzyme family.[1][2] This enzyme catalyses the following chemical reaction

Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position

This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis.

Human matriptases

References

  1. Lee, S.L.; Dickson, R.B.; Lin, C.Y. (2000). "Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease". J. Biol. Chem. 275: 36720–36725. doi:10.1074/jbc.M007802200. PMID 10962009.
  2. Lin, C.Y.; Anders, J.; Johnson, M.; Sang, Q.A.; Dickson, R.B. (1999). "Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity". J. Biol. Chem. 274: 18231–18236. doi:10.1074/jbc.274.26.18231. PMID 10373424.
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