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Matriptase

From Wikipedia, the free encyclopedia
Matriptase
Identifiers
EC no.3.4.21.109
CAS no.241475-96-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
Peptidase S1A, matripase
Identifiers
SymbolS1A
InterProIPR017051
Membranome1287

Matriptases (EC 3.4.21.109) are an enzyme family.[1][2] This enzyme 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. It belongs to proteases of PA superfamily.

Human matriptases

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  • ST14, also known as matriptase
  • TMPRSS6, also known as matriptase 2

References

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  1. ^ Lee SL, Dickson RB, Lin CY (November 2000). "Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease". The Journal of Biological Chemistry. 275 (47): 36720–5. doi:10.1074/jbc.M007802200. PMID 10962009.
  2. ^ Lin CY, Anders J, Johnson M, Sang QA, Dickson RB (June 1999). "Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity". The Journal of Biological Chemistry. 274 (26): 18231–6. doi:10.1074/jbc.274.26.18231. PMID 10373424.
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