Matriptase

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

Matriptase
Identifiers
EC number3.4.21.109
CAS number241475-96-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Peptidase S1A, matripase
Identifiers
SymbolS1A
InterProIPR017051
Membranome1287

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

  • ST14, also known as matriptase
  • TMPRSS6, also known as matriptase 2
gollark: Technically yes, but according to our analysts this may be considered mean.
gollark: Which one is the super key again?
gollark: This operation is run on dedicated computing clusters and not my laptop GPU.
gollark: For legal reasons we do not record this information.
gollark: Aren't hyperfast simulations of reality great?

References

  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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