Matriptase
Matriptase | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.21.109 | ||||||||
CAS no. | 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 | ||||||||
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Peptidase S1A, matripase | |
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Identifiers | |
Symbol | S1A |
InterPro | IPR017051 |
Membranome | 1287 |
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[]
References[]
- ^ 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.
- ^ 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.
External links[]
- Matriptase at the US National Library of Medicine Medical Subject Headings (MeSH)
Categories:
- EC 3.4.21