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
- ↑ 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.
- ↑ 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.
External links
- Matriptase at the US National Library of Medicine Medical Subject Headings (MeSH)
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