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 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 | ||||||||
| |||||||||
| Peptidase S1A, matripase | |
|---|---|
| Identifiers | |
| Symbol | S1A |
| InterPro | IPR017051 |
| Membranome | 1287 |
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
editReferences
edit- ^ 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
edit- Matriptase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
