External links
- Matriptase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Activity | |
|---|---|
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
|
| Matriptase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.109 | ||||||||
| CAS no. | 241475-96-7 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| Peptidase S1A, matripase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | S1A | ||||||
| InterPro | IPR017051 | ||||||
| Membranome | 1287 | ||||||
| |||||||
Matriptases (EC 3.4.21.109) are an enzyme family. 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.
