Hepsin
| Hepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.21.106 | ||||||||
| CAS number | 112398-23-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Hepsin (EC 3.4.21.106) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys
This type-II membrane-associated serine peptidase plays a role in cell growth and development.
References
- ↑ Zhukov, A.; Hellman, U.; Ingelman-Sundberg, M. (1997). "Purification and characterization of hepsin from rat liver microsomes". Biochim. Biophys. Acta. 1337 (1): 85–95. doi:10.1016/s0167-4838(96)00152-5. PMID 9003440.
- ↑ Kazama, Y.; Hamamoto, T.; Foster, D.C.; Kisiel, W. (1995). "Hepsin, a putative membrane-associated serine protease, activates human factor VII and initiates a pathway of blood coagulation on the cell surface leading to thrombin formation". J. Biol. Chem. 270: 66–72. doi:10.1074/jbc.270.1.66. PMID 7814421.
- ↑ Torres-Rosado, A.; O'Shea, K.S.; Tsuji, A.; Chou, S.H.; Kurachi, K. (1993). "Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth". Proc. Natl. Acad. Sci. USA. 90: 7181–7185. doi:10.1073/pnas.90.15.7181. PMC 47100
. PMID 8346233.
See also
External links
- Hepsin at the US National Library of Medicine Medical Subject Headings (MeSH)
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