Metallocarboxypeptidase D
| Metallocarboxypeptidase D | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.17.22 | ||||||||
| CAS number | 153967-26-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Metallocarboxypeptidase D (EC 3.4.17.22, carboxypeptidase D (cattle, human, mouse, rat), gp180 (duck)) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Releases C-terminal Arg and Lys from polypeptides
This enzyme is activated by Co2+, and inhibited by guanidinoethylmercaptosuccinic acid.
References
- ↑ Kuroki, K.; Eng, F.; Ishikawa, T.; Turck, C.; Harada, F.; Ganem, D. (1995). "gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family". J. Biol. Chem. 270: 15022–15028. doi:10.1074/jbc.270.25.15022. PMID 7797483.
- ↑ Song, L.X.; Fricker, L.D. (1995). "Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary". J. Biol. Chem. 270: 25007–25013. doi:10.1074/jbc.270.42.25007. PMID 7559630.
- ↑ Song, L.X.; Fricker, L.D. (1996). "Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D". J. Biol. Chem. 271: 28884–28889. doi:10.1074/jbc.271.46.28884. PMID 8910535.
External links
- Metallocarboxypeptidase+D at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from
Wikipedia.
The text is licensed under Creative Commons - Attribution - Sharealike.
Additional terms may apply for the media files.