Metallocarboxypeptidase D
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| Metallocarboxypeptidase D | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.22 | ||||||||
| CAS no. | 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 (June 1995). "gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family". The Journal of Biological Chemistry. 270 (25): 15022–8. doi:10.1074/jbc.270.25.15022. PMID 7797483.
- ^ Song L, Fricker LD (October 1995). "Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary". The Journal of Biological Chemistry. 270 (42): 25007–13. doi:10.1074/jbc.270.42.25007. PMID 7559630.
- ^ Song L, Fricker LD (November 1996). "Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D". The Journal of Biological Chemistry. 271 (46): 28884–9. doi:10.1074/jbc.271.46.28884. PMID 8910535.
External links
- Metallocarboxypeptidase+D at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
