Membrane Pro-X carboxypeptidase
| Membrane Pro-Xaa carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.17.16 | ||||||||
| CAS number | 9075-64-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Membrane Pro-Xaa carboxypeptidase (EC 3.4.17.16, carboxypeptidase P, microsomal carboxypeptidase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond
This is one of the renal brush border exopeptidases
References
- ↑ Dehm, P.; Nordwig, A. (1970). "The cleavage of prolyl peptides by kidney peptidases. Isolation of a microsomal carboxypeptidase from swine kidney". Eur. J. Biochem. 17: 372–377. doi:10.1111/j.1432-1033.1970.tb01175.x. PMID 5500406.
- ↑ Booth, A.G.; Hubbard, L.M.L.; Kenny, A.J. (1979). "Proteins of the kidney microvillar membrane. Immunoelectrophoretic analysis of the membrane hydrolase: identification and resolution of the detergent- and proteinase-solubilized forms". Biochem. J. 179: 397–405. PMID 486090.
- ↑ Hedeager-Sorensen, S.; Kenny, A.J. (1985). "Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P from pig kidneys". Biochem. J. 229: 251–257. PMID 4038259.
External links
- Membrane Pro-Xaa carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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