| EC |
3.4.17.16 |
| Accepted name: |
membrane Pro-Xaa carboxypeptidase |
| Reaction: |
Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond |
| Other name(s): |
carboxypeptidase P; microsomal carboxypeptidase; membrane Pro-X carboxypeptidase |
| Comments: |
One of the renal brush border exopeptidases |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-64-3 |
| References: |
| 1. |
Dehm, P. and Nordwig, A. The cleavage of prolyl peptides by kidney peptidases. Isolation of a microsomal carboxypeptidase from swine kidney. Eur. J. Biochem. 17 (1970) 372–377. [DOI] [PMID: 5500406] |
| 2. |
Booth, A.G., Hubbard, L.M.L. and Kenny, A.J. 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 (1979) 397–405. [PMID: 486090] |
| 3. |
Hedeager-Sorensen, S. and Kenny, A.J. Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P from pig kidneys. Biochem. J. 229 (1985) 251–257. [PMID: 4038259] |
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| [EC 3.4.17.16 created 1992] |
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