| EC |
3.4.16.2 |
| Accepted name: |
lysosomal Pro-Xaa carboxypeptidase |
| Reaction: |
Cleavage of a -Pro┼Xaa bond to release a C-terminal amino acid |
| Other name(s): |
angiotensinase C; lysosomal carboxypeptidase C; peptidylprolylamino acid carboxypeptidase; aminoacylproline carboxypeptidase; prolyl carboxypeptidase; carboxypeptidase P; proline-specific carboxypeptidase P; PCP |
| Comments: |
A lysosomal peptidase active at acidic pH that inactivates angiotensin II. Inhibited by diisopropyl fluorophosphate. In peptidase family S28 (Pro-X carboxypeptidase family). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9075-64-3 |
| References: |
| 1. |
Walter, R., Simmons, W.H. and Yoshimoto, T. Proline specific endo- and exopeptidases. Mol. Cell. Biochem. 30 (1980) 111–127. [PMID: 6991912] |
| 2. |
Odya, C.E. and Erdös, E.G. Human prolylcarboxypeptidase. Methods Enzymol. 80 (1981) 460–466. [PMID: 7341916] |
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| [EC 3.4.16.2 created 1972 as EC 3.4.12.4, transferred 1978 to EC 3.4.16.2] |
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