Lysosomal Pro-X carboxypeptidase
| Lysosomal Pro-Xaa carboxypeptidase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.16.2 | ||||||||
| 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 | ||||||||
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Lysosomal Pro-Xaa carboxypeptidase (EC 3.4.16.2, angiotensinase C, lysosomal carboxypeptidase C, peptidylprolylamino acid carboxypeptidase, aminoacylproline carboxypeptidase, prolyl carboxypeptidase, carboxypeptidase P, proline-specific carboxypeptidase P, PCP) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Cleavage of a -Pro-Xaa bond to release a C-terminal amino acid
A lysosomal peptidase active at acidic pH that inactivates angiotensin II. This enzyme is inhibited by diisopropyl fluorophosphate.
References
- ↑ Walter, R., Simmons, W.H. and Yoshimoto, T. (1980). "Proline specific endo- and exopeptidases". Mol. Cell. Biochem. 30: 111–127. doi:10.1007/bf00227927. PMID 6991912.
- ↑ Odya, C.E. and Erdös, E.G. (1981). "Human prolylcarboxypeptidase". Methods Enzymol. 80: 460–466. doi:10.1016/s0076-6879(81)80040-7. PMID 7341916.
External links
- Lysosomal Pro-Xaa carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
human prolylcarboxypeptidase entry at OMIM: http://omim.org/entry/176785
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