Lysosomal Pro-X carboxypeptidase
| Lysosomal Pro-Xaa carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.16.2 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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
[edit]- ^ Walter R, Simmons WH, Yoshimoto T (April 1980). "Proline specific endo- and exopeptidases". Molecular and Cellular Biochemistry. 30 (2): 111–27. doi:10.1007/bf00227927. PMID 6991912.
- ^ Odya CE, Erdös EG (1981). "Human prolylcarboxypeptidase". Proteolytic Enzymes, Part C. Methods in Enzymology. Vol. 80 Pt C. pp. 460–6. doi:10.1016/s0076-6879(81)80040-7. ISBN 978-0-12-181980-4. PMID 7341916.
External links
[edit]- Lysosomal+Pro-Xaa+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
human prolylcarboxypeptidase entry at OMIM: http://omim.org/entry/176785
