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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. 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

1. 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.
2. 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

• 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

• Biology

• EC 3.4.16