Lysosomal_prolylcarboxypeptidase

Lysosomal Pro-X carboxypeptidase

Lysosomal Pro-X carboxypeptidase

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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
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A lysosomal peptidase active at acidic pH that inactivates angiotensin II. This enzyme is inhibited by diisopropyl fluorophosphate.

References

  1. [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. [2]
    Odya CE, Erdös EG (1981). Human prolylcarboxypeptidase. Methods in Enzymology. Vol. 80 Pt C. pp. 460–6. doi:10.1016/s0076-6879(81)80040-7. PMID 7341916.

human prolylcarboxypeptidase entry at OMIM: http://omim.org/entry/176785
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