Lysosomal Pro-X carboxypeptidase explained

Lysosomal Pro-Xaa carboxypeptidase
Ec Number:3.4.16.2
Cas Number:9075-64-3

Lysosomal Pro-Xaa carboxypeptidase (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.

External links

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

Notes and References

  1. Walter R, Simmons WH, Yoshimoto T . Proline specific endo- and exopeptidases . Molecular and Cellular Biochemistry . 30 . 2 . 111–27 . April 1980 . 6991912 . 10.1007/bf00227927 .
  2. Book: Odya CE, Erdös EG . Human prolylcarboxypeptidase . Proteolytic Enzymes, Part C . Methods in Enzymology . 80 Pt C . 460–6 . 1981 . 7341916 . 10.1016/s0076-6879(81)80040-7 . 978-0-12-181980-4 .