Lysosomal Prolylcarboxypeptidase
   HOME

TheInfoList



OR:

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 Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. A ...
. This enzyme catalyses the following
chemical reaction A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the pos ...
: Cleavage of a -Pro-Xaa bond to release a
C-terminal The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is ...
amino acid A lysosomal peptidase active at acidic pH that inactivates
angiotensin II Angiotensin is a peptide hormone that causes vasoconstriction and an increase in blood pressure. It is part of the renin–angiotensin system, which regulates blood pressure. Angiotensin also stimulates the release of aldosterone from the adre ...
. This enzyme is inhibited by
diisopropyl fluorophosphate Diisopropyl fluorophosphate (DFP) or Isoflurophate is an oily, colorless liquid with the chemical formula C6H14FO3P. It is used in medicine and as an organophosphorus insecticide. It is stable, but undergoes hydrolysis when subjected to moisture. ...
.


References


External links

* human prolylcarboxypeptidase entry at OMIM: http://omim.org/entry/176785 {{Portal bar, Biology, border=no EC 3.4.16