Carboxypeptidase C
From Wikipedia, the free encyclopedia
Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, deamidase, lysosomal carboxypeptidase A, phaseolin) is a peptidase, an enzyme that degrades proteins. This enzyme catalyses the release of a C-terminal amino acid with broad specificity.[1][2][3][4]
This enzyme is a carboxypeptidase with optimum activity at pH 4.5-6.0. It is inhibited by diisopropyl fluorophosphate.
