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an enzyme group of the hydrolase class (carboxypeptidase-A, carboxypeptidase-B, and yeast car-boxypeptidase) that catalyze the stepped hydrolysis of polypeptides from the C-end, that is, from the amino acid that contains a free carboxyl group (—COOH). The molecular weight of car-boxypeptidases exceeds 34, 000. Carboxypeptidase-A is most active on aromatic amino acids; carboxypeptidase-B, on lysine or arginene; and yeast carboxypeptidase, on glycine or lysine. In addition, carboxypeptidases have esterase activity (the ability to split ether bonds). Carboxypeptidase-A enters the duodenum from the pancreas where it is produced in the form of inactive procarboxypeptidase-A, which becomes carboxypeptidase-A, primarily under the influence of trypsin.
REFERENCESDixon, M., and E. Webb. Fermenty. Moscow, 1966. (Translated from English.)
Mosolov, V. V. Proteoliticheskie fermenty. Moscow, 1971.