I think the source is the pancreas
Yes.
The substrate of carboxypeptidase is a peptide or protein molecule with a terminal amino acid that contains a free carboxyl group. Carboxypeptidase cleaves this terminal amino acid from the substrate by hydrolyzing the peptide bond.
Aminopeptidase
Carboxypeptidase is secreted by Pancreas in inactive form (procarboxypeptidase) and is activated by trypsin. Carboxypeptidase is also secreted by small intestine as brush border enzyme. Reference: Human Anatomy and Physiology by Elaine N. Marieb
Carboxypeptidase breaks down peptides by cleaving off individual amino acids from the C-terminal end of the peptide chain.
Aminopeptidase & carboxypeptidase
The two enzymes differ based on where they cleave the protein being digested. The amino peptidase cleaves the protein from the amino terminus while the carboxypeptidase cleaves the protein from the carboxy terminus.
carboxypeptidase
Zinc in the enzyme carboxypeptidase likely functions as a cofactor, helping to stabilize the enzyme's structure and assist in catalyzing the reaction by participating in binding and activation of the substrate.
Eric Portelance has written: 'The effect of carboxypeptidase N on small cell lung carcinoma cells'
Susan Maria Certossi has written: 'Identification of creative kinase conversion factor as carboxypeptidase N'
Zinc serves as a cofactor in the active site of carboxypeptidase by stabilizing the reaction intermediate during peptide cleavage. It acts as a Lewis acid, facilitating the nucleophilic attack on the peptide bond. Zinc also helps orient the substrate in the active site for optimal binding and catalysis.