| Description | There are conserved sites matching these three zinc-ligands - this entry and . If a protein includes both signatures, the probability of it being a eukaryotic zinc carboxypeptidase is very high. There are a number of different types of zinc-dependent carboxypeptidases (EC 3.4.17.-) [ , ]. All these enzymes seem to be structurally and functionally related. Some enzymes that belong to this family are listed below.Carboxypeptidase A1 (EC 3.4.17.1), a pancreatic digestive enzyme that can remove all C-terminal amino acids with the exception of Arg, Lys and Pro.Carboxypeptidase A2 (EC 3.4.17.15), a pancreatic digestive enzyme with a specificity similar to that of carboxypeptidase A1, but with a preference for bulkier C-terminal residues.Carboxypeptidase B (EC 3.4.17.2), also a pancreatic digestive enzyme, but that preferentially removes C-terminal Arg and Lys.Carboxypeptidase N (EC 3.4.17.3) (also known as arginine carboxypeptidase), a plasma enzyme which protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation.Carboxypeptidase H (EC 3.4.17.10) (also known as enkephalin convertase or carboxypeptidase E), an enzyme located in secretory granules of pancreatic islets, adrenal gland, pituitary and brain. This enzyme removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing.Carboxypeptidase M (EC 3.4.17.12), a membrane bound Arg and Lys specific enzyme.Mast cell carboxypeptidase (EC 3.4.17.1), an enzyme with a specificity to carboxypeptidase A, but found in the secretory granules of mast cells.Streptomyces griseus carboxypeptidase (Cpase SG) (EC 3.4.17.-) [ ], which combines the specificities of mammalian carboxypeptidases A and B.Thermoactinomyces vulgaris carboxypeptidase T (EC 3.4.17.18) (CPT) [ ], which also combines the specificities of carboxypeptidases A and B.All of these enzymes bind an atom of zinc. Three conserved residues are implicated in the binding of the zinc atom: two histidines and a glutamic acid. | Name | Zinc carboxypeptidases, zinc-binding region 1 |
| Short Name | CARBOXYPEPT_ZN_1 | Type | Binding_site |
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