| Type: | Domain | Name: | Proteinase inhibitor, carboxypeptidase propeptide |
| Description: | The peptidases are synthesised as inactive molecules, zymogens, with propeptides that must be removed by proteolytic cleavage to activate the enzyme. Structural studies of carboxypeptidases A and B reveal the propeptide toexist as a globular domain, followed by an extended alpha-helix; this shields the catalytic site, without specifically binding to it, while thesubstrate-binding site is blocked by making specific contacts [, ].Members of this propeptide family are found in the metallocarboxypeptidases: A1, A2 [], A3, A4, A5, A6, U, insect gut carboxypeptidase and B [], and and are associated with peptidases belonging to MEROPS peptidase family M14A. Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (activation peptide) accounts for up to a quarter of the total length of the peptidase. | Short Name: | Prot_inh_M14A |
