Summary: Carboxypeptidase activation peptide
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Carboxypeptidase activation peptide Provide feedback
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, and is responsible for modulation of folding and activity of the pro-enzyme.
Aloy P, Catasus L, Villegas V, Reverter D, Vendrell J, Aviles FX; , Biol Chem 1998;379:149-155.: Comparative analysis of the sequences and three-dimensional models of human procarboxypeptidases A1, A2 and B. PUBMED:9524066 EPMC:9524066
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003146
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 to exist as a globular domain, followed by an extended alpha-helix; this shields the catalytic site, without specifically binding to it, while the substrate-binding site is blocked by making specific contacts [PUBMED:7674922, PUBMED:1548696].
Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (propeptide or activation peptide) accounts for up to a quarter of the total length of the peptidase.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||carboxypeptidase activity (GO:0004180)|
|Biological process||proteolysis (GO:0006508)|
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