alexa Metallocarboxypeptidases
Nutrition

Nutrition

Journal of Nutritional Disorders & Therapy

Author(s): Josep Vendrell, Francesc X Aviles, Lloyd D Fricker

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Metallocarboxypeptidases (CP) catalyze the removal of C-terminal amino acids from proteins and/or peptides. The different members of the CP family differ in their specificity for C-terminal residues and physiological function and can be divided into two subfamilies. Members of the A/B subfamily are generally produced as proenzymes, contain an approximately 300-residue CP catalytic domain, have greatest amino acid sequence identity to the exocrine pancreatic enzymes CPA and CPB, and prefer hydrophobic or basic residues. They function in the breakdown of peptides in food or in other physiological processes ranging from inflammation to fibrinolysis. Members of the N/E group cleave C-terminal basic residues and are not produced as inactive proenzymes but contain an approximately 80-residue region following the 300-residue CP domain with structural homology to transthyretin. They act either extra- or intracellularly in the processing of peptide hormones and neurotransmitters and other physiologically relevant peptides. The tertiary folding of CPs corresponds to the α/β hydrolase fold and is formed by a central mixed parallel/antiparallel eight-strand β-sheet, with a 120° twist between the first and the last strand, over which eight α-helices pack on both sides to form a globular molecule. All of the enzymatically active CPs bind one atom of Zn2+ at the active site. Some members of the CP family that are inactive against standard CP substrates lack some of the cation-binding ligands and may therefore not be able to bind the metal.

This article was published in Encyclopedia of Inorganic and Bioinorganic Chemistry and referenced in Journal of Nutritional Disorders & Therapy

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