Carboxypeptidase - Wikipedia
A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins.
Carboxypeptidase A - Wikipedia
Carboxypeptidase A usually refers to the pancreatic exopeptidase that hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side-chains. Most scientists in the field now refer to this enzyme as CPA1, and to a related pancreatic carboxypeptidase as CPA2.
Carboxypeptidase - an overview | ScienceDirect Topics
Carboxypeptidase A, EC 3.4.12.2, (pancreatic carboxypeptidase) is one of the longest known and most studied peptidases; its properties, structure and active site are known 1–6123456. It acts on many proteins and peptides but C-terminal proline and basic amino acids are not hydrolysed.
Carboxypeptidase - an overview | ScienceDirect Topics
Carboxypeptidases are regulatory enzymes that hydrolyze specific peptide bonds, such as the glutamate residue from methotrexate, leading to the formation of inactive metabolites. You might find these chapters and articles relevant to this topic. In Meyler's Side Effects of …
B1. Carboxypeptidase - Chemistry LibreTexts
A carboxypeptidase is a protease enzyme that hydrolyzes a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide.
Carboxypeptidases - SpringerLink
Carboxypeptidases catalyze the hydrolysis of peptide bonds at the C-terminus of peptides and proteins. This hydrolysis may be a step in the degradation of some substrate molecules or may result in the maturation of others.
Carboxypeptidase A mechanisms. - PMC - National Center for ...
Mechanism of action of carboxypeptidase A in ester hydrolysis. Proc Natl Acad Sci U S A. 1976 Nov; 73 (11):3882–3886. [ PMC free article ] [ PubMed ] [ Google Scholar ]