MRCP UK EXAMINATIONS

Detailed explanation-1: -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.

Detailed explanation-2: -Carboxypeptidase M (EC 3.4. 17.12) belongs to the family of the carboxypeptidases. These enzymes remove C-terminal amino acids from peptides and proteins and exert roles in the physiological processes of blood coagulation/fibrinolysis, inflammation, food digestion and pro-hormone and neuropeptide processing.

Detailed explanation-3: -Carboxypeptidase A (CPA, EC 3.4. 17.1) is a monozinc exopeptidase from the pancreas, specializing in the elimination of a hydrophobic C-terminal amino acid by cleaving the backbone amide bond. In addition to its natural substrates, CPA also hydrolyzes esters with similar configurations, often with faster rates.

Detailed explanation-4: -Carboxypeptidase A (CPA) is a zinc-containing metalloprotease that removes the amino acid residue from the C-terminal of a peptide chain. It has been one of the most intensively studied enzymes in catalytic MIP field. The catalytic action of CPA involves two guanidinium groups and a Zn2+ ion.

Detailed explanation-5: -Carboxypeptidase is an exopeptidase that specifically hydrolyzes the C-terminal peptide bond and releases the C-terminal amino acid. Two problems are associated with its use: the substrate specificity of the enzyme and the continuous action of the enzyme.