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nature : Specificity can peptide from the C-terminal chain began individually degradation, release of a free amino acid peptide chain outside endonuclease. To proenzyme form in the body. Commonly used in the A, B, C and 4 species of carboxypeptidase, the first two are in common use A, B, C and Y carboxypeptidase four, the first two from animal pancreas, C from citrus leaf, Y exists in yeast cells. The most widely used and most studied is the carboxypeptidase A and B. Carboxypeptidase A can be released except proline, hydroxyproline, arginine and lysine in all C-terminal amino acids, more easily hydrolyzed with the aromatic side chains and big fat Side of the carboxyl-terminal amino acids. While carboxypeptidase B only to alkaline hydrolysis of amino acids (arginine and lysine) for the C-terminal residues of the peptide bond. Carboxypeptidase C specificity of hydroxyproline in addition to all other amino acids. Carboxypeptidase Y on the carboxyl terminal amino acid have extensive hydrolysis, the enzyme has become a multi-protein C-terminal peptide chain analysis tools commonly used enzyme, pancreatic and carboxypeptidase A and B, not the same, it is a non-metal ions in acidic protein, and with lipase enzyme activity.
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