N-alpha-acetylenkephalin carboxypeptidase

that's a common mechanism in enzymes, not only in carboxypeptidase. However, the point is, there are several of these "weak" bonds and their sum is strong enough to stretch the peptide causing to be better to hydrolyse.

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Why (in detail please) in the carboxypeptidase mechanism, the weak bonds between an enzyme and a substrate will stretch the peptide bond of the substrate which lowers the bond energy? I just want to know why in detail this happens... Thank ...

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... to chymotrypsin Chymotrypsin (secreted as chymotrypsinogen) - made in pancreas, functions in small intestine to break peptide bonds Carboxypeptidase - made in the pancrease, functions in small intestine to break terminal peptide bonds at carboxyl end Aminopeptidase - made in intestinal ...

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