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 you.

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In the carboxypeptidase mechanism, the enzyme interacts with its substrate, a peptide chain, through weak noncovalent bonds such as hydrogen bonding, van der Waals forces, and electrostatic interactions. These weak interactions allow the enzyme to bind to the substrate in a specific orientation and facilitate the catalytic reaction.

When the enzyme-substrate complex forms, the weak bonds between the enzyme and the substrate can exert a pulling force on the peptide bond, stretching it and lowering its bond energy. This stretching weakens the bond, making it more susceptible to cleavage.

To understand this in more detail, you can delve into the concept of bond energies. Bond energy refers to the amount of energy required to break a specific bond. Peptide bonds are typically strong and require a significant amount of energy to break. However, when an enzyme binds to a substrate and weakens the peptide bond by stretching it, the bond energy decreases. This lower bond energy makes it easier for the bond to be broken during the catalytic process.

To conclude, in the carboxypeptidase mechanism, the weak bonds between the enzyme and the substrate stretch the peptide bond of the substrate, resulting in a lower bond energy, and thus facilitating the cleavage of the bond by the enzyme.