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1. ASP has an important role in hydrogen bonding with the His residue in the catalytic...

1. ASP has an important role in hydrogen bonding with the His residue in the catalytic triad of chymotrypsin. ASP and GLU have very similar properties as amino acids. Yet, mutation of ASP to GLU in the traid results in a 10^5 fold decrease in enzyme activity. Why do you think this could be the case?

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Catatylic triad in chymotrypsin include histidine, aspartic acid and serine. Each amino acid have specific role. The function of adaptic acid is to orient the histidine residue and make it better proton accept or that make it suitable for the catalytic mechanism of the enzyme. But if glutamic acid come in place of aspartic acid, GLU is not able to orient the histidine residue, because it have extra methyl group. This lead to less functioning of histidine and aspartic acid. Therefore, the enzyme activity get decreased.

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