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    Chymotrypsin was able to hydrolyse the substrate N-benzoyl-L-tyrosine ethyl ester (BTEE) but not able to hydrolyse the substrate p-toluene sulphonyyl-L-arginine methyl ester (TAME).

    However the enzyme trypsin was able to hydrolyse both TAME and BTEE substrates, and I was wondering why? And what makes chymotrypsin so much more specific?

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    It is not really that chymotrypsin is so much more specific, but that p-toluene sulphonyyl-L-arginine methyl ester (TAME) has functional groups that are inhibitors of chymotrypsin and not trypsin. Compare the following structures for TAME and tosyl phenylalanyl chloromethyl ketone (TPCK). TPCK is a ...

    Solution Summary

    In this solution we explain why the enzyme trypsin is able to hydrolyse both TAME and BTEE substrates. Additionally, it compares properties of chymotrypsin to trypsin. The solution also includes one reference source for further explanation and research of the subject.