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29 April, 09:24

Put the steps of the mechanism of chymotrypsin catalysis in order from first to last. note: your textbook may not break out each of these steps individually, but all steps should be utilized.

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  1. 29 April, 09:28
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    The steps are the following:

    -His 57 catalyses removal of H from Ser 195 hydroxyl.

    -Ser 195's nucleophilic O attacks carbonyl C of substrate.

    -His 57 donates H to N of sissile peptide bond, tetrahedral intermediate decomposes.

    -The portion (the C-terminal end) of original substrate with the new amino terminus diffuses away.

    -Water donates H to His 57

    -Resulting OH attacks carbonyl of ramining substrate

    -His 57 donates H to Ser 195O, leading to collapse of tetrahedral intermediate

    -The portion (N-terminal end) of original substrate with the new carboxylate terminus diffuses away.

    Explanation:

    It can be said that the primary structure of the compound called chymotrypsin is formed by disulfide bonds, in addition to the active site composed of Ser-195, His-57 and Asp-102. Ser-195 is linked to His-57 via a hydrogen bond and to Asp-102 via a hydrogen bond. The function of His-57 is to polarize the hydroxyl group, while Asp-102 targets His-57 and stabilizes it through hydrogen and electrostatic bonds.
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