Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that some references may not break out each of these steps individually, but all steps should be ordered. There will be eight steps. First step Last step Answer Bank Resulting OH attacks carbonyl of remaining substrate. Water donates H to His 57. His 57 donates H to Ser 195 O, leading to collapse of tetrahedral intermediate. The portion (the C-terminal end) of original substrate with the new amino terminus diffuses away. His 57 donates H to N of scissile peptide bond, tetrahedral intermediate decomposes. The portion (N-terminal end) of original substrate with the new carboxylate terminus diffuses away. His 57 catalyzes removal of H from Ser 195 hydroxyl. Ser 195's nucleophilic O attacks carbonyl C substrate.

Biochemistry
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Chapter1: Biochemistry: An Evolving Science
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Q23:

Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that some references may not break
out each of these steps individually, but all steps should be ordered. There will be eight steps.
First step
Last step
Answer Bank
Resulting OH attacks carbonyl of remaining substrate.
Water donates H to His 57.
His 57 donates H to Ser 195 O, leading to collapse of tetrahedral intermediate.
The portion (the C-terminal end) of original substrate with the new amino terminus diffuses away.
His 57 donates H to N of scissile peptide bond, tetrahedral intermediate decomposes.
The portion (N-terminal end) of original substrate with the new carboxylate terminus diffuses away.
His 57 catalyzes removal of H from Ser 195 hydroxyl.
Ser 195's nucleophilic O attacks carbonyl C
substrate.
Transcribed Image Text:Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that some references may not break out each of these steps individually, but all steps should be ordered. There will be eight steps. First step Last step Answer Bank Resulting OH attacks carbonyl of remaining substrate. Water donates H to His 57. His 57 donates H to Ser 195 O, leading to collapse of tetrahedral intermediate. The portion (the C-terminal end) of original substrate with the new amino terminus diffuses away. His 57 donates H to N of scissile peptide bond, tetrahedral intermediate decomposes. The portion (N-terminal end) of original substrate with the new carboxylate terminus diffuses away. His 57 catalyzes removal of H from Ser 195 hydroxyl. Ser 195's nucleophilic O attacks carbonyl C substrate.
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