First step His 57 catalyzes removal of H from Ser 195 hydroxyl. The portion (the C-terminal end) of original substrate with the new amino terminus diffuses away. Ser 195's nucleophilic O attacks carbonyl C of substrate. His 57 donates H to Ser 195 O, leading to collapse of tetrahedral intermediate. Water donates H to His 57. Resulting OH attacks carbonyl of remaining substrate. 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.
First step His 57 catalyzes removal of H from Ser 195 hydroxyl. The portion (the C-terminal end) of original substrate with the new amino terminus diffuses away. Ser 195's nucleophilic O attacks carbonyl C of substrate. His 57 donates H to Ser 195 O, leading to collapse of tetrahedral intermediate. Water donates H to His 57. Resulting OH attacks carbonyl of remaining substrate. 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.
Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Chapter6: Energy, Enzymes, And Biological Reactions
Section: Chapter Questions
Problem 8TYK: Which of the following statements about the allosteric site is true? a. The allosteric site is a...
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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.
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