Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Textbook Question
Chapter 23, Problem 21P
Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic
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A histidine residue in the active site of aspartate transcarbamoylase is thought to be important in stabilizing the transition state of the bound substrates. Predict the pH dependence of the catalytic rate, assuming that this interaction is essential and dominates the pHactivity profile of the enzyme.
Describe the mechanism of a-chymotrypsin. Explain the roles of constituents of the
catalytic triad, their modes of catalysis, and the significance of the oxyanion hole in the
catalysis.
Order the cofactors based on their use in the mechanism of the a-etogluterate dehydrogenase complex.
1. Stabilizes a carbanion due to decarboxylation
2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction
3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase
4. Final electron acceptor in the overall reaction catalyzed by this complex
1
2
3
4
answer choices: lipoamide, biotin, 2 Fe - 2S cluster, TPP, NAD+, FAD
Chapter 23 Solutions
Biochemistry
Ch. 23 - Prob. 1PCh. 23 - Determining the Amount of ATP Produced from Fatty...Ch. 23 - Prob. 3PCh. 23 - Examining the Labeling of Glucose from 14C.labeled...Ch. 23 - Prob. 5PCh. 23 - Prob. 6PCh. 23 - Prob. 7PCh. 23 - Prob. 8PCh. 23 - Prob. 9PCh. 23 - Prob. 10P
Ch. 23 - Prob. 11PCh. 23 - Understanding Human Energy Consumption During...Ch. 23 - Prob. 13PCh. 23 - Prob. 14PCh. 23 - Prob. 15PCh. 23 - Extending the Mechanism of Methylmalonyl-CoA...Ch. 23 - Prob. 17PCh. 23 - Prob. 18PCh. 23 - Prob. 19PCh. 23 - Understanding a Ubiquitous Series of Metabolic...Ch. 23 - Using the ActiveModel for enoyl-CoA dehydratase,...
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