EBK BIOCHEMISTRY
6th Edition
ISBN: 8220102959286
Author: GRISHAM
Publisher: CENGAGE L
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Chapter 23, Problem 19P
Interpretation Introduction
Interpretation:
Why nature uses FAD/FADH2 as a cofactor in the acyl-CoA dehydrogenase reaction rather than NAD+/NADH should be discussed.
Concept Introduction:
The enzymes involving in ß oxidation can be subdivided as membrane bound and soluble enzymes in matrix. As fatty acid chain getting short in successive cycles of ß oxidation, fatty acid chain moves from membrane bound complex to matrix. The first step of ß oxidation is oxidation of the bond between a and ß carbon of fatty acid. This reaction is catalyzed by one of four acyl CoA dehydrogenases. They are very long chain acyl CoA dehydrogenase and dehydrogenases specific for long chain, medium chain and short chain. Acyl CoA dehydrogenases non-covalently binds FAD which is reduced to FADH2 during ß oxidation.
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Chapter 23 Solutions
EBK 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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