BIOCHEMISTRY (HARDBACK) W/ACCESS CODE
6th Edition
ISBN: 9781337194204
Author: GARRETT
Publisher: CENGAGE L
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Chapter 24, Problem 4P
Interpretation Introduction
Interpretation:
A maximal separation between the malonyl transferase and the β-ketoacyl-ACP synthase active sites should be estimated.
Concept Introduction:
Fatty acid synthase is a multi-enzyme protein which catalyzes the fatty acid biosynthesis.Major function is catalyzing the formation of palmitate from acetyl CoA and malonyl CoA. Mammalian fatty acid synthase contains two identical protein subunits. Three catalytic domains are in N-terminal section which are β-ketoacyl-ACP synthase, malonyl/acetyl transferase and dehydrase. Four catalytic domains are in C-terminal section, which are enoyl reductase, ketoacyl reductase, acyl carrier protein and thioesterase. N terminal section and C terminal section is separated by 600 residues.
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Chapter 24 Solutions
BIOCHEMISTRY (HARDBACK) W/ACCESS CODE
Ch. 24 - Explaining the Stoichiometry of Fatty Acid...Ch. 24 - Tracing Carbon Atom Incorporation in Fatty Acids...Ch. 24 - Modeling the Regulation of AcetyI-CoA Carboxylase...Ch. 24 - Prob. 4PCh. 24 - Prob. 5PCh. 24 - Prob. 6PCh. 24 - Understanding the Stoichiometry of Cholesterol...Ch. 24 - Prob. 8PCh. 24 - Prob. 9PCh. 24 - Prob. 10P
Ch. 24 - Prob. 11PCh. 24 - Understanding the Mechanism of the...Ch. 24 - Prob. 13PCh. 24 - Understanding the Mechanism of the HMC-CoA...Ch. 24 - Prob. 15PCh. 24 - Prob. 16PCh. 24 - Prob. 17PCh. 24 - Prob. 18PCh. 24 - Prob. 19PCh. 24 - Prob. 20PCh. 24 - Prob. 21PCh. 24 - Prob. 22PCh. 24 - Prob. 23PCh. 24 - Prob. 24PCh. 24 - Prob. 25P
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