Inhibition of mammalian fatty acid synthetase activity by NADP involves decreased mobility of the 4'-phosphopantetheine prosthetic group.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. Presence of one essential arginine that specifically binds the 2′-phosphate of NADPH on each of the ketoacyl reductase and enoyl reductase active sites of fatty acid synthetase
2. Chemical modification of an essential lysine at the active site of enoyl-CoA reductase in fatty acid synthetase
3. Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: reduced nicotinamide adenine dinucleotide phosphate binding and formation and reduction of acetoacetyl-enzyme
4. Role of the enoyl reductase domain in the regulation of fatty acid synthase activity by interdomain interaction.
5. The Effects of Reduced Nicotinamide Adenine Dinucleotide Phosphate, Its Structural Analogues, and Coenzyme A and Its Derivatives on the Rate of Dissociation, Conformation, and Enzyme Activity of the Pigeon Liver Fatty Acid Synthetase Complex
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