Abstract
The de novo synthesis of saturated fatty acids, studied in a variety of biological systems, is catalyzed by two enzyme systems, acetyl-CoA carboxylase and fatty acid synthetase. These enzyme complexes are found in the cell cytoplasm when cells are ruptured and the cellular components are fractionated by usual techniques. All the carbon atoms of the fatty acids are derived from acetyl-CoA. Although palmitate is the major fatty acid that is produced by most biosynthetic systems, the chain length of the fatty acid that is produced varies in different biological sources and under different experimental conditions. Examination of the substrates of fatty acid synthesis, acetyl-CoA, adenosine triphosphate (ATP), and nicotinamide adenine dinucleotide phosphate-oxidase (NADPH), suggests that this biosynthetic pathway can be controlled by regulation of the availability of these substrates. Acetyl-CoA carboxylase catalyzes the first reaction in the synthesis of fatty acids, which is unique to this biosynthetic pathway, and, therefore, this enzyme is regulated.
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