Abstract
The synthesis of palmitic acid by avian fatty acid synthetase occurs through successive elongation of the acetyl primer by two-carbon acyl residues from malonyl-CoA, and reduction of the resulting ketoacyl intermediates by NADPH to corresponding saturated acyl derivatives. After completion of seven elongation cycles, enzyme-bound palmitate is released as the free acid. The enzyme complex is a dimeric molecule comprised of identical subunits. Each subunit contains, in addition to active sites for component reactions, a phosphopantetheine SH group which serves as a carrier for the covalently attached acyl intermediates (1).
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© 1988 Springer-Verlag New York Inc.
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Hsu, R.Y. (1988). Fatty Acid Synthetase of Chicken Liver: A Novel Active-Site Structure for Condensation Comprised of SH Groups from a Cysteine Residue and an Oscillating Phosphopantetheine Swinging Arm on Adjacent Subunits. In: Chock, P.B., Huang, C.Y., Tsou, C.L., Wang, J.H. (eds) Enzyme Dynamics and Regulation. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3744-0_3
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DOI: https://doi.org/10.1007/978-1-4612-3744-0_3
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