Fatty acid biosynthetic reactions, scheme

The last step in the fatty acid biosynthetic pathway is catalyzed by enoyl-acyl carrier protein (ACP) reductase, which is responsible for reduction of the double bond in the enoyl-ACP derivative (Heath and Rock, 1995 Payne et al., 2002). While fabl genes encode enoyl-ACP reductases (FabI enzymes) in S. aureus and E. coli, an alternative enoyl-ACP reductase, FabK, replaces the function of Fabl in a number of bacterial species such as Streptococcus pneumoniae (Heath and Rock, 2000). More interestingly, a number of bacterial species (such as Enterococcus faecalis and Pseudomonas aeruginosa) possess both the Fabl and FabK enzymes (Heath and Rock, 2000). To discover Fabl-specific antibacterial inhibitors, Payne and colleagues at GlaxoSmithKline (GSK) developed assays for various versions of enoyl-ACP reductases (Payne et al., 2002 Seefeld et al., 2003) based on the following reaction scheme ... 

Spener and Mangold, 1974) in a manner similar to the biosynthesis of prostaglandins (Lands et al., 1977). However, polyunsaturated fatty acids that would undergo such a reaction have not been found in various tissues and cell cultures of Flacourtiaceae (Spener and Mangold, 1974, 1975 Spener et al., 1974). Alternatively, the occurrence of an homologous series of even-numbered cyclopentenyl fatty acids implied a biosynthetic scheme analogous to that for the common fatty acids. 

The Fatty Acid Synthase Enzyme Systems The FAS enzyme systems are central for the biosynthesis of saturated fatty acids [1] and share many similarities with the polyketide synthases (PKSs) involved in the biosynthesis of many polyketides [6] see Section 2.1 for details. Common precursors, functional gronps, and reactions are involved in each biosynthetic step. Saturated fatty acids, such as palmitic acid (1, Scheme 3.2), represent a rather small and structurally simple class of natural products produced by the FAS enzyme systems. The FAS enzyme system in animals is a large multifunctional protein with seven individnal... 

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