This enzyme, which has been characterized from the bacterium Pseudomonas aeruginosa PAO1, catalyses the condensation of octanoyl-CoA, obtained from exogenously supplied fatty acids via beta-oxidation, with malonyl-[acp], forming 3-oxodecanoyl-[acp], an intermediate of the fatty acid elongation cycle. The enzyme provides a shunt for beta-oxidation degradation intermediates into de novo fatty acid biosynthesis.
the KASIII domain-containing enzyme FabY from open reading frame PA3286 shunts fatty acid degradation intermediates from the beta-oxidation pathway by condensing octanoyl-CoA with malonyl-ACP to make beta-keto-decanoyl-ACP, a key building block common to saturated fatty acids, unsaturated fatty acids, and lipopolysaccharides
FabY, a beta-ketoacyl synthase KASI/II domain-containing enzyme that condenses acetyl-CoA with malonyl-acyl carrier protein (ACP) to make the fatty acid synthesis, FAS, primer beta-acetoacetyl-ACP. FabY is an enzyme required for FAS initiation in the absence of exogenous fatty acids
gene fabY is replaced with fabH (pTMT123) or deleted (pTMT124) in Pseudomonas aeruginosa strain PAO1. The fabY deletion strain grows slowly in comparison to the fabHEc exchange control without C10 supplementation, synthetic lethal analysis for fabY with KASIII domain fabH orthologues and fatty acid rescue, overview. The fabY deletion is synthetic lethal when introduced into the KASIII domain knockout strain TMT16. Synthetic lethal relationship between PA3286 and fabY indicates shared acetyl-CoA:malonyl-ACP condensing activity. PA3286 cross complements fabH and confers a fatty acid shunt in Escherichia coli