Disease relevance of fadE

• Fusion of the lacZ gene coding for beta-galactosidase to the fadA,B and fadE operons was accomplished by using the phage Mu d (Apr lac) [1].
• The enigmatic Escherichia coli fadE gene is yafH [2].
• Genes encoding acyl-CoA dehydrogenase (AcdH) homologues from Streptomyces coelicolor and Streptomyces avermitilis provide insights into the metabolism of small branched-chain fatty acids and macrolide antibiotic production [3].
• Acyl-CoA dehydrogenase gene (yafH) of Escherichia coli was expressed together with polyhydroxyalkanoate synthase gene (phaC(Ac)) and (R)-enoyl-CoA hydratase gene (phaJ(Ac)) from Aeromonas caviae [4].
• Coexpression of acyl-CoA dehydrogenase gene (yafH) from E. coli and Vitreoscilla hemoglobin gene (vgb) from Vitreoscilla together with the whole A. hydrophila CGMCC 0911 polyhydroxyalkanoate synthesis operon facilitated cell growth and polyhydroxyalkanoate accumulation in E. coli [5].

High impact information on fadE

• Functional role of the active site glutamate-368 in rat short chain acyl-CoA dehydrogenase [6].
• Our prior genome array analyses showed that transcription of the yafH gene is controlled by the FadR regulatory protein [2].
• Five enzymes of the fatty acid beta-oxidation pathway, acyl-coenzyme A (CoA) synthase, crotonase, thiolase, beta-hydroxyacyl-CoA dehydrogenase, and acyl-CoA dehydrogenase, were identified [7].
• These results demonstrate that the previously observed regulation of both the fadA and fadE operons is at the transcriptional level [1].
• NMR spectral data confirmed that the oxidized product of isobutyryl-CoA is methacrylyl-CoA, which is the expected product at the acyl-CoA dehydrogenase step in the catabolism of valine in streptomycetes [3].

Biological context of fadE

• Semi-quantitative reverse transcription PCR analysis showed that the additional expression of fadD in E. coli strongly induced the expression of both fadE and fadBA [8].
• These results are consistent with the acdH gene encoding an acyl-CoA dehydrogenase with a broad substrate specificity that has a role in the catabolism of branched-chain amino acids in S. coelicolor and S. avermitilis [3].

Associations of fadE with chemical compounds

• Feeding studies with 13C triple-labelled isobutyrate revealed a significant decrease in the incorporation of label into the methylmalonyl-CoA-derived positions of avermectin in the acdH mutant [3].
• Disruption of the S. avermitilis acdH produced a mutant unable to grow on solid minimal medium containing valine, isoleucine or leucine as sole carbon sources [3].
• We cloned the gene of rat mitochondrial medium-chain acyl-CoA dehydrogenase into a bacterial expression vector pLM1 with six continuous histidine codons attached to the 3' of the gene [9].

Analytical, diagnostic and therapeutic context of fadE

• Our overexpression in E. coli and one-step purification of the highly active rat mitochondrial medium-chain acyl-CoA dehydrogenase greatly facilitated our further investigation of this enzyme, and our result from site-directed mutagenesis increased our understanding of medium-chain acyl-CoA dehydrogenase [9].

References