Disease relevance of fadD

• In Escherichia coli this enzyme, encoded by the fadD gene, is required for the coupled import and activation of exogenous long-chain fatty acids [1].
• A fadD mutant of Sinorhizobium meliloti shows multicellular swarming migration and is impaired in nodulation efficiency on alfalfa roots [2].
• Gene fadD33 of Mycobacterium tuberculosis, one of the 36 homologues of gene fadD of Escherichia coli identified in the M. tuberculosis genome, predictively encodes an acyl-CoA synthase, an enzyme involved in fatty acids metabolism [3].

High impact information on fadD

• Genetic studies have allowed the cloning, sequencing, and disruption of the genes included in the pha locus (phaC1, phaC2, and phaZ) as well as those related to the biosynthesis of precursors (fadD) or to the catabolism of their derivatives (acuA, fadA, and paa genes) [4].
• Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase [5].
• Primer extension of total in vivo mRNA from two fadD-specific oligonucleotides defined the transcriptional start at an adenine residue 60 base pairs upstream from the predicted translational start site [5].
• The acyl-CoA synthetase structural gene, fadD, has been identified on clone 6D1 of the Kohara E. coli gene library and by a process of subcloning and complementation analyses shown to be contained on a 2.2-kilobase NcoI-ClaI fragment of genomic DNA [5].
• Transport of long-chain fatty acids (LCFA) across the cytoplasmic membrane of Escherichia coli requires functional fadL and fadD genes [6].

Chemical compound and disease context of fadD

• In trans expression of multicopy fadD restored growth on oleate, control of motility and the symbiotic phenotype of QS77, as well as acyl-CoA synthetase activity of an Escherichia coli fadD mutant [2].

Biological context of fadD

• All the fad-lacZ fusions examined (fadBA, fadL, and fadD) are increasingly expressed in stationary phase with kinetics similar to that of the increased expression of uspA [7].
• The incorporation of exogenous [1-14C]palmitate into phosphatidylethanolamine in fadD mutants was inhibited by chloramphenicol and was depressed by preventing the acylation of the amino terminus of the lipoproteins with the antibiotic globomycin [8].
• 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 [9].

Associations of fadD with chemical compounds

• This family is extended by several new members and subdivided into four groups. fadD is assigned to a subgroup that does not include long chain acyl-CoA synthetases from eukaryotic organisms [10].
• In fadD strains, exogenous fatty acids were introduced exclusively into the 1-position of phosphatidylethanolamine [11].
• The fadD gene codes for an acyl-CoA synthetase (fatty acid: CoA ligase (AMP forming] which has broad chain length specificity and is loosely bound to the cytoplasmic membrane [6].
• Although mutations in two genes (fadD and fadL) involved in fatty acid failed to affect lipoate utilization, disruption of the smp gene severely decreased lipoate utilization [12].
• Replacing the partially defective fadD gene of strain L8-2/3 with a wild type allele conferred on this strain the palmitate sensitivity and the acyltransferase activity of the parent strain L8-2 [13].

Other interactions of fadD

• Using P1 mediated cotransduction, we mapped pel- mutations between markers fadD and eda in the interval of minute 40 of the revised E. coli K-12 map [14].
• The biosynthesis of the acyl moieties in murein lipoprotein was studied by fusion of [3H]palmitate-labeled phospholipid vesicles with intact cells of an fadD mutant of Escherichia coli [15].

References