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SulfurCarbonUbiquitin-Protein LigasesSulfur CompoundsDNA LigasesSKP Cullin F-Box Protein LigasesSulfur DioxideCarbon DioxideSulfur IsotopesAmino Acids, SulfurCarbon MonoxideNanotubes, CarbonCullin ProteinsUbiquitinationPolynucleotide LigasesUbiquitinMustard GasSulfidesCoenzyme A LigasesThiosulfatesRING Finger DomainsCarbon Monoxide PoisoningSulfur OxidesUbiquitin-Conjugating EnzymesCarbon IsotopesMolecular Sequence DataRNA Ligase (ATP)ChlorobiSulfatesCarbon TetrachlorideF-Box ProteinsAmino Acid SequenceCarbon DisulfideCarbon SequestrationOxidoreductases Acting on Sulfur Group DonorsEndosomal Sorting Complexes Required for TransportUbiquitinsSulfur HexafluorideOxidation-ReductionChromatiaceaeProteasome Endopeptidase ComplexChemical Warfare AgentsSubstrate SpecificitySulfurtransferasesCysteinePeptide SynthasesNitrogenProtein Structure, TertiaryProtein BindingSulfur AcidsUbiquitin-Protein Ligase ComplexesPolyubiquitinUbiquitin-Activating EnzymesPhylogenyMutationCarbon-Oxygen LigasesCarbon Tetrachloride PoisoningChlorobiumHydrogen SulfideProto-Oncogene Proteins c-cblMethionineAtmosphereSequence Homology, Amino AcidSulfitesCatalysisChromatiumBacterial ProteinsProteolysisModels, MolecularS-Phase Kinase-Associated ProteinsProtein Inhibitors of Activated STATSeawaterAcidithiobacillusAir PollutantsSulfonium CompoundsSUMO-1 ProteinBacteriaSaccharomyces cerevisiaeKineticsSmall Ubiquitin-Related Modifier ProteinsSulfur-Reducing BacteriaCulture MediaModels, BiologicalGeologic SedimentsSaccharomyces cerevisiae ProteinsCarbon FootprintEscherichia coliBiodegradation, EnvironmentalCysteine SynthaseAnaerobiosisIron-Sulfur ProteinsBinding SitesAutotrophic ProcessesCarrier ProteinsBiomassCarbon RadioisotopesRNA, Ribosomal, 16SCarbon Compounds, InorganicSumoylationSequence Alignment

Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis. (9/22)

FadD28 from Mycobacterium tuberculosis belongs to the fatty-acyl AMP ligase (FAAL) family of proteins. It is essential for the biosynthesis of a virulent phthiocerol dimycocerosate (PDIM) lipid that is only found in the cell wall of pathogenic mycobacteria. The N-terminal domain, comprising of the first 460 residues, was crystallized by the hanging-drop vapour-diffusion method at 295 K. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.97, b = 60.74, c = 136.54 angstroms. The crystal structure of the N-terminal domain of FadD28 at 2.35 angstroms resolution has been solved using the MAD method.  (+info)

Expression of Vibrio harveyi acyl-ACP synthetase allows efficient entry of exogenous fatty acids into the Escherichia coli fatty acid and lipid A synthetic pathways. (10/22)

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Fatty acid activation in cyanobacteria mediated by acyl-acyl carrier protein synthetase enables fatty acid recycling. (11/22)

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Single-nucleotide polymorphism in the fadD28 gene as a genetic marker for East Asia Lineage Mycobacterium tuberculosis. (12/22)

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A high-throughput screening fluorescence polarization assay for fatty acid adenylating enzymes in Mycobacterium tuberculosis. (13/22)

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The acyl-acyl carrier protein synthetase from Synechocystis sp. PCC 6803 mediates fatty acid import. (14/22)

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Disruption of plastid acyl:acyl carrier protein synthetases increases medium chain fatty acid accumulation in seeds of transgenic Arabidopsis. (15/22)

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Pathways for the incorporation of exogenous fatty acids into phosphatidylethanolamine in Escherichia coli. (16/22)

Two distinct pathways for the incorporation of exogenous fatty acids into phospholipids were identified in Escherichia coli. The predominant route originates with the activation of fatty acids by acyl-CoA synthetase followed by the distribution of the acyl moieties into all phospholipid classes via the sn-glycerol-3-phosphate acyltransferase reaction. This pathway was blocked in mutants (fadD) lacking acyl-CoA synthetase activity. In fadD strains, exogenous fatty acids were introduced exclusively into the 1-position of phosphatidylethanolamine. This secondary route is related to 1-position fatty acid turnover in phosphatidylethanolamine and proceeds via the acyl-acyl carrier protein synthetase/2-acylglycerophosphoethanolamine acyltransferase system. The turnover pathway exhibited a preference for saturated fatty acids, whereas the acyl-CoA synthetase-dependent pathway was less discriminating. Both pathways were inhibited in mutants (fadL) lacking the fatty acid permease, demonstrating that the fadL gene product translocates exogenous fatty acids to an intracellular pool accessible to both synthetases. These data demonstrate that acyl-CoA synthetase is not required for fatty acid transport in E. coli and that the metabolism of exogenous fatty acids is segregated from the metabolism of acyl-acyl carrier proteins derived from fatty acid biosynthesis.  (+info)