Search results for "Acyl-CoA"

showing 10 items of 42 documents

Effect of acyl-CoA oxidase activity on the accumulation of gamma-decalactone by the yeast Yarrowia lipolytica: a factorial approach.

2007

International audience; beta-Oxidation is a cyclic pathway involved in the degradation of lipids. In yeast, it occurs in peroxisomes and the first step is catalyzed by an acyl-CoA oxidase (Aoxp). The yeast Yarrowia lipolytica possesses several genes (POX) coding for Aoxps. This study is based on the factorial analysis of results obtained with the many POX derivative strains that have been constructed previously. The effect of interactions between Aoxps on the acyl-CoA oxidase (Aox) activity was important even at the second order. We then investigated the effect of Aox activity on growth and lactone production. Aox activity was correlated with acidification of the medium by cells and with ce…

0106 biological sciencesYarrowia lipolyticaMESH: Enzyme ActivationMetabolic Clearance RateMESH: Factor Analysis StatisticalYarrowiaBiologymodèleModels Biological01 natural sciencesApplied Microbiology and BiotechnologyLactones03 medical and health sciencesEnzyme activatorSpecies SpecificityMESH: Computer Simulation010608 biotechnologyCombinatorial Chemistry TechniquesAcyl-CoA oxidaseMESH: Species SpecificityComputer Simulation030304 developmental biologychemistry.chemical_classificationMESH: Metabolic Clearance Rate0303 health sciencesOxidase testmétabolisme des acides grasAcyl-CoA oxidase activityMESH: Acyl-CoA OxidaseMESH: Models BiologicalYarrowia[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyGeneral MedicinePeroxisomebiology.organism_classificationYeastEnzyme ActivationBiochemistrychemistrylactoneMolecular MedicineMESH: Combinatorial Chemistry TechniquesMESH: YarrowiaAcyl-CoA OxidaseFactor Analysis StatisticalLactoneMESH: Lactones
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Protective Effect of Cactus Cladode Extracts on Peroxisomal Functions in Microglial BV-2 Cells Activated by Different Lipopolysaccharides

2017

International audience; In this study, we aimed to evaluate the antioxidant and anti-inflammatory properties of Opuntia ficus-indica cactus cladode extracts in microglia BV-2 cells. Inflammation associated with microglia activation in neuronal injury can be achieved by LPS exposure. Using four different structurally and biologically well-characterized LPS serotypes, we revealed a structure-related differential effect of LPS on fatty acid β-oxidation and antioxidant enzymes in peroxisomes: Escherichia coli-LPS decreased ACOX1 activity while Salmonella minnesota-LPS reduced only catalase activity. Different cactus cladode extracts showed an antioxidant effect through microglial catalase activ…

0301 basic medicineAntioxidant[SDV]Life Sciences [q-bio]medicine.medical_treatmentAnti-Inflammatory AgentsPharmaceutical Scienceacyl-CoA oxidase 1; catalase; β-oxidation; <i>Escherichia coli</i>; lipopolysaccharides; LPS; nitric oxide; Opuntia; peroxisomes; <i>Salmonella minnesota</i>AntioxidantsAnalytical ChemistryMicechemistry.chemical_compoundSalmonellaDrug Discoverychemistry.chemical_classificationbiologyMicrogliaFatty AcidscatalaseOpuntiaPeroxisome[SDV] Life Sciences [q-bio]Neuroprotective Agentsmedicine.anatomical_structureBiochemistryChemistry (miscellaneous)CatalaseMolecular MedicineACOX1Microgliamedicine.symptomOxidation-ReductionLPSInflammationArticleCell LineNitric oxideMicrobiologylcsh:QD241-44103 medical and health scienceslcsh:Organic chemistrynitric oxideEscherichia colimedicineAnimalsSalmonella minnesotaPhysical and Theoretical Chemistryacyl-CoA oxidase 1[ SDV ] Life Sciences [q-bio]Plant ExtractsOrganic ChemistryperoxisomeslipopolysaccharidesOxidative Stress030104 developmental biologyEnzymechemistrybiology.proteinβ-oxidationReactive Oxygen SpeciesMolecules
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Circadian and Dopaminergic Regulation of Fatty Acid Oxidation Pathway Genes in Retina and Photoreceptor Cells.

2016

The energy metabolism of the retina might comply with daily changes in energy demand and is impaired in diabetic retinopathy-one of the most common causes of blindness in Europe and the USA. The aim of this study was to investigate putative adaptation of energy metabolism in healthy and diabetic retina. Hence expression analysis of metabolic pathway genes was performed using quantitative polymerase chain reaction, semi-quantitative western blot and immunohistochemistry. Transcriptional profiling of key enzymes of energy metabolism identified transcripts of mitochondrial fatty acid β-oxidation enzymes, i.e. carnitine palmitoyltransferase-1α (Cpt-1α) and medium chain acyl-CoA dehydrogenase (A…

0301 basic medicineMalePhysiologyDopamineMice ObeseGene Expressionlcsh:MedicineBiochemistryAcyl-CoA DehydrogenaseMice0302 clinical medicineCatecholaminesEndocrinologyMedicine and Health SciencesAminesEnzyme Chemistrylcsh:ScienceBeta oxidationMice KnockoutMice Inbred C3HMultidisciplinaryOrganic CompoundsDopaminergicFatty AcidsNeurochemistryDiabetic retinopathyNeurotransmittersCircadian RhythmChemistryCircadian Oscillatorsmedicine.anatomical_structurePhysical SciencesFemaleAnatomyOxidation-Reductionmedicine.drugResearch Articlemedicine.medical_specialtyBiogenic AminesEndocrine DisordersOcular AnatomyBiologyRetinaEnzyme Regulation03 medical and health sciencesOcular SystemInternal medicinemedicineGeneticsDiabetes MellitusAnimalsPhotoreceptor CellsGene RegulationCircadian rhythmCarnitineACADMRetinaDiabetic RetinopathyCarnitine O-PalmitoyltransferaseReceptor Melatonin MT1Receptors Dopamine D4Organic Chemistrylcsh:RChemical CompoundsBiology and Life Sciencesmedicine.diseaseHormonesMice Inbred C57BLMetabolic pathwayDisease Models Animal030104 developmental biologyEndocrinologyMetabolismMicroscopy FluorescenceMetabolic DisordersEnzymologylcsh:Qsense organsEnergy MetabolismPhysiological ProcessesChronobiology030217 neurology & neurosurgeryNeurosciencePLoS ONE
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Conjugated linoleic acid isomers in mitochondria

2002

The beneficial effects exerted by low amounts of conjugated linoleic acids (C222222237) suggest that CLA are maximally conserved and raise the question about their mitochondrial oxidizability. Cis-9,trans-11-C18:2 (CLA1) and trans-10,cis-12-C18:2 (CLA2) were compared to cis-9,cis-12-C18:2 (linoleic acid; LA) and cis-9-C16:1 (palmitoleic acid; PA), as substrates for total fatty acid (FA) oxidation and for the enzymatic steps required for the entry of FA into rat liver mitochondria. Oxygen consumption rate was lowest when CLA1 was used as a substrate with that on CLA2 being intermediate between it and the respiration on LA and PA. The order of the radiolabeled FA oxidation rate was PA >> LA >…

030309 nutrition & dieteticsConjugated linoleic acidLinoleic acidCAT-IIchemistry.chemical_elementQD415-436BiochemistryOxygenacyl-CoA synthetase03 medical and health scienceschemistry.chemical_compoundEndocrinologymedicinePalmitoleic acidCarnitineBeta oxidation030304 developmental biologychemistry.chemical_classification0303 health sciencescarnitineFatty acidCell BiologyCLAEnzymechemistryBiochemistryCAT-Irespirationmedicine.drugJournal of Lipid Research
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Involvement of acyl coenzyme A oxidase isozymes in biotransformation of methyl ricinoleate into gamma-decalactone by Yarrowia lipolytica.

2000

ABSTRACT We reported previously on the function of acyl coenzyme A (acyl-CoA) oxidase isozymes in the yeast Yarrowia lipolytica by investigating strains disrupted in one or several acyl-CoA oxidase-encoding genes ( POX1 through POX5 ) (H. Wang et al., J. Bacteriol. 181:5140–5148, 1999). Here, these mutants were studied for lactone production. Monodisrupted strains produced similar levels of lactone as the wild-type strain (50 mg/liter) except for Δ pox3 , which produced 220 mg of γ-decalactone per liter after 24 h. The Δ pox2 Δpox3 double-disrupted strain, although slightly affected in growth, produced about 150 mg of lactone per liter, indicating that Aox2p was not essential for the biotra…

Applied Microbiology and BiotechnologyIsozymeLactonesMESH : BiotransformationBiotransformation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAcyl-CoA oxidase[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Oxidoreductases[INFO.INFO-BT]Computer Science [cs]/BiotechnologyMESH: Saccharomycetales[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyComputingMilieux_MISCELLANEOUSBiotransformationchemistry.chemical_classificationMESH : Isoenzymes[SDV.EE]Life Sciences [q-bio]/Ecology environmentMESH: BiotransformationOxidase testEcologyStrain (chemistry)biologyChemistryMESH: Acyl-CoA OxidaseYarrowiaMESH : SaccharomycetalesACYLCOENZYME Abiology.organism_classificationMESH : OxidoreductasesPhysiology and BiotechnologyYeastMESH : LactonesMESH: Ricinoleic AcidsIsoenzymes[INFO.INFO-BT] Computer Science [cs]/BiotechnologyBiochemistryMESH : Ricinoleic AcidsSaccharomycetalesMESH: IsoenzymesMESH : Acyl-CoA OxidaseAcyl-CoA OxidaseOxidoreductasesRicinoleic AcidsLactone[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyMESH: LactonesFood ScienceBiotechnology
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Stimulation of peroxisomal palmitoyl-CoA oxidase activity by ciprofibrate in hepatic cell lines: comparative studies in Fao, MH1C1 and HepG2 cells.

1993

The response of two rat cell lines, Fao and MH1C1, and one human cell line, HepG2, to the peroxisome proliferator ciprofibrate, was studied. Using a fluorometric assay for palmitoyl-CoA oxidase, the dose- and time-dependent increase of this enzymatic activity was determined. From the lowest concentration (100 microM) stimulation is evident in the two rat cell lines. In the Fao line, the activity was stimulated reaching a seven-fold increase over the control level at 250 microM after 72 h of treatment. In the MH1C1 line, the maximum stimulation, four- to five-fold, was obtained at 250 and 500 microM after 72 h. In the HepG2 cell line, activity increased two-fold at 250 microM after 72 h reac…

Carcinoma HepatocellularStimulationBiologyMicrobodiesClofibric AcidLiver Neoplasms ExperimentalmedicineTumor Cells CulturedAcyl-CoA oxidaseAnimalsHumansHypolipidemic AgentsOxidase testLiver NeoplasmsFibric AcidsCell BiologyGeneral MedicinePeroxisomePalmitoyl-CoA oxidase activityBiochemistryLiverCell cultureHepatic stellate cellCiprofibrateOxidoreductasesmedicine.drugBiology of the cell
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Cloning and characterization of the peroxisomal acyl CoA oxidaseACO3 gene from the alkane-utilizing yeastYarrowia lipolytica

1998

The ACO3 gene, which encodes one of the acyl-CoA oxidase isoenzymes, was isolated from the alkane-utilizing yeast Yarrowia lipolytica as a 10 kb genomic fragment. It was sequenced and found to encode a 701-amino acid protein very similar to other ACOs, 67.5% identical to Y. lipolytica Aco1p and about 40% identical to S. cerevisiae Pox1p. Haploid strains with a disrupted allele were able to grow on fatty acids. The levels of acyl-CoA oxidase activity in the ACO3 deleted strain, in an ACO1 deleted strain and in the wild-type strain, suggested that ACO3 encodes a short chain acyl-CoA oxidase isoenzyme. This narrow substrate spectrum was confirmed by expression of Aco3p in E. coli.

CloningOxidase testStrain (chemistry)BioengineeringYarrowiaBiologybiology.organism_classificationApplied Microbiology and BiotechnologyBiochemistryMolecular biologyYeastBiochemistryGene expressionGeneticsAcyl-CoA oxidaseGeneBiotechnologyYeast
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Long-chain fatty acyl-CoA esters induce lipase activation in the absence of a water-lipid interface.

2003

In most lipases a mobile element or lid domain covers the catalytic site of the enzyme and the lid opening event, which usually proceed at a lipid-water interface, is required to form the catalytically competent lipase. We report here a noticeable increase in activity of two fungal lipases assayed in aqueous solution in absence of any interface when adding submicellar concentrations of amphipathic physiological molecules like long-chain acyl-CoAs. The catalytic activity was dramatically dependent on the acyl chain length of the amphiphile and could be related with a lid-opening process. Our data support that lipase activation can be triggered in the absence of a well-defined interface, and …

Conformational changeCatalysisSubstrate SpecificityAcyl-CoAchemistry.chemical_compoundAmphiphileLipaseMolecular Biologychemistry.chemical_classificationAqueous solutionbiologyChemistryWaterEstersCell BiologyLipaseLipid MetabolismGeotrichumLipidsEnzyme ActivationSolutionsEnzymeBiochemistrybiology.proteinAcyl Coenzyme ALong chainRhizopusBiochimica et biophysica acta
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Cloning and tissue expression of two cDNAs encoding the peroxisomal 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in the guinea pig liver

1996

Abstract The 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (HD) is the second enzyme of the peroxisomal β-oxidation pathway. In human and rat, only one HD mRNA has been so far detected in the liver. This paper reports for the first time in a mammal species, the guinea pig, the cloning and sequencing of two cDNAs encoding an HD. The 3,274 nucleotide-cDNA is a strictly identical but longer copy of the 2,494 nucleotide-form. A 2,178 by-open reading frame encodes a protein of 726 amino acids ( M r 79.3 kDa) with the peroxisomal-targeting signal (tripeptide SKL) at the carboxyterminus. Northern blot analysis of HD mRNA identified three mRNAs of respective sizes 3.5, 2.6 and 1.6 kb in the…

DNA ComplementaryGuinea PigsMolecular Sequence DataBiophysicsGene ExpressionDehydrogenasePeroxisomeBiologyKidneyMicrobodiesBiochemistryStructural BiologyComplementary DNAGeneticsAnimalsPhosphofructokinase 2Amino Acid SequenceRNA MessengerNorthern blotCloning Molecular2-Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenaseBifunctional enzymeEnoyl-CoA HydrataseMolecular BiologyCloningBase Sequence3-Hydroxyacyl CoA DehydrogenasesSequence Analysis DNACell BiologyPeroxisomeEnoyl-CoA hydrataseBlotting NorthernGuinea pigMolecular biology3-Hydroxyacyl-CoA DehydrogenaseLiverBiochemistrycDNAFEBS Letters
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Identification and Expression of the SOS Response, aidB-Like, Gene in the Marine Sponge Geodia cydonium: Implication for the Phylogenetic Relationshi…

1998

Sponges (Porifera) are the phylogenetically oldest metazoan organisms. From one member of the siliceous sponges, Geodia cydonium, the cDNA encoding a putative SOS protein, the AidB-like protein of the Ada system from bacteria, was isolated and characterized. The cDNA, GCaidB, comprises an open reading frame of 446 amino acid (aa) residues encoding a polypeptide with a calculated Mr of 49,335. This molecule shows high similarity to the bacterial AidB proteins from Mycobacterium tuberculosis and Escherichia coli and somewhat lower similarities to acyl-CoA dehydrogenases (ADHs) and acyl-CoA oxidases (AOXs). Northern blot analysis confirmed the presence of the complete transcript. The deduced s…

DNA ComplementarySequence analysisMolecular Sequence DataSequence alignmentBiologymedicine.disease_causeAcyl-CoA DehydrogenaseEvolution MolecularBacterial ProteinsPhylogeneticsComplementary DNAGeneticsmedicineAnimalsAmino Acid SequenceSOS Response GeneticsMolecular BiologyGeneEscherichia coliPeptide sequencePhylogenyEcology Evolution Behavior and SystematicsGeneticsBase SequenceEscherichia coli ProteinsAcyl-CoA Dehydrogenase Long-ChainSequence Analysis DNABlotting NorthernInvertebratesPoriferaOpen reading frameBiochemistryOxidoreductasesSequence AlignmentJournal of Molecular Evolution
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