Search results for "Hydrogenase"

showing 10 items of 575 documents

Experimental conditions affect the site of tetrazolium violet reduction in the electron transport chain of Lactococcus lactis

2009

The reduction of tetrazolium salts to coloured formazans is often used as an indicator of cell metabolism during microbiology studies, although the reduction mechanisms have never clearly been established in bacteria. The objective of the present study was to identify the reduction mechanisms of tetrazolium violet (TV) in Lactococcus lactis using a mutagenesis approach, under two experimental conditions generally applied in microbiology: a plate test with growing cells, and a liquid test with non-growing (resting) cells. The results showed that in both tests, TV reduction resulted from electron transfer from an intracellular donor (mainly NADH) to TV via the electron transport chain (ETC), …

DNA Bacterial[SDV]Life Sciences [q-bio]Tetrazolium SaltsMicrobiologyElectron Transport03 medical and health scienceschemistry.chemical_compoundElectron transfer030304 developmental biology0303 health sciencesbiology030306 microbiologyLactococcus lactisNADH dehydrogenaseNADH DehydrogenaseVitamin K 2biology.organism_classificationNADElectron transport chainCulture MediaLactococcus lactisMutagenesis InsertionalMembranechemistryBiochemistryGenes Bacterialbiology.proteinFormazanOxidation-ReductionIntracellularBacteria
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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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Targeted disruption of the peroxisomal thiolase B gene in mouse: a new model to study disorders related to peroxisomal lipid metabolism

2004

The peroxisomal beta-oxidation system consists of four steps catalysed by three enzymes: acyl-CoA oxidase, 3-hydroxyacyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (multifunctional enzyme) and thiolase. In humans, thiolase activity is encoded by one gene, whereas in rodents, three enzymes encoded by three distinct genes (i.e. thiolase A, thiolase B and SCP2/thiolase) catalyse the thiolase activity. So far, acyl-CoA oxidase- and multifunctional enzyme-deficient patients have been identified and knock-out mice for these genes have been produced. Conversely, no isolated thiolase-deficient patient has been found, and no thiolase (A or B)-deficient mice have been generated. Hence, to better u…

DehydrogenaseBiologymedicine.disease_causeBiochemistryGene Expression Regulation EnzymologicPeroxisomal DisordersMiceStructure-Activity RelationshipPeroxisomesmedicineAnimalsHumansRNA MessengerGeneHydro-LyasesSCP2chemistry.chemical_classificationMutationOxidase testThiolaseStem Cells3-Hydroxyacyl CoA DehydrogenasesGeneral MedicinePeroxisomeAcetyl-CoA C-AcyltransferaseEmbryo MammalianLipid MetabolismMolecular biologyMice Mutant StrainsMice Inbred C57BLDisease Models AnimalPhenotypeEnzymechemistryBiochemistryAcyl-CoA OxidaseBiochimie
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Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying

2014

The retention of the enzyme activity of alcohol dehydrogenase (ADH) has been studied in various drying processes such as spray drying. The aim of this study is to encapsulate ADH in mannitol, either with or without additive in order to limit the thermal denaturation of the enzyme during the drying process. The retention of ADH activity was investigated at different drying temperatures. When mannitol was used, the encapsulated ADH was found inactive in all the dried powders. This is presumably due to the quick crystallization of mannitol during spray drying that resulted in the impairment of enzyme protection ability in comparison to its amorphous form. Maltodextin (dextrose equivalent = 11)…

Dextrose equivalentlcsh:RS1-441Pharmaceutical ScienceArticlelaw.inventionlcsh:Pharmacy and materia medicachemistry.chemical_compoundlawmedicinespray dryingCrystallizationAlcohol dehydrogenasechemistry.chemical_classificationChromatographybiologyChemistryalcohol dehydrogenasemannitolMaltodextrinEnzyme assayEnzymeBiochemistrySpray dryingalcohol dehydrogenase; encapsulation; spray drying; mannitolbiology.proteinencapsulationMannitolhormones hormone substitutes and hormone antagonistsmedicine.drugPharmaceutics
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Fusarium proliferatum: induction and intracellular location of a lipoxygenase

1998

The fungus Fusarium proliferatum was grown in a soya oil- and glucose-supplemented medium. Induction of lipoxygenase activity (13-fold) in an extract of Fusarium biomass has been observed at day four on soya oil culture medium. A band at 232 kDa was detected using a specific lipoxygenase stain combined with native PAGE. The method of fungal homogenate obtained has been checked via subcellular marker enzymes activities: succinate dehydrogenase (SDH) for mitochondrial fraction and NADH-cytochrome C reductase (NADH-cyt. C) for the microsomal fraction. Protoplasts production and disintegration followed by subcellular fractionation using differential centrifugation was the best method to recover…

Differential centrifugationFusariumSuccinate dehydrogenasefood and beveragesFusarium proliferatumBioengineeringBiologyReductasebiology.organism_classificationApplied Microbiology and BiotechnologyBiochemistryLipoxygenaseBiochemistrybiology.proteinSpecific activityCell fractionationBiotechnologyEnzyme and Microbial Technology
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Artificial increase of uracilemia during fluoropyrimidine treatment can lead to DPD deficiency misinterpretation

2021

Each year in France, >75 000 patients receive fluoropyrimidines, including 5-fluorouracil (5-FU) and its oral prodrug capecitabine (Xeloda), to treat digestive, breast and head and neck cancers.1 Among them, ∼20% will experience severe hematological and digestive toxicities and <2% will have a fatal outcome in the first two cycles. A part of these toxicities may result from a deficiency in dihydropyrimidine dehydrogenase (DPD) which catabolizes the endogenous uracil (U) into dihydrouracil (UH2) as well as 5-FU. In 2018, French Health Authorities [Haute Autorité de Santé (HAS) and Institut National du Cancer, (INCa)] recommended the evaluation of the enzymatic activity of DPD by measuring th…

Dihydropyrimidine Dehydrogenase Deficiencybusiness.industryMEDLINEHematologyBioinformaticsmedicine.diseaseDihydropyrimidine dehydrogenase deficiencyText miningOncologyFluorouracilmedicineHumansFluorouracilbusinessLead (electronics)CapecitabineDihydrouracil Dehydrogenase (NADP)medicine.drugAnnals of Oncology
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Pharmacogenomics in colorectal carcinomas: Future perspectives in personalized therapy

2005

The recent introduction of new drugs such as capecitabine, irinotecan, and oxaliplatinum has greatly improved the clinical outcome of patients with advanced/metastatic colorectal cancer. Nevertheless, some patients may suffer from the adverse drug reactions which will probably be the main cause of chemotherapy failure. The goal of pharmacogenomics is to find correlations between therapeutic responses to drugs and the genetic profiles of patients; the different responses to a particular drug are due, in fact, not only to the specific clinico-pathological features of the patient or to environmental factors, but also to the ethnic origins and the particular individual's genetic profile. Genes …

DrugPhysiologyColorectal cancermedia_common.quotation_subjectmedicine.medical_treatmentClinical BiochemistryPharmacologyBioinformaticsThymidylate synthaseCapecitabinemedicineDihydropyrimidine dehydrogenaseAnimalsHumansColorectal Neoplasms/geneticmedia_commonChemotherapyPolymorphism Geneticbiologybusiness.industryColorectal Neoplasms/drug therapyCell Biologymedicine.diseasePersonal Health ServicesIrinotecanPharmacogeneticsPharmacogenomicsbiology.proteinColorectal Neoplasmsbusinessmedicine.drugJournal of Cellular Physiology
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Drug-metabolizing enzymes in the skin of man, rat, and pig.

2007

The mammalian skin has long been considered to be poor in drug metabolism. However, many reports clearly show that most drug metabolizing enzymes also occur in the mammalian skin albeit at relatively low specific activities. This review summarizes the current state of knowledge on drug metabolizing enzymes in the skin of human, rat, and pig, the latter, because it is often taken as a model for human skin on grounds of anatomical similarities. However only little is known about drug metabolizing enzymes in pig skin. Interestingly, some cytochromes P450 (CYP) have been observed in the rat skin which are not expressed in the rat liver, such as CYP 2B12 and CYP2D4. As far as investigated most d…

Drugcytochrome P450Swinemedia_common.quotation_subjectMetaboliteAldehyde dehydrogenaseHuman skinEpoxide hydrolaseEsterasechemistry.chemical_compoundOrgan Culture TechniquesCytochrome P-450 Enzyme SystemSpecies SpecificityGlycosyltransferaseAnimalsHumansPharmacology (medical)ratGeneral Pharmacology Toxicology and PharmaceuticsFlavin monooxygenaseCells Culturedmedia_commonSkinchemistry.chemical_classificationquinone reductase [NAD(P)H]biologyintegumentary systemAlcohol dehydrogenaseSulfotransferaseCytochrome P450Aldehyde dehydrogenaseMetabolic Detoxication Phase IIEnzymesRatsGlutathione S-transferaseIsoenzymesEnzymechemistryBiochemistryPharmaceutical PreparationsN-acetyltransferasebiology.proteinMetabolic Detoxication Phase IPig skin drug metabolismDrug metabolismUDP-glucuronosyltransferaseHuman
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The effect of water on protein dynamics

2004

Neutron diffraction and spectroscopy were applied to describe the hydration and dynamics of a soluble protein and a natural membrane from extreme halophilic Archaea. The quantitative dependence of protein motions on water activity was clearly illustrated, and it was established that a minimum hydration shell is required for the systems to access their functional resilience, i.e. a dynamics state that allows biological activity.

Dynamical transitionWater activityNeutron diffractionHalophilic malate dehydrogenaseBacteriorhodopsinHydration shellNeutronEuryarchaeotaGeneral Biochemistry Genetics and Molecular BiologyMalate DehydrogenaseSpectroscopySpectrum AnalysibiologyChemistrySpectrum AnalysisProtein dynamicsWaterBacteriorhodopsinPurple membraneAgricultural and Biological Sciences (miscellaneous)Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Neutron DiffractionMembraneSolvation shellAgricultural and Biological Sciences (all)BiochemistryChemical physicsBacteriorhodopsinsbiology.proteinBacteriorhodopsinsGeneral Agricultural and Biological SciencesResearch ArticlePhilosophical Transactions of the Royal Society of London. Series B: Biological Sciences
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