Search results for "REDUCTASE"

showing 10 items of 798 documents

Role of plant residues in determining temporal patterns of the activity, size and structure of nitrate reducer communities in soil

2010

ABSTRACT The incorporation of plant residues into soil not only represents an opportunity to limit soil organic matter depletion resulting from cultivation but also provides a valuable source of nutrients such as nitrogen. However, the consequences of plant residue addition on soil microbial communities involved in biochemical cycles other than the carbon cycle are poorly understood. In this study, we investigated the responses of one N-cycling microbial community, the nitrate reducers, to wheat, rape, and alfalfa residues for 11 months after incorporation into soil in a field experiment. A 20- to 27-fold increase in potential nitrate reduction activity was observed for residue-amended plot…

DNA BacterialCrop residueTime FactorsBiologyNitrate reductaseApplied Microbiology and BiotechnologyNitrate ReductasePolymerase Chain Reactionchemistry.chemical_compoundSoilNutrientPlant MicrobiologyNitrateNitrogen FixationNitrogen cycleSoil Microbiology[SDV.EE]Life Sciences [q-bio]/Ecology environmentEcologySoil organic matterfood and beveragesPlantsBiotaAgronomychemistryNitrogen fixationSoil microbiologyFood ScienceBiotechnology
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Psychrotolerant Sulfate-reducing Bacteria from an Oxic Freshwater Sediment Description of Desulfovibrio cuneatus sp. nov. and Desulfovibrio litoralis…

1998

The most abundant culturable sulfate-reducing bacteria were isolated from the littoral sediment of the oligotrophic Lake Stechlin. The strains STL1 and STL4 were obtained from the oxic uppermost layer, while strain STL6 was isolated from the anoxic zone in 20 to 30 mm depth. The isolates showed a striking morphological feature in tapering off at one end of the cell. Physiological characteristics related them to the genus Desulfovibrio. They contained desulfoviridin. H2, formate, pyruvate, lactate, and fumarate were utilized with sulfate, sulfite, thiosulfate, or elemental sulfur as electron acceptors. All isolates were able to reduce oxygen and survived 120 h of aeration. However, aerobic g…

DNA BacterialGeologic SedimentsMolecular Sequence DataHydrogensulfite reductasechemistry.chemical_elementFresh WaterBiologyDNA RibosomalPolymerase Chain ReactionApplied Microbiology and BiotechnologyMicrobiologyMicrobiologychemistry.chemical_compoundNephelometry and TurbidimetryGermanyMicroscopy Phase-ContrastOxidoreductases Acting on Sulfur Group DonorsHydrogensulfite ReductaseSulfate-reducing bacteriaPhylogenyEcology Evolution Behavior and SystematicsThiosulfateBase SequenceSulfatesRespirationSequence Analysis DNAbiology.organism_classification16S ribosomal RNASulfurAnoxic watersDesulfovibrioMicroscopy ElectronchemistryCytochromesDesulfovibrioWater MicrobiologyOxidation-ReductionBacteriaSystematic and Applied Microbiology
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Vibrio ponticus sp. nov., a neighbour of V fluvialis-V. furnissii clade, isolated from gilthead sea bream, mussels and seawater.

2004

A new Vibrio species, Vibrio ponticus, is proposed to accommodate four marine bacteria isolated from sea water, mussels and diseased sea bream (Sparus aurata), at the Mediterranean coast of Spain. Strains are Gram negative, slightly halophilic bacteria that require Na+ ion for growth, oxidase and catalase positive, negative for arginine dihydrolase and ornithine decarboxylase but positive for lysine decarboxylase and indole, and utilize beta-hydroxybutyrate as a sole carbon source. Phylogenetic analysis locate these marine bacteria in the vicinity of the V. fluvialis-V. furnissii clade, sharing with these two species 16S rDNA sequence similarities slightly above 97% (97.1 and 97.3%, respect…

DNA BacterialIndolesCarboxy-LyasesHydrolasesMolecular Sequence DataBiologyOrnithine DecarboxylaseApplied Microbiology and BiotechnologyMicrobiologyDNA RibosomalMicrobiologyMarine bacteriophageVibrionaceaeVibrio InfectionsRNA Ribosomal 16SSequence Homology Nucleic AcidMediterranean SeaAnimalsSeawaterRibosomal DNAEcology Evolution Behavior and SystematicsPhylogenyVibrioLysine decarboxylase3-Hydroxybutyric AcidFatty AcidsNucleic Acid HybridizationSequence Analysis DNA16S ribosomal RNAbiology.organism_classificationCatalaseVibrioSea BreamBivalviaSpainVibrio InfectionsPhenazinesGentian VioletOxidoreductasesBacteriaSystematic and applied microbiology
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Quantification of a novel group of nitrate-reducing bacteria in the environment by real-time PCR

2004

Abstract Nitrate reduction is performed by phylogenetically diverse bacteria. Analysis of narG (alpha subunit of the membrane bound nitrate reductase) trees constructed using environmental sequences revealed a new cluster that is not related to narG gene from known nitrate-reducing bacteria. In this study, primers targeting this as yet uncultivated nitrate-reducing group were designed and used to develop a real-time SYBR® Green PCR assay. The assay was tested with clones from distinct nitrate-reducing groups and applied to various environmental samples. narG copy number was high ranging between 5.08×108 and 1.12×1011 copies per gram of dry weight of environmental sample. Environmental real-…

DNA BacterialMicrobiology (medical)Geologic SedimentsMolecular Sequence DataGene DosageBiologyNitrate reductaseNitrate ReductasePolymerase Chain ReactionMicrobiologyDenitrifying bacteriaNitrate ReductasesRNA Ribosomal 16STaq Polymerase[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyMolecular BiologyGeneNitritesPhylogenySoil MicrobiologyGramGeneticsBacteriaBase SequencePhylogenetic treeSequence Analysis DNAbiology.organism_classification16S ribosomal RNA[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyReal-time polymerase chain reactionSequence AlignmentBacteriaJournal of Microbiological Methods
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Relative Abundances of Proteobacterial Membrane-Bound and Periplasmic Nitrate Reductases in Selected Environments

2007

ABSTRACT Dissimilatory nitrate reduction is catalyzed by a membrane-bound and a periplasmic nitrate reductase. We set up a real-time PCR assay to quantify these two enzymes, using the narG and napA genes, encoding the catalytic subunits of the two types of nitrate reductases, as molecular markers. The narG and napA gene copy numbers in DNA extracted from 18 different environments showed high variations, with most numbers ranging from 2 × 10 2 to 6.8 × 10 4 copies per ng of DNA. This study provides evidence that, in soil samples, the number of proteobacteria carrying the napA gene is often as high as that of proteobacteria carrying the narG gene. The high correlation observed between narG an…

DNA BacterialMolecular Sequence DataEnvironmentNitrate reductaseNitrate ReductasePlant RootsPolymerase Chain ReactionApplied Microbiology and BiotechnologyMicrobial Ecologychemistry.chemical_compoundBacterial ProteinsNitrateProteobacteriaGeneSoil Microbiology[SDV.EE]Life Sciences [q-bio]/Ecology environmentNAPAEcologybiologyMembrane ProteinsPeriplasmic spacebiology.organism_classificationBiochemistrychemistryPeriplasmic ProteinsProteobacteriaBacteriaDNAFood ScienceBiotechnologyApplied and Environmental Microbiology
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Functional and genomic diversity of methylotrophic Rhodocyclaceae: description of Methyloversatilis discipulorum sp. nov.

2015

Three strains of methylotrophic Rhodocyclaceae (FAM1T, RZ18-153 and RZ94) isolated from Lake Washington sediment samples were characterized. Based on phylogenetic analysis of 16S rRNA gene sequences the strains should be assigned to the genus Methyloversatilis. Similarly to other members of the family, the strains show broad metabolic capabilities and are able to utilize a number of organic acids, alcohols and aromatic compounds in addition to methanol and methylamine. The main fatty acids were 16:1ω7c (49–59 %) and 16:0 (32–29 %). Genomes of all isolates were sequenced, assembled and annotated in collaboration with the DOE Joint Genome Institute (JGI). Genome comparison revealed that the s…

DNA BacterialWashingtonGeologic SedimentsRhodocyclaceaeSequence analysisMolecular Sequence Datalake sedimentsRhodocyclaceaeMicrobiologyPhylogeneticsRNA Ribosomal 16SMalate synthasePhylogenyEcology Evolution Behavior and SystematicsGeneticsbiologyMethanol dehydrogenaseta1184phylogenetic analysista1183Fatty AcidsGenomicsSequence Analysis DNAGeneral MedicineIsocitrate lyaseRibosomal RNA16S ribosomal RNAbiology.organism_classificationBacterial Typing TechniquesAlcohol OxidoreductasesLakesBiochemistrybiology.proteinmetabolismGenome BacterialInternational Journal of Systematic and Evolutionary Microbiology
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Cloning and sequencing of the cDNA encoding human glutaredoxin.

1994

Glutaredoxin (thioltransferase) is a small, heat-stable protein, which is involved in thiol/disulfide exchange reactions. We have isolated a cDNA that encodes glutaredoxin from a human brain cDNA library. The encoded protein contains 106 amino acids with a calculated molecular mass of 11.76 kDa and an isoelectric point of 8.09. The amino acid sequence deduced from the cDNA is more than 80% identical to those of other mammalian glutaredoxins.

DNA ComplementaryMolecular Sequence DataBiophysicsSequence alignmentMolecular cloningBiologyBiochemistryStructural BiologyGlutaredoxinComplementary DNAGeneticsHumansAmino Acid SequenceCloning MolecularPeptide sequenceGlutaredoxinschemistry.chemical_classificationBase SequencecDNA libraryNucleic acid sequenceBrainProteinsMolecular biologyAmino acidchemistryBiochemistryOxidoreductasesBiochimica et biophysica acta
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Tonoplast subcellular localization of maize cytochrome b5 reductases

2000

Plant cytochrome b 5 reductases (b 5 R) are assumed to be part of an ER-associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 (cyt b 5 ) to ER-associated fatty acyl desaturase and related hydroxylases, as in mammalian cells. Here we report on cDNA cloning of a novel maize b 5 R, NFR II, strongly related to a previously cloned cDNA, NFR I (Bagnaresi et al., 1999, Biochem, J. 338, 499-5051. Maize b 5 R isoforms are produced by a small multi-gene family. The NFR cDNAs were shown to encode active b 5 Rs by heterologous expression in yeast. Both reductases, in addition to Fe 3+ -chelates, efficiently reduced Cu 2+ -chelates. Using a polyclonal antibody able to recogniz…

DNA ComplementaryMolecular Sequence DataSaccharomyces cerevisiaePlant ScienceMolecular cloningBiologyPlant RootsZea maysIsozymeGene Expression Regulation EnzymologicComplementary DNACytochrome b5GeneticsAmino Acid SequenceMicroscopy ImmunoelectronCytochrome ReductasesCytochrome b5 reductaseSequence Homology Amino AcidCytochrome bSequence Analysis DNACell BiologySubcellular localizationMolecular biologyIsoenzymesBiochemistryVacuolesHeterologous expressionSequence AlignmentCytochrome-B(5) ReductaseThe Plant Journal
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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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Plant progesterone 5β-reductase is not homologous to the animal enzyme. Molecular evolutionary characterization of P5βR from Digitalis purpurea

2007

Plants of the genus Digitalis produce cardiac glycosides, i.e. digoxin, which are widely used for congestive heart failure. Progesterone 5beta-reductase (P5betaR) is a key enzyme in the biosynthesis of these natural products. Here, we have carried out the purification and partial amino acid sequencing of the native P5betaR from foxglove (Digitalis purpurea), and isolated a cDNA encoding this enzyme. Similarly to other steroid 5beta-reductases, the recombinant P5betaR catalyzes the stereospecific reduction of the Delta(4)-double bond of several steroids with a 3-oxo,Delta(4,5) structure. The gene encoding P5betaR is expressed in all plant organs, and maximally transcribed in leaves and matur…

DNA ComplementarySubfamilyRecombinant Fusion ProteinsMolecular Sequence DataPlant ScienceHorticultureReductaseBiochemistryGas Chromatography-Mass SpectrometryEvolution Molecularchemistry.chemical_compoundPhylogeneticsComplementary DNACardenolideAnimalsAmino Acid SequenceMolecular BiologyGenePhylogenyProgesteronePlant Proteinschemistry.chemical_classificationGeneticsDigitalisBase SequenceMolecular StructureSequence Homology Amino AcidbiologyProgesterone ReductaseReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingDigitalis purpureaGeneral Medicinebiology.organism_classificationEnzymeModels ChemicalBiochemistrychemistryElectrophoresis Polyacrylamide GelPhytochemistry
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