Search results for "2-dioxygenase"

showing 4 items of 4 documents

Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the correspondi…

1997

p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 4…

0106 biological sciencesDNA ComplementaryMolecular Sequence DataBiology4-Hydroxyphenylpyruvate Dioxygenase01 natural sciencesBiochemistry03 medical and health sciencesDioxygenaseComplementary DNA[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceCells CulturedComputingMilieux_MISCELLANEOUS030304 developmental biologyHomogentisate 12-dioxygenase0303 health sciencesBase SequenceSequence Homology Amino AcidMolecular massDioxygenase activityNucleic acid sequenceCell BiologyMolecular biologyDaucus carotaBiochemistryElectrophoresis Polyacrylamide Gel4-Hydroxyphenylpyruvate dioxygenaseResearch ArticleChromatography LiquidSubcellular Fractions010606 plant biology & botany
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Isoproturon

2010

Frequent use of phenylurea herbicide isoproturon (IPU) in agricultural fields has resulted not only in the contamination of the natural resources including soil and water but also in the adaptation of the soil microflora to its rapid degradation. However, up to now, the mechanisms underlying this microbial adaptation are not well elucidated. The aim of this study was to explore the processes and factors implicated in IPU degradation from the agricultural field to the genes coding for catabolic genes. The study carried out at the experimental field of Epoisses cropped with a winter wheat / barley / rape seed crop rotation indicated that as a result of its periodically repeated use, the soil …

[SDE] Environmental Sciences[SDV.SA] Life Sciences [q-bio]/Agricultural sciencesHerbicidesVARIABILITE SPATIALE1Clonage BACSpatial variability[SDV] Life Sciences [q-bio]BAC cloningVOIE METABOLIQUESoil microbiologyMicrobiologie du sol12-DIOXYGENASEMetabolic pathwayBiodegradationVoie métaboliqueHerbicideIsoproturon2-dioxygenaseVariabilité spatiale
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Availability of O 2 as a Substrate in the Cytoplasm of Bacteria under Aerobic and Microaerobic Conditions

1998

ABSTRACT The growth rates of Pseudomonas putida KT2442 and mt-2 on benzoate, 4-hydroxybenzoate, or 4-methylbenzoate showed an exponential decrease with decreasing oxygen tensions (partial O 2 tension [pO 2 ] values). The oxygen tensions resulting in half-maximal growth rates were in the range of 7 to 8 mbar of O 2 (corresponding to 7 to 8 μM O 2 ) (1 bar = 10 5 Pa) for aromatic compounds, compared to 1 to 2 mbar for nonaromatic compounds like glucose or succinate. The decrease in the growth rates coincided with excretion of catechol or protocatechuate, suggesting that the activity of the corresponding oxygenases became limiting. The experiments directly establish that under aerobic and micr…

CytoplasmOxygenasePhysiology and MetabolismDiffusionCatecholsParabenschemistry.chemical_elementBenzoatesMicrobiologyOxygenDioxygenaseschemistry.chemical_compoundOxygen ConsumptionCatechol 12-dioxygenaseMolecular BiologyBenzoic acidbiologyPseudomonas putidaSubstrate (chemistry)SuccinatesBenzoic Acidbiology.organism_classificationAerobiosisCatechol 12-DioxygenasePseudomonas putidaGlucoseBiochemistrychemistryCytoplasmOxygenasesBiophysicsJournal of Bacteriology
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Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site

2003

Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …

Models MolecularAFSG Stafafdelingen (WUATV)10050 Institute of Pharmacology and Toxicologydrug protein bindingEnantioselectivityEpoxide hydrolaseCrystallography X-Rayuncultured actinomyceteCatalytic Domain2400 General Immunology and Microbiologyalpha helixRhodococcuscholesterol epoxide hydrolasenaphthalene 12-dioxygenasedcl14limonene 12 epoxide hydrolaseEpoxide hydrolaseBacteria (microorganisms)delta(5)-3-ketosteroid isomeraseEpoxide HydrolasesLimonene-12-epoxide hydrolaseGeneral Neurosciencearticle2800 General NeuroscienceActinobacteria (class)Articlesagrobacterium-radiobacterEnzyme structureRecombinant Proteinsunclassified drugenzyme structurereaction analysisBiochemistrypriority journalenzyme active siteMechanism2-dioxygenaseDimerizationBiotechnologychemical reactioncrystal structureaspergillus-nigermacromolecular structuresStereochemistrybeta sheetvalpromideMolecular Sequence Data610 Medicine & healthGenetics and Molecular BiologyBiologyGeneral Biochemistry Genetics and Molecular BiologyBacterial Proteinssite directed mutagenesis1300 General Biochemistry Genetics and Molecular BiologyHydrolase1312 Molecular BiologyAmino Acid SequencedetoxificationRhodococcus erythropolisBiologyMonoterpene degradationMolecular Biologyprotein data-bankenzyme substrate complexEnzyme substrate complexnonhumancatalysisSequence Homology Amino AcidGeneral Immunology and Microbiologybacterial enzymeActive sitecrystal-structureAFSG Staff Departments (WUATV)enzyme metabolismProtein SubunitsenzymeEpoxide HydrolasesGeneral Biochemistrybiology.proteinMutagenesis Site-Directed570 Life sciences; biologyselenomethioninenaphthalene 1Alpha helix
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