Search results for "ENZYME"

showing 10 items of 3924 documents

The Tonoplast H+ -ATPase of Acer pseudoplatanus is a vacuolar-type ATPase that operates with a phosphoenzyme intermediate

1995

The tonoplast H+-ATPase of Acer pseudoplatanus has been purified from isolated vacuoles. After solubilization, the purification procedure included size-exclusion and ion-exchange chromatography. The H+-ATPase consists of at least eight subunits, of 95, 66, 56, 54, 40, 38, 31, and 16 kD, that did not cross-react with polyclonal antibodies raised to the plasmalemma ATPase of Arabidopsis thaliana. The 66-kD polypeptide cross-reacted with monoclonal antibodies raised to the 70-kD subunit of the vacuolar H+-ATPase of oat roots. The functional molecular size of the tonoplast H+-ATPase, analyzed in situ by radiation inactivation, was found to be around 400 kD. The 66-kD subunit of the tonoplast H+…

0106 biological sciencesPhysiologyATPaseProtein subunitPlant ScienceVacuole01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health scienceschemistry.chemical_compoundHydroxylamineProton transport[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsGenetics030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyAcer pseudoplatanusbiology.organism_classificationEnzymechemistryBiochemistryPolyclonal antibodiesbiology.protein010606 plant biology & botanyResearch Article
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NADPH Oxidase-Mediated Reactive Oxygen Species Production: Subcellular Localization and Reassessment of Its Role in Plant Defense

2009

International audience; Chemiluminescence detection of reactive oxygen species (ROS) triggered in tobacco BY-2 cells by the fungal elicitor cryptogein was previously demonstrated to be abolished in cells transformed with an antisense construct of the plasma membrane NADPH oxidase, NtrbohD. Here, using electron microscopy, it has been confirmed that the first hydrogen peroxide production occurring a few minutes after challenge of tobacco cells with cryptogein is plasma membrane located and NtrbohD mediated. Furthermore, the presence of NtrbohD in detergent-resistant membrane fractions could be associated with the presence of NtrbohD-mediated hydrogen peroxide patches along the plasma membran…

0106 biological sciencesPhysiologyBiology01 natural sciencesDNA AntisenseFungal Proteins03 medical and health sciencesMicroscopy Electron TransmissionNtrbohDTobaccoGene expressionNADPHPlant defense against herbivory[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCells CulturedPlant Proteins030304 developmental biologychemistry.chemical_classification0303 health sciencesReactive oxygen speciesOxidase testNADPH oxidaseHydrogen PeroxideGeneral MedicinePlants Genetically ModifiedSubcellular localizationElicitorPlant LeavesEnzymechemistryBiochemistrybiology.proteinREACTIVE OXYGEN SPECIES (ROS)OxidoreductasesReactive Oxygen SpeciesAgronomy and Crop Science010606 plant biology & botanyMolecular Plant-Microbe Interactions®
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Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass

2005

Abstract In grasses, residues homologous to residues Ile-1,781 and Ile-2,041 in the carboxyl-transferase (CT) domain of the chloroplastic acetyl-coenzyme A (CoA) carboxylase (ACCase) from the grass weed black-grass (Alopecurus myosuroides [Huds.]) are critical determinants for sensitivity to two classes of ACCase inhibitors, aryloxyphenoxypropionates (APPs) and cyclohexanediones. Using natural mutants of black-grass, we demonstrated through a molecular, biological, and biochemical approach that residues Trp-2,027, Asp-2,078, and Gly-2,096 are also involved in sensitivity to ACCase inhibitors. In addition, residues Trp-2,027 and Asp-2,078 are very likely involved in CT activity. Using three-…

0106 biological sciencesPhysiologyCoenzyme AMutantPlant Sciencemedicine.disease_cause01 natural scienceschemistry.chemical_compound[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyGeneticsmedicineVULPIN[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyBinding siteComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationMutationbiologyAlopecurus myosuroidesfood and beveragesActive site04 agricultural and veterinary sciencesbiology.organism_classificationPyruvate carboxylaseEnzymechemistryBiochemistry040103 agronomy & agriculturebiology.protein0401 agriculture forestry and fisheries010606 plant biology & botanyPlant Physiology
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An isoleucine residue within the carboxyl-transferase domain of multidomain acetyl-coenzyme A carboxylase is a major determinant of sensitivity to ar…

2003

Abstract A 3,300-bp DNA fragment encoding the carboxyl-transferase domain of the multidomain, chloroplastic acetyl-coenzyme A carboxylase (ACCase) was sequenced in aryloxyphenoxypropionate (APP)-resistant and -sensitive Alopecurus myosuroides (Huds.). No resistant plant contained an Ile-1,781-Leu substitution, previously shown to confer resistance to APPs and cyclohexanediones (CHDs). Instead, an Ile-2,041-Asn substitution was found in resistant plants. Phylogenetic analysis of the sequences revealed that Asn-2,041 ACCase alleles derived from several distinct origins. Allele-specific polymerase chain reaction associated the presence of Asn-2,041 with seedling resistance to APPs but not to C…

0106 biological sciencesPhysiologyMolecular Sequence DataSequence alignmentPlant ScienceBiology01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants geneticschemistry.chemical_compoundMagnoliopsida[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsmental disordersGeneticsTransferaseVULPINAmino Acid SequenceIsoleucinePeptide sequencePhylogenyComputingMilieux_MISCELLANEOUS2. Zero hungerchemistry.chemical_classificationPolymorphism GeneticCyclohexanonesHerbicidesAcetyl-CoA carboxylase04 agricultural and veterinary sciencesACETYL-COA CARBOXYLASEPyruvate carboxylaseProtein Structure TertiaryEnzymeBiochemistrychemistryMutation040103 agronomy & agriculture0401 agriculture forestry and fisheriesIsoleucinePropionatesSequence AlignmentDNA010606 plant biology & botanyResearch Article
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Phosphoproteins Involved in the Signal Transduction of Cryptogein, an Elicitor of Defense Reactions in Tobacco

2000

We previously reported that the signal transduction of cryptogein, an elicitor of defense reactions in Nicotiana tabacum cells, involves upstream protein phosphorylation. In the present study, induction of these early physiological events was further investigated with inhibitors of protein phosphatase (PP), okadaïc acid, and calyculin A. Calyculin A mimicked the effects of cryptogein, inducing an influx of calcium, an extracellular alkalinization, and the production of active oxygen species (AOS), suggesting that during cryptogein signal transduction the balance between specific protein kinase (PK) and PP activities was modified. To identify the phosphorylated proteins that could be involv…

0106 biological sciencesPhysiologyPhosphataseBiology01 natural sciencesFungal Proteins03 medical and health scienceschemistry.chemical_compound[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]TobaccoPhosphoprotein Phosphatasesmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyStaurosporineProtein phosphorylationEnzyme InhibitorsPhosphorylationProtein Kinase InhibitorsComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesFungal proteinIon TransportAlgal ProteinsGeneral MedicinePhosphoproteinsElicitorPlants ToxicchemistryBiochemistryPhosphorylationCalciumSignal transductionAgronomy and Crop ScienceSignal Transduction010606 plant biology & botanyCalyculinmedicine.drugMolecular Plant-Microbe Interactions®
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Underwater high frequency noise: Biological responses in sea urchin Arbacia lixula (Linnaeus, 1758)

2020

Marine life is extremely sensitive to the effects of environmental noise due to its reliance on underwater sounds for basic life functions, such as searching for food and mating. However, the effects on invertebrate species are not yet fully understood. The aim of this study was to determine the biochemical responses of Arbacia lixula exposed to high-frequency noise. Protein concentration, enzyme activity (esterase, phosphatase and peroxidase) and cytotoxicity in coelomic fluid were compared in individuals exposed for three hours to consecutive linear sweeps of 100 to 200 kHz lasting 1 s, and control specimens. Sound pressure levels ranged between 145 and 160 dB re 1μPa. Coelomic fluid was …

0106 biological sciencesPhysiologyPhosphataseZoology01 natural sciencesBiochemistryEsteraseHemolysis03 medical and health sciencesbiology.animalAnimalsHomeostasisHSP70 Heat-Shock ProteinsMatingSettore BIO/06 - Anatomia Comparata E CitologiaMolecular BiologySea urchinArbacia lixulaHSP70030304 developmental biologyInvertebrateCell ProliferationPeroxidaseArbacia0303 health sciencesbiologyEchinoderm010604 marine biology & hydrobiologyEsterasesMarine invertebrateMarine invertebratesbiology.organism_classificationAlkaline PhosphataseAcoustic stimuluEnzyme assayCoelomomycesBody Fluidsbiology.proteinMetabolomePhysiological stress.Noise
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Purification and characterization of geranyl diphosphate synthase from Vitis vinifera L. cv Muscat de Frontignant cell cultures

1993

A geranyl diphosphate synthase (EC 2.5.1.1), which catalyzes the formation of geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate, was isolated from Vitis vinifera L. cv Muscat de Frontignan cell cultures. Purification of the enzyme was achieved successively by ammonium sulfate precipitation and chromatography on DEAE-Sephacel, hydroxylapatite, Mono Q, Phenyl Superose, Superose 12, and preparative nondenaturing polyacrylamide gels. The enzyme formed only geranyl diphosphate as a product. In all cases, neither neryl diphosphate, the cis isomer, nor farnesyl diphosphate was detected. The enzyme showed a native molecular mass of 68 [plus or minus] 5 kD as determined …

0106 biological sciencesPhysiologyStereochemistry[SDV]Life Sciences [q-bio]PolyacrylamidePlant Science01 natural sciencesCofactor[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health scienceschemistry.chemical_compound[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsGeneticsSodium dodecyl sulfateAmmonium sulfate precipitationComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyMolecular mass[SDV] Life Sciences [q-bio]EnzymechemistryCell cultureCULTURE DE CELLULEbiology.proteinCis–trans isomerism010606 plant biology & botanyResearch Article
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Elicitor and resistance-inducing activities of -1,4 cellodextrins in grapevine, comparison with -1,3 glucans and -1,4 oligogalacturonides

2007

Cellodextrins (CD), water-soluble derivatives of cellulose composed of beta-1,4 glucoside residues, have been shown to induce a variety of defence responses in grapevine (Vitis vinifera L.) cells. The larger oligomers of CD rapidly induced transient generation of H2O2 and elevation in free cytosolic calcium, followed by a differential expression of genes encoding key enzymes of the phenylpropanoid pathway and pathogenesis-related (PR) proteins as well as stimulation of chitinase and beta-1,3 glucanase activities. Most of these defence reactions were also induced by linear beta-1,3 glucans (betaGlu) and alpha-1,4 oligogalacturonides (OGA) of different degree of polymerization (DP), but the i…

0106 biological sciencesPhysiology[SDV]Life Sciences [q-bio]Plant ScienceBiology01 natural sciences03 medical and health sciencesGene expressionBotanyGRAPEVINE[SDV.BV]Life Sciences [q-bio]/Vegetal Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesPhenylpropanoidINDUCED RESISTANCEOligosaccharideGlucanaseElicitor[SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyCytosolEnzymechemistryBiochemistryChitinasebiology.proteinCELLODEXTRINSDEFENCE RESPONSES010606 plant biology & botany
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Universal primers for PCR-sequencing of grass chloroplastic acetyl-CoA carboxylase domains involved in resistance to herbicides

2005

Summary Primers were designed to amplify two regions involved in sensitivity to herbicides inhibiting the plastidic acetyl-CoA carboxylase (ACCase) from grasses (Poaceae). The first primer pair amplified a 551-bp amplicon containing a variable Ile/Leu codon at position 1781 in Alopecurus myosuroides sequence. The second primer pair amplified a 406-bp amplicon containing four variable codons (Trp/Cys, Ile/Asn, Asp/Gly, Gly/Ala) at positions 2027, 2041, 2078 and 2096, respectively, in A. myosuroides sequence. Both primer pairs amplified the targeted fragments from genes encoding plastidic ACCases, but not from the very similar genes encoding cytosolic ACCases. Clear DNA sequences were obtaine…

0106 biological sciencesPlant Science01 natural sciencesDNA sequencinglaw.inventionlaw[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyPoa annua[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyACETYL COENZYME-A CARBOXYLASEGeneEcology Evolution Behavior and SystematicsPolymerase chain reactionComputingMilieux_MISCELLANEOUSGeneticsbiologyAlopecurus myosuroidesAcetyl-CoA carboxylasefood and beverages04 agricultural and veterinary sciencesAmpliconbiology.organism_classificationBiochemistry040103 agronomy & agriculture0401 agriculture forestry and fisheriesPrimer (molecular biology)Agronomy and Crop Science010606 plant biology & botany
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Current view of nitric oxide-responsive genes in plants

2009

International audience; Significant efforts have been directed towards the identification of genes differentially regulated through nitric oxide (NO)-dependent processes. These efforts comprise the use of medium- and large-scale transcriptomic analyses including microarray and cDNA-amplification fragment length polymorphism (AFLP) approaches. Numerous putative NO-responsive genes have been identified in plant tissues and cell suspensions with transcript levels altered by artificially released NO, or endogenously produced. Comparative analysis of the data from such transcriptomic analyses in Arabidopsis reveals that a significant part of these genes encode proteins related to plant adaptive …

0106 biological sciencesPlant ScienceBiology01 natural sciencesNitric oxide synthase-like enzymeTranscriptomic analysisTranscriptome03 medical and health sciencesL-NAME[ SDV.SA.AGRO ] Life Sciences [q-bio]/Agricultural sciences/AgronomyTranscription (biology)Complementary DNAArabidopsisGenetics[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyGeneTranscription factor030304 developmental biologyGenetics0303 health sciencesBiotic and abiotic stressesNitric oxide-responsive genesPromoterNitric oxideGeneral Medicinebiology.organism_classificationStress biotiqueDNA microarrayAgronomy and Crop Science010606 plant biology & botany
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