Search results for "Pyruvate carboxylase"

showing 10 items of 27 documents

C3cotyledons are followed by C4leaves: intra-individual transcriptome analysis ofSalsola soda(Chenopodiaceae)

2016

The genome of Salsola soda allows a transition from C3 to C4 photosynthesis. A developmental transcriptome series revealed novel genes showing expression patterns similar to those encoding C4 proteins.

0106 biological sciences0301 basic medicineSalsolaC4 photosynthesisfood.ingredientSalsolaPhysiologyPlant ScienceChenopodiaceaecotyledonBiology01 natural sciences03 medical and health sciencesfoodRNA seqBotanyPhotosynthesisChenopodiaceaedevelopmentSalsola sodaCarbon IsotopesleafCaryophyllalesGene Expression Profilingfood and beveragesbiology.organism_classificationCaryophyllalesPlant Leaves030104 developmental biologyMRNA SequencingSeedlingTranscriptomePhosphoenolpyruvate carboxylaseCotyledonResearch Paper010606 plant biology & botanyJournal of Experimental Botany
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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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An isoleucine-leucine substitution in chloroplastic acetyl-CoA carboxylase from green foxtail (Setaria viridis L. Beauv.) is responsible for resistan…

2002

The cDNAs encoding chloroplastic acetyl-CoA carboxylase (ACCase, EC 6.4.1.2) from three lines of Setaria viridis (L. Beauv.) resistant or sensitive to sethoxydim, and from one sethoxydim-sensitive line of Setaria italica (L. Beauv.) were cloned and sequenced. Sequence comparison revealed that a single isoleucine-leucine substitution discriminated ACCases from sensitive and resistant lines. Using near-isogenic lines of S. italica derived from interspecific hybridisation, we demonstrated that the transfer of the S. viridis mutant ACCase allele into a sethoxydim-sensitive S. italica line conferred resistance to this herbicide. We confirmed this result using allele-specific polymerase chain rea…

0106 biological sciencesSetariaChloroplastsMutantMolecular Sequence DataDrug ResistancePlant ScienceMolecular cloningPoaceae01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants geneticsLeucine[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsGeneticsPoint MutationAmino Acid SequenceIsoleucineComputingMilieux_MISCELLANEOUSAllelesPhylogenyGenes DominantbiologySequence Homology Amino AcidSetaria viridisCyclohexanonesHerbicidesAcetyl-CoA carboxylase04 agricultural and veterinary sciencesbiology.organism_classification3. Good healthPyruvate carboxylaseBiochemistryAmino Acid Substitution040103 agronomy & agriculture0401 agriculture forestry and fisheriesLeucineIsoleucineSequence Alignment010606 plant biology & botanyAcetyl-CoA CarboxylasePlanta
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Carbon isotope composition of plant photosynthetic tissues reflects a Crassulacean Acid Metabolism (CAM) continuum in the majority of CAM lineages

2021

Abstract The stable carbon isotope composition of plant tissues, commonly expressed as δ13C, holds a wealth of information about photosynthetic pathway, water relations and stress physiology. Crassulacean acid metabolism (CAM) is a derived form of photosynthesis that allows plants to fix carbon at a higher water-use efficiency compared to the ancestral C3 photosynthesis. While the central carbon-fixing enzyme of C3 plants, Rubisco, strongly discriminates against the heavy 13C isotope, CAM is characterized by a dual use of Rubisco and the much less discriminating PEP carboxylase as carbon-fixing enzymes, causing the δ13C values of CAM plant tissues to be generally less negative than those fo…

0106 biological sciencesVascular plantMesembryanthemumbiologyRuBisCOPlant Sciencebiology.organism_classificationPhotosynthesisCrassulaceae010603 evolutionary biology01 natural sciencesCrassulaceaeAeonieaeCrassulacean Acid MetabolismAizoaceaeBotanybiology.proteinδ13CAizoaceaeCrassulacean acid metabolismMesembryanthemumPhosphoenolpyruvate carboxylaseEcology Evolution Behavior and Systematics010606 plant biology & botany
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2012

Abstract. Global change forces ecosystems to adapt to elevated atmospheric concentrations of carbon dioxide (CO2). We understand that carbonyl sulfide (COS), a trace gas which is involved in building up the stratospheric sulfate aerosol layer, is taken up by vegetation with the same triad of the enzymes which are metabolizing CO2, i.e. ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), phosphoenolpyruvate carboxylase (PEP-Co) and carbonic anhydrase (CA). Therefore, we discuss a physiological/biochemical acclimation of these enzymes affecting the sink strength of vegetation for COS. We investigated the acclimation of two European tree species, Fagus sylvatica and Quercus ilex, grown …

Carbon dioxide in Earth's atmospherebiologyRuBisCOchemistry.chemical_elementAcclimatizationSulfurTrace gaschemistry.chemical_compoundchemistryEnvironmental chemistryCarbon dioxidebiology.proteinPhosphoenolpyruvate carboxylaseEcology Evolution Behavior and SystematicsEarth-Surface ProcessesCarbonyl sulfideBiogeosciences
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Molecular characterization of a phosphoenolpyruvate carboxylase in the gymnosperm Picea abies (Norway spruce)

1996

Phosphoenolpyruvate carboxylase (PEPC) genes and cDNA sequences have so far been isolated from a broad range of angiosperm but not from gymnosperm species. We constructed a cDNA library from seedlings of Norway spruce (Picea abies) and identified cDNAs coding for PEPC. A full-length PEPC cDNA was sequenced. It consists of 3522 nucleotides and has an open reading frame (ORF) that encodes a polypeptide (963 amino acids) with a molecular mass of 109551. The deduced amino acid sequence revealed a higher similarity to the C3-form PEPC of angiosperm species (86-88%) than to the CAM and C4 forms (76-84%). The putative motif (Lys/Arg-X-X-Ser) for serine kinase, which is conserved in all angiosperm …

DNA ComplementaryDNA PlantProtein ConformationMolecular Sequence DataPlant ScienceBiologyTreesEvolution MolecularGymnospermComplementary DNABotanyGeneticsAmino Acid SequenceRNA MessengerCloning MolecularPeptide sequencePhylogenySouthern blotBase SequenceSequence Homology Amino AcidcDNA libraryHybridization probefungifood and beveragesPicea abiesGeneral MedicineBlotting Northernbiology.organism_classificationPhosphoenolpyruvate CarboxylaseBlotting SouthernBiochemistryPhosphoenolpyruvate carboxylaseAgronomy and Crop SciencePlant Molecular Biology
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Phosphoenolpyruvate Carboxylase Activity and Malate Content of Spruce Needles of Healthy and Damaged Trees at Three Mountain Sites

1991

Summary Investigations were carried out on the phosphoenolpyruvate carboxylase (PEPC) activity and the malate content in spruce trees [Picea abies (L.) Karst] at three natural sites. In needles of damaged spruce the PEPC activity is significantly higher than in needles of undamaged spruce. Therefore, the PEPC activity seems to be a biochemical damage indicator in spruce needles. The increase in PEPC activity in damaged trees is discussed as a repair mechanism to compensate the increased need of carbon skeletons by providing oxaloacetate. The malate content is enhanced in needles of severely damaged trees. An increase in malate seems to indicate senescence reactions and may be related to the…

EcophysiologybiologyfungiPhosphoenolpyruvate carboxylase activityPicea abiesGeneral MedicineGeneral Chemistrybiology.organism_classificationchemistry.chemical_compoundchemistryBotanybiology.proteinCitrate synthaseMalic acidPhosphoenolpyruvate carboxylaseBiochemie und Physiologie der Pflanzen
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Investigation on phospheonol pyruvate carboxylase and proline in damaged and indamaged needles of Picea Abies and Abies Alba

1998

The client of forest damage is rapidly characterized by visible criteria such as loss and yellowing of leaves and needles Additionally damage to Norway spruce (Picea abies) and silver fit (Abies alba) can be diagnosed by biochemical criteria. The results in the present study performed in 1993 and 1994 on six Norway Spruces of each of the eleven open air stands in south-western Germany indicate that the activity of phosphoenol pyruvate carboxylase (PEPC) correlates with the extent of damage and of the loss of needles, respectively. Needles of severely damaged trees had higher levels of PEPC than needles of healthy trees. There was also a positive correlation between the activity of PEPC and …

Environmental EngineeringCarboxy-lyasesbiologyHealth Toxicology and MutagenesisfungiPublic Health Environmental and Occupational HealthPicea abiesGeneral MedicineGeneral Chemistrybiology.organism_classificationPositive correlationPollutionPyruvate carboxylaseAbies albaBotanyEnvironmental ChemistryProlinePhosphoenolpyruvate carboxylaseOpen airChemosphere
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Extracellular oxidoreduction potential modifies carbon and electron flow in Escherichia coli.

2000

ABSTRACT Wild-type Escherichia coli K-12 ferments glucose to a mixture of ethanol and acetic, lactic, formic, and succinic acids. In anoxic chemostat culture at four dilution rates and two different oxidoreduction potentials (ORP), this strain generated a spectrum of products which depended on ORP. Whatever the dilution rate tested, in low reducing conditions (−100 mV), the production of formate, acetate, ethanol, and lactate was in molar proportions of approximately 2.5:1:1:0.3, and in high reducing conditions (−320 mV), the production was in molar proportions of 2:0.6:1:2. The modification of metabolic fluxes was due to an ORP effect on the synthesis or stability of some fermentation enzy…

MESH : Models Chemical0106 biological sciencesMESH: Oxidation-ReductionMESH : Acetic AcidMESH : Escherichia coliMESH : NADFormatesOxaloacetatesMESH: Phosphoenolpyruvate CarboxylaseSuccinic AcidMESH: Alcohol DehydrogenaseMESH : CarbonMESH : EthanolMESH: Carbon Dioxide01 natural sciencesPhosphoenolpyruvatechemistry.chemical_compoundModels[INFO.INFO-BT]Computer Science [cs]/BiotechnologyAcetic Acid0303 health sciencesbiologyMESH: Escherichia coliMESH: Models ChemicalMESH : Acetyl Coenzyme AMESH: NADLactic acidMESH : Carbon DioxideBiochemistryFormic AcidsMESH: PhosphoenolpyruvateMESH: Acetic AcidMESH: Pyruvate KinaseMESH : Phosphoenolpyruvate CarboxylaseMESH: Oxaloacetic AcidsOxidation-Reduction[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyMESH: EthanolPhysiology and MetabolismPyruvate KinaseElectronsChemicalMESH: CarbonMESH : Formic AcidsChemostatMicrobiologyMESH: Fermentation03 medical and health sciencesAcetic acidMESH : Alcohol DehydrogenaseAcetyl Coenzyme AMESH : Fermentation010608 biotechnology[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyEscherichia coliFormate[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyLactic Acid[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular Biology030304 developmental biologyAlcohol dehydrogenaseMESH : Oxidation-ReductionMESH: ElectronsEthanolEthanolMESH : Succinic AcidAlcohol DehydrogenaseCarbon DioxideNADMESH: Formic AcidsMESH : Pyruvate KinaseCarbonOxaloacetic AcidsPhosphoenolpyruvate CarboxylaseMESH: Succinic Acid[INFO.INFO-BT] Computer Science [cs]/BiotechnologychemistryModels ChemicalSuccinic acidMESH : Lactic AcidMESH : Oxaloacetic AcidsFermentationbiology.proteinFermentationMESH: Lactic AcidMESH : ElectronsMESH : PhosphoenolpyruvateMESH: Acetyl Coenzyme A
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