Search results for "Histidine"

showing 10 items of 152 documents

Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2).

1990

Abstract Biochemical and genetic data indicate that in Streptomyces coelicolor A3(2) the majority of the genes involved in the biosynthesis of histidine are clustered in a small region of the chromosome [Carere et al., Mol. Gen. Genet. 123 (1973) 219–224; Russi et al., Mol. Gen. Genet. 123 (1973) 225–232]. To investigate the structural organization and the regulation of these genes, we have constructed genomic libraries from S. coelicolor A3(2) in pUC vectors. Recombinant clones were isolated by complementation of an Escherichia coli hisBd auxotroph. A recombinant plasmid containing a 3.4-kb fragment of genomic DNA was further characterized. When cloned in the plasmid vector, pIJ699, this f…

GeneticsbiologyBase SequenceOperonStreptomyces coelicolorGenes FungalGenetic Complementation TestMolecular Sequence DataRestriction MappingNucleic acid sequencehisBGeneral MedicineMolecular cloningbiology.organism_classificationMolecular biologyStreptomycesgenomic DNAGene clusterGeneticsEscherichia coliGenomic libraryHistidineAmino Acid SequenceCloning MolecularPlasmidsGene
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Zebrafish Reveals Different and Conserved Features of Vertebrate Neuroglobin Gene Structure, Expression Pattern, and Ligand Binding

2004

Neuroglobin has been identified as a respiratory protein that is primarily expressed in the mammalian nervous system. Here we present the first detailed analysis of neuroglobin from a non-mammalian vertebrate, the zebrafish Danio rerio. The zebrafish neuroglobin gene reveals a mammalian-type exon-intron pattern in the coding region (B12.2, E11.0, and G7.0), plus an additional 5'-non-coding exon. Similar to the mammalian neuroglobin, the zebrafish protein displays a hexacoordinate deoxy-binding scheme. Flash photolysis kinetics show the competitive binding on the millisecond timescale of external ligands and the distal histidine, resulting in an oxygen affinity of 1 torr. Western blotting, i…

GillsDNA Complementaryanimal structuresBlotting WesternDanioNeuroglobinNerve Tissue ProteinsIn situ hybridizationBiologyLigandsBinding CompetitiveBiochemistryRetinaDiffusionExonChloridesAnimalsCoding regionHistidineRNA MessengerCloning MolecularMolecular BiologyZebrafishConserved SequenceIn Situ HybridizationZebrafishMessenger RNAModels GeneticExonsOlfactory PathwaysCell Biologybiology.organism_classificationMolecular biologyIntronsRecombinant ProteinsGlobinsMitochondriaCell biologyOxygenRespiratory proteinKineticsGene Expression RegulationMicroscopy FluorescenceSpectrophotometryNeuroglobinJournal of Biological Chemistry
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Amino acid activation in Ciona ovary and developing egg

1964

E stata studiata la attivazione di alcuni amini acidi negli ovociti nell'uovo vergine e nell'uovo fecondato diCiona intestinalis. L'andamento della attivazione della glicina e stato seguito sino alla neurulazione. Il quantitativo di amino acidi attivati e minimo nell'uovo vergine, esso aumenta rapidamente dopo la fecondazione. Durante la gastrulazione la attivazione della glicina raggiunge i valori maggiori.

GlycineOvaryIn Vitro TechniquesBiologyArginineCellular and Molecular NeuroscienceChordata NonvertebrateLeucinemedicineAnimalsHistidineMolecular BiologyOvumPharmacologyAmino acid activationAlanineOvaryCell Biologybiology.organism_classificationMolecular biologyCionamedicine.anatomical_structureBiochemistryProtein BiosynthesisTyrosineMolecular MedicineFemaleExperientia
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Metabolomics discloses donor liver biomarkers associated with early allograft dysfunction

2014

Background & Aims Early allograft dysfunction (EAD) dramatically influences graft and patient outcome after orthotopic liver transplantation and its incidence is strongly determined by donor liver quality. Nevertheless, objective biomarkers, which can assess graft quality and anticipate organ function, are still lacking. This study aims to investigate whether there is a preoperative donor liver metabolomic biosignature associated with EAD. Methods A comprehensive metabolomic profiling of 124 donor liver biopsies collected before transplantation was performed by mass spectrometry coupled to liquid chromatography. Donor liver grafts were classified into two groups: showing EAD and immediate g…

Graft RejectionMalemedicine.medical_specialtyOrthotopic liver transplantationmedicine.drug_classBiopsyHistidine MetabolismGastroenterologyBile Acids and SaltsModel for End-Stage Liver DiseaseMetabolomicsPredictive Value of TestsRisk FactorsInternal medicineLipidomicsmedicineHumansMetabolomicsHistidinePhospholipidsHepatologyBile acidbusiness.industryMiddle AgedAllograftsTissue DonorsLiver TransplantationSphingomyelinsTransplantationLiverBiochemistryFemaleLysophospholipidsbusinessLiving donor liver transplantationBiomarkersJournal of Hepatology
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Interaction of iron(II)-heme and artemisinin with a peptide mimic of Plasmodium falciparum HRP-II

2007

Abstract The interaction of heme or heme-artemisinin adducts (heme-art) with different peptides mimicking repeat sequences of the Histidine-Rich-Protein-II of Plasmodium falciparum (PfHRP-II) was investigated. The pseudo-first order rate constants of the coordination of heme or heme-art onto a histidine rich peptide, used as a mimic of PfHRP-II putative heme binding sequence, are of the same order of magnitude, namely 42 and 14 s −1 , respectively. Despite the intrinsic reactivity of the carbonyl at C10 of heme-art toward a hydroxyl function, a peptide containing a serine or threonine residue does not readily react with heme-art adducts. Therefore, a much higher affinity of heme-art compare…

Heme bindingStereochemistryIronPlasmodium falciparumProtozoan ProteinsmalariaPeptide010402 general chemistry01 natural sciencesBiochemistryInorganic Chemistry03 medical and health scienceschemistry.chemical_compoundResidue (chemistry)[ SDV.BBM.BC ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]hemozoinAnimals[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]hemeHemealkylationHistidineComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesMolecular StructurebiologyHemozoinMolecular MimicryProteinsPlasmodium falciparumbiology.organism_classificationArtemisininsProtein tertiary structure3. Good health0104 chemical sciencesKineticsModels ChemicalchemistryBiochemistryartemisininPeptidesProtein Binding
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Nature of O2, CO, and CN binding to hemoprotein models

2004

Parametrization of a molecular-mechanics program to include terms specific for five- and six-coordinate transition metal complexes results in computer-simulated structures of hemo complexes. The principal new feature peculiar to five- and six-coordination is a term that measures the effect of electron-pair repulsion modified by the ligand electronegativity and takes into account the different structural possibilities. The work consists in the modification of program molecular mechanics for penta and hexacoordination. The model system takes into account the structural differences of the fixing center in the hemoglobin subunits. The customary proximal histidine is added. The macrocycle hemo I…

HemeproteinBent molecular geometryHemoglobin SubunitsCondensed Matter PhysicsLigand (biochemistry)PorphyrinAtomic and Molecular Physics and OpticsElectronegativitychemistry.chemical_compoundchemistryMyoglobinComputational chemistryPhysical and Theoretical ChemistryHistidineInternational Journal of Quantum Chemistry
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Nature of FeIII–O2, FeII–CO and FeIII–CN complexes of hemoprotein models

2003

Abstract Parametrization of a molecular-mechanics program to include terms specific for 5- and 6-coordinate transition metal complexes results in computer-simulated structures of hemo complexes. The principal new feature peculiar to 5- and 6-coordination is a term that measures the effect of electron-pair repulsion modified by the ligand electronegativity and takes into account the different structural possibilities. The work consists in the modification of program molecular mechanics for 5- and 6-coordination. The model system takes into account the structural differences of the fixing centre in the haemoglobin (Hb) subunits. The customary proximal histidine is added. The macrocycle hemo I…

HemeproteinLigandBent molecular geometryPorphyrinInorganic ChemistryElectronegativitychemistry.chemical_compoundTransition metalMyoglobinchemistryComputational chemistryMaterials ChemistryPhysical and Theoretical ChemistryHistidinePolyhedron
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Cyanide binding and heme cavity conformational transitions in **Drosophila melanogaster** hexacoordinate hemoglobin

2006

The reason for the presence of hemoglobin-like molecules in insects, such as Drosophila melanogaster, that live in fully aerobic environments has yet to be determined. Heme endogenous hexacoordination (where HisE7 and HisF8 axial ligands to the heme Fe atom are both provided by the protein) is a recently discovered mechanism proposed to modulate O-2 affinity in hemoglobins from different species. Previous results have shown that D. melanogaster hemoglobin 1 (product of the glob1 gene) displays heme endogenous hexacoordination in both the ferrous and ferric states. Here we present kinetic data characterizing the exogenous cyanide ligand binding process, and the three-dimensional structure (a…

HemeproteinStereochemistryProtein ConformationCyanideMolecular Sequence DataNeuroglobinNerve Tissue ProteinsHemeCrystallography X-RayLigandsBiochemistrychemistry.chemical_compoundHemoglobinsMiceSequence Analysis ProteinMelanogasterAnimalsDrosophila ProteinsHumansCRYSTAL-STRUCTUREHistidineHemeBinding SitesCyanidesbiologyCytoglobinCytoglobinHexacoordinatebiology.organism_classificationGlobinsFERRIC APLYSIAKineticsDrosophila melanogasterchemistryHUMAN NEUROGLOBINAPLYSIA-LIMACINA MYOGLOBINX-RAYHemoglobinDrosophila melanogaster
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Evolutionary history of the OmpR/IIIA family of signal transduction two component systems in Lactobacillaceae and Leuconostocaceae

2011

15 pages, 3 tables, 7 figures.

Histidine KinaseEvolutionMolecular Sequence DataSignal transductionEvolution MolecularBacterial ProteinsPhylogeneticsQH359-425Lactic acid bacteriaAmino Acid SequenceGeneEcology Evolution Behavior and SystematicsPhylogenyGeneticsTwo component systemLeuconostocaceaebiologyPhylogenetic treeLactobacillalesfungiLactobacillaceaebiology.organism_classificationTwo-component regulatory systemResponse regulatorLactobacillaceaeMultigene FamilyLeuconostocaceaeProtein KinasesSequence AlignmentOmpR/IIIA familyResearch Article
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Fumarate regulation of gene expression in Escherichia coli by the DcuSR (dcuSR genes) two-component regulatory system.

1998

ABSTRACT In Escherichia coli the genes encoding the anaerobic fumarate respiratory system are transcriptionally regulated by C 4 -dicarboxylates. The regulation is effected by a two-component regulatory system, DcuSR, consisting of a sensory histidine kinase (DcuS) and a response regulator (DcuR). DcuS and DcuR are encoded by the dcuSR genes (previously yjdHG ) at 93.7 min on the calculated E. coli map. Inactivation of the dcuR and dcuS genes caused the loss of C 4 -dicarboxylate-stimulated synthesis of fumarate reductase ( frdABCD genes) and of the anaerobic fumarate-succinate antiporter DcuB ( dcuB gene). DcuS is predicted to contain a large periplasmic domain as the supposed site for C 4…

Histidine KinaseGenetics and Molecular Biologymedicine.disease_causeMicrobiologyAntiportersBacterial ProteinsFumaratesmedicineEscherichia coliDicarboxylic AcidsMolecular BiologyEscherichia coliRegulation of gene expressionDicarboxylic Acid TransportersbiologySuccinate dehydrogenaseEscherichia coli ProteinsHistidine kinaseMembrane ProteinsPeriplasmic spaceGene Expression Regulation BacterialFumarate reductaseTwo-component regulatory systemDNA-Binding ProteinsSuccinate DehydrogenaseResponse regulatorMutagenesis InsertionalBiochemistryGenes Bacterialbiology.proteinCarrier ProteinsProtein KinasesSignal TransductionTranscription FactorsJournal of bacteriology
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