Search results for "Histidine"

showing 10 items of 152 documents

Hyperthermal stability of neuroglobin and cytoglobin

2005

Neuroglobin (Ngb) and cytoglobin (Cygb), recent additions to the globin family, display a hexa-coordinated (bis-histidyl) heme in the absence of external ligands. Although these proteins have the classical globin fold they reveal a very high thermal stability with a melting temperature (Tm) of 100 °C for Ngb and 95 °C for Cygb. Moreover, flash photolysis experiments at high temperatures reveal that Ngb remains functional at 90 °C. Human Ngb may have a disulfide bond in the CD loop region; reduction of the disulfide bond increases the affinity of the iron atom for the distal (E7) histidine, and leads to a 3 °C increase in the Tm for ferrous Ngb. A similar Tm is found for a mutant of human Ng…

ChemistryCytoglobinMutantCell BiologyBiochemistryGlobin foldchemistry.chemical_compoundBiochemistryNeuroglobinBiophysicsThermal stabilityGlobinMolecular BiologyHemeHistidineFEBS Journal
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Nanoreactors for the multi-functionalization of poly-histidine fragments

2019

Water-soluble MBHA derivatives were found to self-assemble in a water environment to generate aggregates showing core–shell architectures. The aggregates appeared to be capable of working as nanoreactors performing a multi-functionalization of poly-histidine fragments, which after an initial interaction with the solvated oligo(ethylene glycol) shell reach the reactive core.

ChemistryShell (structure)Core (manufacturing)General ChemistryNanoreactorCatalysisNanoreactorschemistry.chemical_compoundChemical engineeringMaterials ChemistryWater environmentSurface modificationEthylene glycolHistidine
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Amino acids in the second transmembrane helix of the Lhca4 subunit are important for formation of stable heterodimeric light-harvesting complex LHCI-…

2007

Photosynthetic light-harvesting complexes (LHCs) are assembled from apoproteins (Lhc proteins) and non-covalently attached pigments. Despite a considerable amino acid sequence identity, these proteins differ in their oligomerization behavior. To identify the amino acid residues determining the heterodimerization of Lhca1 and Lhca4 to form LHCI-730, we mutated the poorly conserved second transmembrane helix of the two subunits. Mutated genes were expressed in Escherichia coli and the resultant proteins were refolded in vitro and subsequently analyzed by gel electrophoresis. Replacement of the entire second helix in Lhca4 by the one of Lhca3 abolished heterodimerization, whereas it had no eff…

ChlorophyllModels MolecularMolecular Sequence DataLight-Harvesting Protein ComplexesBiologyProtein Structure SecondarySerineSolanum lycopersicumStructural BiologyChlorophyll bindingConsensus sequenceHistidineHomology modelingAmino Acid SequenceAmino AcidsProtein Structure QuaternaryMolecular BiologyPeptide sequenceHistidinePlant Proteinschemistry.chemical_classificationPhotosystem I Protein ComplexAmino acidTransmembrane domainProtein SubunitschemistryBiochemistryMutagenesisChlorophyll Binding ProteinsDimerizationSequence AlignmentJournal of molecular biology
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How copper ions and membrane environment influence the structure of the human and chicken tandem repeats domain?

2019

Abstract Prion proteins (PrPs) from different species have the enormous ability to anchor copper ions. The N-terminal domain of human prion protein (hPrP) contains four tandem repeats of the –PHGGGWGQ– octapeptide sequence. This octarepeat domain can bind up to four Cu2+ ions. Similarly to hPrP, chicken prion protein (chPrP) is able to interact with Cu2+ through the tandem hexapeptide -HNPGYP- region (residues 53–94). In this work, we focused on the human octapeptide repeat (human Octa4, hPrP60–91) (Ac-PHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQ-NH2) and chicken hexapeptide repeat (chicken Hexa4, chPrP54–77) (Ac-HNPGYPHNPGYPHNPGYPHNPGYP-NH2) prion protein fragments. Due to the fact that PrP is a membr…

Circular dichroism010402 general chemistry01 natural sciencesBiochemistryMicelleInorganic Chemistrychemistry.chemical_compoundMembrane LipidsTandem repeatPeptide bondAnimalsHumansAmino Acid SequenceSodium dodecyl sulfateLipid bilayerMembrane mimicking environmentMicelleschemistry.chemical_classification010405 organic chemistryChemistryCopper ionsSodium Dodecyl SulfateHistidine residues0104 chemical sciencesPrion proteinsMembraneTandem Repeat SequencesBiophysicsPotentiometryThermodynamicsGlycoproteinChickensCopper
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Zn(II)-alloferon complexes - Similar sequence, different coordination modes, no antibacterial activity.

2020

Often, in the search for a highly defined scientific phenomenon, a different one becomes apparent. This was also the case of this work, in the scope of which we planned to search for metal-enhanced, novel antibacterial/ antifungal compounds. Instead, we denied the existence of such and revealed the details of the bioinorganic chemistry of Zn(II)-alloferon complexes. Zinc(II) complexes of alloferon 1 and 2, ligands with a sequential difference of one amino acid only, show a substantially different coordination pattern at physiological pH. In the case of Zn(II)-alloferon 1 species, a histamine-like binding mode is observed (N-terminal amine and imidazole of His-1) and the coordination sphere …

Coordination sphereAlloferon; Metal-antimicrobial peptide complex; Metal-peptide thermodynamics; Zinc(II)StereochemistryProton Magnetic Resonance Spectroscopychemistry.chemical_elementZincMicrobial Sensitivity Tests010402 general chemistryLigands01 natural sciencesBiochemistryMass SpectrometryInorganic ChemistryAlloferonchemistry.chemical_compoundStructure-Activity RelationshipCoordination ComplexesImidazoleMetal-antimicrobial peptide complexHistidineAmino Acid Sequencechemistry.chemical_classificationMetal-peptide thermodynamics010405 organic chemistryBioinorganic chemistryZinc(II)0104 chemical sciencesAmino acidAnti-Bacterial AgentsZincchemistryThermodynamicsChemical stabilityAmine gas treatingAntibacterial activityPeptidesJournal of inorganic biochemistry
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The sequence alteration associated with a mutational hotspot in p53 protects cells from lysis by cytotoxic T lymphocytes specific for a flanking pept…

1998

A high proportion of tumors arise due to mutation of the p53 tumor suppressor protein. A p53 hotspot mutation at amino acid position 273 from R to H, flanking a peptide epitope that spans residues 264–272, renders cells resistant to killing by human histocompatibility leukocyte antigen (HLA)-A*0201–restricted cytotoxic T lymphocytes (CTLs) specific for this epitope. Acquisition of the R to H mutation at residue 273 of the human p53 protein promotes tumor growth in vivo by selective escape from recognition by p53.264–272 peptide-specific CTLs. Synthetic 27-mer p53 polypeptides covering the antigenic nonamer region 264–272 of p53 were used as proteasome substrates to investigate whether the R…

Cytotoxicity Immunologicp53Epitopes T-LymphocyteEpitopeSubstrate SpecificityMice0302 clinical medicineTumor Cells CulturedImmunology and AllergyCytotoxic T cellPeptide sequence0303 health sciencesAntigen PresentationproteasomesHydrolysisArticles3. Good healthCysteine Endopeptidasestumor antigensCell DivisionProteasome Endopeptidase ComplexImmunologyAntigen presentationMolecular Sequence DataMice TransgenicBiologyArgininecytotoxic T lymphocytes03 medical and health sciencesAntigenMultienzyme Complexesantigen processingAnimalsHumansPoint MutationHistidineAmino Acid Sequence030304 developmental biologyBinding SitesLinear epitopeHLA-A AntigensPoint mutationCytotoxicity Tests ImmunologicMolecular biologyPeptide FragmentsCTL*Tumor Suppressor Protein p53Peptides030215 immunologyT-Lymphocytes CytotoxicThe Journal of experimental medicine
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Requirement of the Lactobacillus casei MaeKR two-component system for L-malic acid utilization via a malic enzyme pathway.

2009

ABSTRACTLactobacillus caseican metabolizel-malic acid via malolactic enzyme (malolactic fermentation [MLF]) or malic enzyme (ME). Whereas utilization ofl-malic acid via MLF does not support growth, the ME pathway enablesL. caseito grow onl-malic acid. In this work, we have identified in the genomes ofL. caseistrains BL23 and ATCC 334 a cluster consisting of two diverging operons,maePEandmaeKR, encoding a putative malate transporter (maeP), an ME (maeE), and a two-component (TC) system belonging to the citrate family (maeKandmaeR). Homologous clusters were identified inEnterococcus faecalis,Streptococcus agalactiae,Streptococcus pyogenes, andStreptococcus uberis. Our results show that ME is …

DNA BacterialLactobacillus caseiHistidine KinaseMalic enzymeCatabolite repressionDNA FootprintingMalatesGenetics and Molecular Biologymedicine.disease_causeApplied Microbiology and Biotechnologychemistry.chemical_compoundBacterial ProteinsOperonmedicineEnterococcus faecalisDirect repeatPromoter Regions Geneticchemistry.chemical_classificationEcologybiologySequence Homology Amino AcidGene Expression Profilingfungifood and beveragesStreptococcusGene Expression Regulation Bacterialbiology.organism_classificationMolecular biologyAmino acidResponse regulatorLacticaseibacillus caseichemistryBiochemistryMultigene FamilyStreptococcus pyogenesMalic acidProtein KinasesMetabolic Networks and PathwaysFood ScienceBiotechnologyProtein BindingSignal TransductionTranscription FactorsApplied and environmental microbiology
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Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches

2013

The tyrosinase gene from Ralstonia solanacearum (GenBank NP518458) was subjected to random mutagenesis resulting in tyrosinase variants (RVC10 and RV145) with up to 3.2-fold improvement in kcat, 5.2-fold lower Km and 16-fold improvement in catalytic efficiency for D-tyrosine. Based on RVC10 and RV145 mutated sequences, single mutation variants were generated with all variants showing increased kcat for D-tyrosine compared to the wild type (WT). All single mutation variants based on RV145 had a higher kcat and Km value compared to the RV145 and thus the combination of four mutations in RV145 was antagonistic for turnover, but synergistic for affinity of the enzyme for D-tyrosine. Single muta…

DNA BacterialProtein ConformationSequence analysisTyrosinasehomology modelingMolecular Sequence DataMutation Missenserandom mutagenesisBioengineeringtyrosinaseProtein Engineering010402 general chemistry01 natural sciencesApplied Microbiology and Biotechnologyenzyme catalysis03 medical and health sciencessite specific mutagenesisMissense mutationSite-directed mutagenesisHistidine030304 developmental biology0303 health sciencesRalstonia solanacearumbiologyMonophenol MonooxygenaseWild typeActive siteSequence Analysis DNAbiology.organism_classificationMolecular biologyRecombinant Proteins0104 chemical sciencesKineticsMutagenesisRalstonia solanacearumbiology.proteinTyrosineD-tyrosineMutant ProteinsBiotechnology
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Phosphorylation and DNA binding of the regulator DcuR of the fumarate-responsive two-component system DcuSR of Escherichia coli

2004

The function of the response regulator DcuR of the DcuSR fumarate two-component sensory system of Escherichia coli was analysed in vitro. Isolated DcuR protein was phosphorylated by the sensory histidine kinase, DcuS, and ATP, or by acetyl phosphate. In gel retardation assays with target promoters (frdA, dcuB, dctA), phosphoryl DcuR (DcuR-P) formed a high-affinity complex, with an apparent K D (app. K D) of 0·2–0·3 μM DcuR-P, and a low-affinity (app. K D 0·8–2 μM) complex. The high-affinity complex was formed only with promoters transcriptionally-regulated by DcuSR, whereas low-affinity binding was seen also with some DcuSR-independent promoters. The binding site of DcuR-P at the dcuB promo…

DNA BacterialTranscription GeneticMolecular Sequence DataBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundFumaratesEscherichia colimedicinePhosphorylationBinding sitePromoter Regions GeneticEscherichia coliBinding SitesBase SequenceEscherichia coli ProteinsHistidine kinasePromoterGene Expression Regulation BacterialMolecular biologyTwo-component regulatory systemDNA-Binding ProteinsResponse regulatorchemistryBiochemistryPhosphorylationProtein KinasesDNASignal TransductionTranscription FactorsMicrobiology
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Which lactic acid bacteria are responsible for histamine production in wine?

2005

Aims: To quantify the ability of 136 lactic acid bacteria (LAB), isolated from wine, to produce histamine and to identify the bacteria responsible for histamine production in wine. Methods and Results: A qualitative method based on pH changes in a plate assay was used to detect wine strains capable of producing high levels of histamine. Two quantitative, highly sensitive methods were used, an enzymatic method and HPLC, to quantify the histamine produced by LAB. Finally, an improved PCR test was carried out to detect the presence of histidine decarboxylase gene in these bacteria. The species exhibiting the highest frequency of histamine production is Oenococcus oeni. However, the concentrati…

DNA Bacterialved/biology.organism_classification_rank.speciesWineLactobacillus hilgardiiHistidine DecarboxylaseGram-Positive BacteriaApplied Microbiology and BiotechnologyPolymerase Chain Reactionchemistry.chemical_compoundLactobacillusPediococcusHistamine ProductionChromatography High Pressure LiquidWinemakingOenococcus oenibiologyved/biologyfood and beveragesGeneral Medicinebiology.organism_classificationLactobacilluschemistryBiochemistryGenes BacterialFood MicrobiologyPediococcusHistamineOenococcusLeuconostocBiotechnologyHistamineJournal of applied microbiology
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