Search results for "Tryptophan"

showing 10 items of 141 documents

Phenylalanine Hydroxylase Participation in the Synthesis of Serotonin and Pteridines in Drosophila melanogaster

1997

Abstract Phenylalanine hydroxylase is involved in the synthesis of serotonin and pteridines, probably catalysing the hydroxylation of tryptophan and a tetrahydropterin oxidase reaction, respectively. Supplementation of the wild-type Drosophila diet with either L-Phe or L-Trp induced a significant increase in the phenylalanine hydroxylase concentration, while L-Tyr supplementation had no effect. The level of serotonin in adult heads of the PAH-defective mutant Henna recessive-3 was significantly lower than that obtained for the wild-type strain. A 4-fold increase in the concentration of phenylalanine hydroxylase is observed during the pharate adult head development. It occurs in parallel wit…

PharmacologyPhenylalanine hydroxylasebiologyTyrosine hydroxylaseImmunologyTryptophanTryptophan hydroxylaseHydroxylationchemistry.chemical_compoundchemistryBiochemistrybiology.proteinAromatic amino acidsSerotonin5-HydroxytryptophanComparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology
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Regulation of pteridine biosynthesis and aromatic amino acid hydroxylation in Drosophila melanogaster

1989

The relationship between high dietary levels of aromatic amino acid and regulation of pteridines in Drosophila eyes was examined by measuring changes in pool levels of six pterins in the wild type and mutants and amino acid pool levels in flies that carry mutations for pteridine biosynthesis. The effect upon relative viability and developmental times was also analyzed; relative viability was affected by L-phenylalanine, L-tryptophan, and L-tyrosine in decreasing order and the D-amino acids had little or no effect. The changes in concentration of biopterin, dihydrobiopterin, pterin, sepiapterin, drosopterins, and isoxanthopterin showed a characteristic pattern of increased and/or decreased a…

PhenylalanineBiopterinPhenylalanineBiologyHydroxylationBiochemistrychemistry.chemical_compoundDihydrobiopterinGeneticsmedicineAromatic amino acidsAnimalsAmino AcidsPterinMolecular BiologyEcology Evolution Behavior and Systematicschemistry.chemical_classificationPteridinesTryptophanGeneral MedicineTetrahydrobiopterinAmino acidDrosophila melanogasterchemistryBiochemistryMutationTyrosinePteridinemedicine.drug
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Intramolecular Electron Transfer between Tyrosine and Tryptophan Photosensitized by a Chiral π,π* Aromatic Ketone

2005

The photochemical reaction of Trp and Tyr and related peptides with Suprofen (SUP) as sensitizer in H2O/CH3CN (28:1 v/v) solutions has been studied by time-resolved spectroscopy. The results show that SUP induces oxidation of both Trp and Tyr, as well as intramolecular-ET reactions in the related peptides. The influence of photosensitizer configuration on the involved processes has been studied by using the enantiomerically pure compounds. A significant chiral recognition is observed in which the concentration of the radicals formed after triplet quenching depends on the configuration of the chiral center; the quenching process is higher when using the (R)-SUP enantiomer.

PhotolysisQuenching (fluorescence)ChemistryRadicalAnti-Inflammatory Agents Non-SteroidalOrganic ChemistryTryptophanTryptophanSuprofenStereoisomerismSuprofenGeneral ChemistryPhotochemistryCatalysisKineticsElectron transferModels ChemicalIntramolecular forcemedicineTyrosinePhotosensitizerEnantiomermedicine.drugChemistry - A European Journal
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Effects of indole-3-acetic acid on Sinorhizobium meliloti survival and on symbiotic nitrogen fixation and stem dry weight production

2009

We evaluated the effects of the main auxin phytohormone, indole-3-acetic acid (IAA), on the central metabolism of Sinorhizobium meliloti strain 1021. We either treated the Sinorhizobium meliloti 1021 strain with 0.5 mM IAA (1021+) or use a derivative, RD64, of the same strain harbouring a pathway for IAA biosynthesis converting tryptophan into IAA via indoleacetamide. We assayed the activity of key enzymes in the major energy-yielding pathways (Entner-Doudoroff, Embden-Meyerhof-Parnas, pentose phosphate, glyoxylate bypass and tricarboxylic acid cycle). We found that activity of two main regulative tricarboxylic acid (TCA) cycle enzymes was increased. Citrate synthase (CS) activity, as compa…

PolyestersHydroxybutyratesDehydrogenaseCitrate (si)-SynthaseApplied Microbiology and BiotechnologyCell survival . PHB . TCA . Nitrogen fixationchemistry.chemical_compoundBacterial ProteinsPlant Growth RegulatorsAcetyl Coenzyme AAuxinNitrogen FixationMedicago truncatulaCitrate synthaseKetoglutarate Dehydrogenase ComplexBiomasschemistry.chemical_classificationSinorhizobium melilotiMicrobial ViabilityIndoleacetic AcidsPlant StemsbiologyTryptophanfood and beveragesGeneral MedicineMetabolismbiology.organism_classificationCitric acid cycleBiochemistrychemistrybiology.proteinIndole-3-acetic acidSinorhizobium melilotiBiotechnologyApplied Microbiology and Biotechnology
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Genetic diversity within the R408W phenylketonuria mutation lineages in Europe

2003

The R408W phenylketonuria mutation in Europe has arisen by recurrent mutation in the human phenylalanine hydroxylase (PAH) locus and is associated with two major PAH haplotypes. R408W-2.3 exhibits a west-to-east cline of relative frequency reaching its maximum in the Balto–Slavic region, while R408W-1.8 exhibits an east-to-west cline peaking in Connacht, the most westerly province of Ireland. Spatial autocorrelation analysis has demonstrated that the R408W-2.3 cline, like that of R408W-1.8, is consistent with a pattern likely to have been established by human dispersal. Genetic diversity within wild-type and R408W chromosomes in Europe was assessed through variable number tandem repeat (VNT…

Population geneticsEurope; PAH; Phenylalanine hydroxylase; Phenylketonuria; PKU; Population genetics; STR; VNTR;VNTRPopulation geneticsLocus (genetics)Minisatellite RepeatsBiologyArginineSTRPhenylketonuriasGeneticsHumansPhenylketonuriaGenetic TestingAlleleGenetics (clinical)GeneticsGenetic diversityPhenylalanine hydroxylaseHaplotypeTryptophanGenetic VariationCline (biology)PAHFounder EffectEuropeVariable number tandem repeatAmino Acid SubstitutionPKUMutationMicrosatelliteMicrosatellite Repeats
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HPLC demonstration that an all Trp--Phe replacement in gramicidin A results in a conformational rearrangement from beta-helical monomer to double-str…

1995

We have taken advantage of our previously reported high performance liquid chromatographic (HPLC) strategy to investigate the conformational behavior of the optically reversed gramicidin M (gM-), an analog of gramicidin A with all tryptophans replaced by phenylalanines, in different model membranes. It is quantitatively demonstrated for the first time that once inserted in the lipid environment, gM- (unlike the native peptide) undergoes a conformational transition from beta-helical monomers to thermodynamically stable double-stranded dimers. This transition is faster the higher the incubation temperature and can be neatly observed in both small unilamellar phospholipid vesicles and lysophos…

Protein ConformationDimerPhenylalanineBiophysicsPeptideBiochemistryMicelleHigh-performance liquid chromatographyIon ChannelsProtein Structure Secondarychemistry.chemical_compoundStructure-Activity RelationshipGramicidin AOrganic chemistryMolecular BiologyChromatography High Pressure Liquidchemistry.chemical_classificationChemistrytechnology industry and agricultureGramicidinTryptophanMembrane ProteinsMembranes ArtificialCell BiologyCrystallographyMembraneMonomerlipids (amino acids peptides and proteins)Double strandedBiochemical and biophysical research communications
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Conformational changes involved in thermal aggregation processes of bovine serum albumin

2003

We report a kinetic study on thermal aggregation process of the model protein bovine serum albumin (BSA) in low concentration regime. Aim of this study is to provide information on relationship between conformational changes and initial step of aggregation. The experimental approach is based on steady-state fluorescence spectra of the two tryptophans located in two different domains, in way to study conformational changes in the surrounding of these residues. We also follow emission spectra of Fluorescein-5-Maleimide dye bound to the single free cysteine of BSA. Complementary information on the extent of aggregation and on the structural changes is obtained by Rayleigh scattering and circul…

Protein DenaturationCircular dichroismHot TemperatureLightKineticsSerum albuminBiophysicsProtein aggregationCircular dichroismBiochemistryProtein Structure SecondaryProtein structureAnimalsHumansScattering RadiationCysteineBovine serum albuminPhysical and Theoretical ChemistryProtein secondary structurebiologyChemistryOrganic ChemistryTryptophanSerum Albumin BovineFluoresceinsConformational changeProtein Structure TertiaryKineticsCrystallographySpectrometry FluorescenceBovine serum albuminSteady-state fluorescencebiology.proteinCattlesense organsProtein aggregationCysteine
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TrpM, a Small Protein Modulating Tryptophan Biosynthesis and Morpho-Physiological Differentiation in Streptomyces coelicolor A3(2).

2016

In the model actinomycete Streptomyces coelicolor A3(2), small open reading frames encoding proteins with unknown functions were identified in several amino acid biosynthetic gene operons, such as SCO2038 (trpX) in the tryptophan trpCXBA locus. In this study, the role of the corresponding protein in tryptophan biosynthesis was investigated by combining phenotypic and molecular analyses. The 2038KO mutant strain was characterized by delayed growth, smaller aerial hyphae and reduced production of spores and actinorhodin antibiotic, with respect to the WT strain. The capability of this mutant to grow on minimal medium was rescued by tryptophan and tryptophan precursor (serine and/or indole) su…

Proteomics0301 basic medicineProtein ExtractionMutantlcsh:MedicineStreptomyces coelicolor A3(2)Settore BIO/19 - Microbiologia GeneraleBiochemistrySerinechemistry.chemical_compoundAromatic Amino AcidsSmall ProteinAntibioticsTRPMMicrobial PhysiologyMedicine and Health SciencesBacterial PhysiologyAmino Acidslcsh:ScienceProtein MetabolismExtraction TechniquesMultidisciplinarybiologyOrganic CompoundsAntimicrobialsStreptomyces coelicolorTryptophanDrugsChemistryBiochemistryPhysical SciencesPhysiological DifferentiationResearch ArticleTryptophan BiosynthesiSmall Protein; Biosynthesis; Morpho-Physiological Differentiation: Streptomyces coelicolorBiosynthesisResearch and Analysis MethodsMicrobiologyStreptomycesActinorhodin03 medical and health sciencesBiosynthesisMicrobial ControlBacterial SporesPharmacology030102 biochemistry & molecular biologyOrganic Chemistrylcsh:RChemical CompoundsTryptophanTrpM; Small Protein; Tryptophan Biosynthesis; Morphological Differentiation; Physiological Differentiation; Streptomyces coelicolor A3(2); ProteomicsBiology and Life SciencesProteinsBacteriologybiology.organism_classificationAmino Acid MetabolismMetabolism030104 developmental biologychemistrylcsh:QMorphological DifferentiationTrpM
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The Role of Site-Specific Hydrogen Bonding Interactions in the Solvation Dynamics of N-Acetyltryptophanamide

2012

Measurements of the ultrafast broadband UV fluorescence of N-acetyltryptophanamide (NATA) provide detailed information on its relaxation patterns in three different solvents: methanol (MeOH), water and acetonitrile (ACN). Several processes leading to excited state solvation and cooling are found to occur on different characteristic time scales and are thoroughly analyzed. Comparison between protic MeOH and aprotic ACN allows one to single out a 12 Ps component in the former, which is attributed to the rearrangement of H-bonds existing between the protic solvent and excited NATA. This significantly stabilizes the excited state and provides the molecule with an efficient cooling mechanism. Th…

Quenching (fluorescence)ChemistryHydrogen bondFluorescence up-conversionSettore FIS/01 - Fisica SperimentaleTryptophanSolvationQuantum yieldhydrogen bondingPhotochemistrySurfaces Coatings and Filmschemistry.chemical_compoundExcited stateMaterials ChemistryMoleculesolvationPhysical and Theoretical ChemistryAcetonitrileProtic solventThe Journal of Physical Chemistry B
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Photosensibilisierte Oxidation von Lysozym bei Verschiedenen Wellenlängen

1974

The photooxidation of lysozyme in the presence of methylene blue, riboflavine, and bengal rose at differentpH values and wavelengths was studied. Monochromatic irradiation at shorter wavelengths (345 and 365 nm) is - in contrast to visible light - characterized by higher energy yields and lower oxygen consumption. This behavior suggests that the mechanism of photooxidation depends on the wavelength. The specific destruction of amino acid residues is also wavelength-dependent. Using visible light of 448 and 621 nm for riboflavine and methylene blue, respectively, we have confirmed the selective destruction of histidine and tryptophan atpH 7,0. The energy yield for the destruction of tryptoph…

Radiationdigestive oral and skin physiologyBiophysicsCystineTryptophanfood and beveragesPhotochemistryeye diseasesstomatognathic diseaseschemistry.chemical_compoundchemistryRose bengalsense organsIrradiationLysozymeMethylene blueHistidineGeneral Environmental ScienceVisible spectrumRadiation and Environmental Biophysics
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