Search results for "Flavin-Adenine Dinucleotide"

showing 5 items of 5 documents

Photobleaching effects onin vivoskin autofluorescence lifetime

2015

The autofluorescence lifetime of healthy human skin was measured using excitation provided by a picosecond diode laser operating at a wavelength of 405 nm and with fluorescence emission collected at 475 and 560 nm. In addition, spectral and temporal responses of healthy human skin and intradermal nevus in the spectral range 460 to 610 nm were studied before and after photobleaching. A decrease in the autofluorescences lifetimes changes was observed after photobleaching of human skin. A three-exponential model was used to fit the signals, and under this model, the most significant photoinduced changes were observed for the slowest lifetime component in healthy skin at the spectral range 520 …

AdultTime FactorsMaterials scienceLightPhotochemistryBiomedical EngineeringHuman skinAbsorption (skin)LipofuscinBiomaterialsNuclear magnetic resonanceFlavinsIntradermal NevusmedicineHumansNevusskin and connective tissue diseasesPhospholipidsSkinInflammationPhotobleachingbusiness.industryEquipment DesignMiddle AgedHandmedicine.diseasePhotobleachingFluorescenceAtomic and Molecular Physics and OpticsElectronic Optical and Magnetic MaterialsAutofluorescenceSpectrometry FluorescenceOxyhemoglobinsPicosecondFlavin-Adenine DinucleotideNevus IntradermalOptoelectronicsbusinessJournal of Biomedical Optics
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Post-Translational Regulation of CYP450s Metabolism As Revealed by All-Atoms Simulations of the Aromatase Enzyme.

2019

Phosphorylation by kinases enzymes is a widespread regulatory mechanism able of rapidly altering the function of target proteins. Among these are cytochrome P450s (CYP450), a superfamily of enzymes performing the oxidation of endogenous and exogenous substrates thanks to the electron supply of a redox partner. In spite of its pivotal role, the molecular mechanism by which phosphorylation modulates CYP450s metabolism remains elusive. Here by performing microsecond-long all-atom molecular dynamics simulations, we disclose how phosphorylation regulates estrogen biosynthesis, catalyzed by the Human Aromatase (HA) enzyme. Namely, we unprecedentedly propose that HA phosphorylation at Y361 markedl…

CytochromeFlavin MononucleotideProtein ConformationGeneral Chemical EngineeringFlavin mononucleotide-Oxidative phosphorylationLibrary and Information SciencesMolecular Dynamics Simulation01 natural scienceschemistry.chemical_compoundAromatase0103 physical sciencesPost-translational regulationAromatasePhosphorylationBinding Sites010304 chemical physicsbiologyKinaseGeneral ChemistryMetabolism0104 chemical sciencesComputer Science ApplicationsCell biology010404 medicinal & biomolecular chemistrychemistrySettore CHIM/03 - Chimica Generale E Inorganicabiology.proteinFlavin-Adenine DinucleotidePhosphorylationQuantum TheoryProtein Processing Post-TranslationalNADPJournal of chemical information and modeling
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Antimutagenic effects and possible mechanisms of action of vitamins and related compounds against genotoxic heterocyclic amines from cooked food.

1999

Possible antimutagenic activity of 26 vitamins and related compounds - ascorbic acid, beta-carotene, cyanocobalamin, folic acid, nicotinic acid, nicotinamide, pantothenic acid, pyridoxale, pyridoxamine, pyridoxine, retinal, retinol, retinoic acid, retinyl acetate, retinyl palmitate, riboflavin, riboflavin 5'-phosphate, flavin adenine dinucleotide (FAD), alpha-tocopherol, alpha-tocopherol acetate, vitamins K(1), K(3), K(4), 1, 4-naphthoquinone, and coenzyme Q(10) - was tested against six heterocyclic amine (HCA) mutagens, i.e., 2-amino-3-methyl-imidazo[4, 5-f]quinoline (IQ), 2-amino-3,4-dimethyl-imidazo[4,5-f]quinoline (MeIQ), 2-amino-3,8-dimethyl-imidazo[4,5-f]quinoxaline (MeIQx), 2-amino-1…

MaleSalmonella typhimuriumHot TemperatureVitamin KHealth Toxicology and MutagenesisRiboflavinFood ContaminationRetinyl acetateIn Vitro TechniquesRats Sprague-Dawleychemistry.chemical_compoundMenadioneRetinyl palmitateGeneticsAnimalsVitamin ABiotransformationFlavin adenine dinucleotidechemistry.chemical_classificationNicotinamideMutagenicity TestsAntimutagenic AgentsVitaminsAscorbic acidRatschemistryBiochemistryHeterocyclic amineFlavin-Adenine DinucleotideMicrosomes LiverQuinolinesFood AnalysisMutagensMutation research
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Cholesterol oxidase: ultrahigh-resolution crystal structure and multipolar atom model-based analysis

2015

International audience; Author(s) of this paper may load this reprint on their own web site or institutional repository provided that this cover page is retained. Republication of this article or its storage in electronic databases other than as specified above is not permitted without prior permission in writing from the IUCr. For further information see http://journals.iucr.org/services/authorrights.html Acta Cryst. (2015). D71, 954-968 Zarychta et al. · Cholesterol oxidase research papers 954 http://dx. Examination of protein structure at the subatomic level is required to improve the understanding of enzymatic function. For this purpose, X-ray diffraction data have been collected at 100…

Models MolecularElectron densityCholesterol oxidaseProtein ConformationCrystallography X-Ray010402 general chemistry01 natural sciences03 medical and health scienceschemistry.chemical_compoundProtein structureStructural Biologycholesterol oxidase[CHIM.CRIS]Chemical Sciences/Cristallography[CHIM]Chemical Sciences030304 developmental biologyFlavin adenine dinucleotide0303 health sciencesHydrogen bondIntermolecular forceResolution (electron density)Hydrogen BondingGeneral MedicineStreptomyces0104 chemical sciencesBond lengthCrystallographychemistryFlavin-Adenine Dinucleotide
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Xanthine oxidase catalyzes the synthesis of retinoic acid

2001

Milk xanthine oxidase (xanthine: oxygen oxidoreductase; XO; EC 1.1.3.22) was found to catalyze the conversion of retinaldehyde to retinoic acid. The ability of XO to synthesize all trans-retinoic acid efficiently was assessed by its turnover number of 31.56 min-1, determined at pH 7.0 with 1 nM XO and all trans-retinaldehyde varying between 0.05 to 2 microM. The determination of both retinoid and purine content in milk was also considered in order to correlate their concentrations with kinetic parameters of retinaldehyde oxidase activity. The velocity of the reaction was dependent on the isomeric form of the substrate, the all trans- and 9-cis-forms being the preferred substrates rather tha…

Xanthine OxidaseStereochemistryRetinoic AcidMolecular ConformationRetinoic acidAllopurinolTretinoinXanthineBiochemistrychemistry.chemical_compoundOxidoreductaseSettore BIO/10 - BiochimicamedicineAnimalsXanthine oxidaseChromatography High Pressure Liquidchemistry.chemical_classificationOxidase testChemistryHydrogen-Ion ConcentrationNADXanthineUric AcidOxygenMilkXanthine dehydrogenaseBiochemistryRetinaldehydeFlavin-Adenine DinucleotideRetinaldehydeMolecular MedicineRetinaldehyde OxidasePurine inhibitionmedicine.drug
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