Search results for "Alcohol Oxidoreductase"

showing 8 items of 28 documents

Sepiapterin reductase in cultured human cells.

1987

Sepiapterin reductase, an enzyme involved in the synthesis of tetrahydrobiopterin (the natural cofactor for phenylalanine, tyrosine and tryptophan hydroxylases), has been assayed in cultured human amniotic fibroblasts and in cultured mononuclear blood cells. In both cases, the Michaelis constants for sepiapterin and NADPH were essentially equal; 20 microM and 6 microM respectively for stimulated mononuclear blood cells and 22 microM and 5 microM respectively for amniotic fibroblasts. The inhibition by N-acetylserotonin was also similar in both cases. The concentration that produced 50% inhibition in stimulated mononuclear blood cells and in amniotic fibroblasts was 2 microM. The results str…

SepiapterinSerotoninBiophysicsPhenylalanineBiochemistryCofactorchemistry.chemical_compoundmedicineHumansAmnionTyrosineSepiapterin reductaseMolecular BiologyCells Culturedchemistry.chemical_classificationbiologyTryptophanCell BiologyTetrahydrobiopterinMolecular biologyAlcohol OxidoreductasesKineticsEnzymechemistryBiochemistrybiology.proteinLeukocytes Mononuclearmedicine.drugBiochemical and biophysical research communications
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Bacterial 2,3-butanediol dehydrogenases

1978

Enterobacter aerogenes, Aeromonas hydrophila, Serratia marcescens and Staphylococcus aureus possessing L(+)-butanediol dehydrogenase produced mainly meso-butanediol and small amounts of optically active butanediol; Acetobacter suboxydans, Bacillus polymyxa and Erwinia carotovora containing D(-)-butanediol dehydrogenase produced more optically active butanediol than meso-butanediol. Resting and growing cells of these organisms oxidezed only one enantiomer of racemic butanediol. The D(-)-butanediol dehydrogenase from Bacillus polymyxa was partially purified (30-fold) with a specific activity of 24.5. Except NAD and NADH no other cofactors were required. Optimum pH-values for oxidation and red…

Staphylococcus aureusEnterobacterBacillusDehydrogenaseBiologyEnterobacter aerogenesBiochemistryMicrobiologyCofactorchemistry.chemical_compoundGenetics23-ButanediolAcetobacterButylene GlycolsMolecular BiologySerratia marcescensChromatographyBacteriaCell-Free SystemAcetoinAcetoinTemperatureGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationDiacetylAlcohol OxidoreductaseschemistryBiochemistryButanediolbiology.proteinErwiniaAeromonasNAD+ kinaseOxidation-ReductionArchives of Microbiology
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Retinoid dynamics in chicken eye during pre- and postnatal development.

1994

Changes in the steady state level of retinols, retinaldehydes and retinyl esters in the trans and 11-cis forms and trans retinoic acid were measured in whole chicken eye during development from day 6 in ovo to day 3 post-hatch. These retinoids, quantified by different HPLC systems, were detected in this time sequence: trans-retinol and trans-retinyl esters in the first week in ovo, 11-cis-retinol in the second week. The highest level of 11-cis-retinaldehyde and 11-cis-retinyl esters was reached at the end of development in ovo; however, their levels increased further after hatching. The retinoic acid level decreased at the end of the first week, rising again at the end of the second week. T…

animal structuresgenetic structuresmedicine.drug_classClinical BiochemistryRetinoic acidDehydrogenaseTretinoinChick EmbryoEyeAndrologychemistry.chemical_compoundRetinoidsmedicineAnimalsRetinoidVitamin AMolecular Biologychemistry.chemical_classificationRetinolCell BiologyGeneral MedicineMetabolismAlcohol OxidoreductasesEnzymechemistryBiochemistryAcyltransferaseembryonic structuresRetinaldehydeRetinaldehydeChickensMolecular and cellular biochemistry
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Regulatory changes in pterin and carotenoid genes underlie balanced color polymorphisms in the wall lizard

2019

Significance Reptiles show an amazing color diversity based on variation in melanins, carotenoids, and pterins. This study reveals genes controlling differences between three color morphs (white, orange, and yellow) in the common wall lizard. Orange pigmentation, due to high levels of orange/red pterins in skin, is caused by genetic changes in the sepiapterin reductase gene. Yellow skin, showing high levels of yellow carotenoids, is controlled by the beta-carotene oxygenase 2 locus. Thus, the color polymorphism in the common wall lizard is associated with changes in two small regions of the genome containing genes with crucial roles in pterin and carotenoid metabolism. These genes are likel…

balanced polymorphismBalanced polymorphismgenetic structuresEvolutionIntrogressionintrogressionColorpterin pigmentationSkin PigmentationDioxygenasesEvolutionsbiologiGeneticAnimalscarotenoid pigmentationPolymorphismPterin pigmentationEvolutionary BiologyPolymorphism GeneticBalanced polymorphism; Carotenoid pigmentation; Introgression; Podarcis muralis; Pterin pigmentation; Alcohol Oxidoreductases; Animals; Carotenoids; Color; Dioxygenases; Lizards; Pigmentation; Polymorphism Genetic; Pterins; Skin PigmentationPigmentationLizardsBiological SciencesCarotenoidsPterinsAlcohol OxidoreductasesPNAS PlusCarotenoid pigmentationPodarcis muralissense organs
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Chromatin structure of the 5′ flanking region of the yeastLEU2 gene

1989

The chromatin structure of theLEU2 gene and its flanks has been studied by means of nuclease digestion, both with micrococcal nuclease and DNase I. The gene is organized in an array of positioned nucleosomes. Within the promoter region, the nucleosome positioning places the regulatory sequences, putative TATA box and upstream activator sequence outside the nucleosomal cores. The tRNA3 Leu gene possesses a characteristic structure and is protected against nucleases. Most of the 5′ flank is sensitive to DNase I digestion, although no clear hypersensitive sites were found. The chromatin structure is independent of either the transcriptional state of the gene or the chromosomal or episomal loca…

biologyGenes Fungal5' flanking regionSaccharomyces cerevisiaeTATA BoxMolecular biologyChromatinChromatin3-Isopropylmalate DehydrogenaseAlcohol OxidoreductasesGeneticsbiology.proteinDeoxyribonuclease IMicrococcal NucleaseNucleosomeDNase I hypersensitive siteDeoxyribonuclease IMolecular BiologyHypersensitive siteAllelesChIA-PETMicrococcal nucleaseMolecular and General Genetics MGG
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Reduction of benzo(a)pyrene mutagenicity by dihydrodiol dehydrogenase

1979

THE enigma of how inert chemicals can exert potent mutagenic, carcinogenic, allergenic and cytotoxic effects has been much debated. It has been learned that such compounds are metabolically converted to chemically reactive species1. In the case of aromatic or olefinic compounds, monooxygenases located in the membranes of the cell can transform these compounds into epoxides2–5 which by virtue of electrophilic reactivity can bind chemically to cellular macromolecules such as DNA, RNA and proteins, thereby disturbing biochemical control mechanisms and leading to the above mentioned toxic effects. The same membranes in which such epoxides are produced possess an enzyme, epoxide hydratase, which…

chemistry.chemical_classificationMultidisciplinarybiologyChemistryEpoxideMonooxygenaseCofactorAlcohol OxidoreductasesMiceStructure-Activity Relationshipchemistry.chemical_compoundEnzymeBiochemistryBenzo(a)pyreneMutationMicrosomes Liverpolycyclic compoundsbiology.proteinAnimalsPyreneBenzopyrenesBiotransformationCarcinogenDNANature
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Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superf…

2006

Perakine reductase (PR) is a novel member of the aldo-keto reductase enzyme superfamily from higher plants. PR from the plant Rauvolfia serpentina is involved in the biosynthesis of monoterpenoid indole alkaloids by performing NADPH-dependent reduction of perakine, yielding raucaffrinoline. However, PR can also reduce cinnamic aldehyde and some of its derivatives. After heterologous expression of a triple mutant of PR in Escherichia coli, crystals of the purified and methylated enzyme were obtained by the hanging-drop vapour-diffusion technique at 293 K with 100 mM sodium citrate pH 5.6 and 27% PEG 4000 as precipitant. Crystals belong to space group C222(1) and diffract to 2.0 A, with unit-…

endocrine systemStereochemistryAldo-Keto ReductasesBiophysicsAlcohol oxidoreductaseReductaseCrystallography X-Raymedicine.disease_causeBiochemistryRauwolfiachemistry.chemical_compoundBiosynthesisAldehyde ReductaseStructural BiologyRauvolfia serpentinaGeneticsmedicineEscherichia colichemistry.chemical_classificationAldo-keto reductasebiologyCondensed Matter Physicsbiology.organism_classificationAlcohol OxidoreductasesEnzymeBiochemistrychemistryCrystallization CommunicationsHeterologous expressionCrystallizationActa Crystallographica Section F Structural Biology and Crystallization Communications
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The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS

2007

Membrane fission is an essential process in membrane trafficking and other cellular functions. While many fissioning and trafficking steps are mediated by the large GTPase dynamin, some fission events are dynamin independent and involve C-terminal-binding protein-1/brefeldinA-ADP ribosylated substrate (CtBP1/BARS). To gain an insight into the molecular mechanisms of CtBP1/BARS in fission, we have studied the role of this protein in macropinocytosis, a dynamin-independent endocytic pathway that can be synchronously activated by growth factors. Here, we show that upon activation of the epidermal growth factor receptor, CtBP1/BARS is (a) translocated to the macropinocytic cup and its surroundi…

genetic structuresEndocytic cycleGTPaseBiologyTRANSCRIPTIONAL COREPRESSOREPIDERMAL GROWTH-FACTORArticleGeneral Biochemistry Genetics and Molecular BiologySYNAPTIC VESICLE ENDOCYTOSISMembrane fissionCell Line TumorMacropinocytic cupHumansPhosphorylationMacropinosomeMolecular BiologyDynaminEpidermal Growth FactorGeneral Immunology and MicrobiologyMEMBRANE FISSIONGeneral NeuroscienceActinsEnterovirus B HumanProtein Structure TertiaryTransport proteinCell biologyDNA-Binding ProteinsAlcohol OxidoreductasesProtein Transportp21-Activated KinasesPLASMA-MEMBRANEPinocytosisPhosphorylationCell Surface ExtensionsIntegrin alpha2beta1The EMBO Journal
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