Results 171 to 180 of about 10,583 (192)
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Biochemical and Biophysical Research Communications, 2012
Alcohol dehydrogenases (ADHs) from thermophilic microorganisms are interesting enzymes that have their potential applications in biotechnology and potentially provide insight into the mechanisms of action of thermo-tolerant proteins. The molecular mechanisms of ADHs under thermal stress in vivo have yet to be explored.
Qian, Wang +7 more
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Alcohol dehydrogenases (ADHs) from thermophilic microorganisms are interesting enzymes that have their potential applications in biotechnology and potentially provide insight into the mechanisms of action of thermo-tolerant proteins. The molecular mechanisms of ADHs under thermal stress in vivo have yet to be explored.
Qian, Wang +7 more
openaire +2 more sources
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
This paper describes the determination of stereospecificity of hydride transfer reaction of an alcohol dehydrogenase isolated from the archaebacterium Sulfolobus solfataricus. The 1H-NMR and EI-MS data indicate that the enzyme transfers the pro-R hydrogen from coenzyme to substrate and is therefore an A-specific dehydrogenase.
A Trincone +5 more
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This paper describes the determination of stereospecificity of hydride transfer reaction of an alcohol dehydrogenase isolated from the archaebacterium Sulfolobus solfataricus. The 1H-NMR and EI-MS data indicate that the enzyme transfers the pro-R hydrogen from coenzyme to substrate and is therefore an A-specific dehydrogenase.
A Trincone +5 more
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Process Biochemistry, 2011
Abstract The stereoinversion process involving two sequential stereoselective oxidation and reduction reactions by oxidoreductases was a typical and important one-pot method for chiral secondary alcohol synthesis which has great potential for industrial application.
Xiao Qing Mu +3 more
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Abstract The stereoinversion process involving two sequential stereoselective oxidation and reduction reactions by oxidoreductases was a typical and important one-pot method for chiral secondary alcohol synthesis which has great potential for industrial application.
Xiao Qing Mu +3 more
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Journal of biochemistry, 1991
Acyclic monoterpene primary alcohol:NADP+ oxidoreductase, a key enzyme in the biosynthesis of monoterpene alcohols in plants, is unstable and has been only poorly characterized. However we have established conditions which stabilize the enzyme from Rauwolfia serpentina cells, and then purified it to homogeneity.
H, Ikeda +6 more
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Acyclic monoterpene primary alcohol:NADP+ oxidoreductase, a key enzyme in the biosynthesis of monoterpene alcohols in plants, is unstable and has been only poorly characterized. However we have established conditions which stabilize the enzyme from Rauwolfia serpentina cells, and then purified it to homogeneity.
H, Ikeda +6 more
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The FEBS Journal, 2010
The in vitro Entamoeba histolytica pyruvate:ferredoxin oxidoreductase (EhPFOR) kinetic properties and the effect of oxidative stress on glycolytic pathway enzymes and fluxes in live trophozoites were evaluated. EhPFOR showed a strong preference for pyruvate as substrate over other oxoacids.
Erika, Pineda +5 more
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The in vitro Entamoeba histolytica pyruvate:ferredoxin oxidoreductase (EhPFOR) kinetic properties and the effect of oxidative stress on glycolytic pathway enzymes and fluxes in live trophozoites were evaluated. EhPFOR showed a strong preference for pyruvate as substrate over other oxoacids.
Erika, Pineda +5 more
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International Journal of Cancer, 1990
AbstractNAD(P)H:(quinone‐acceptor)oxidoreductase (QAO), previously known as DT‐diaphorase, catalyzes the reduction of qui‐nones to hydroquinones. Enhanced activity of the enzyme has been suggested to protect cells against the cellular toxicity and carcinogenicity of quinones, but may activate some cyto‐toxic anti‐tumor quinones. Cytosolic levels of QAO,
J J, Schlager, G, Powis
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AbstractNAD(P)H:(quinone‐acceptor)oxidoreductase (QAO), previously known as DT‐diaphorase, catalyzes the reduction of qui‐nones to hydroquinones. Enhanced activity of the enzyme has been suggested to protect cells against the cellular toxicity and carcinogenicity of quinones, but may activate some cyto‐toxic anti‐tumor quinones. Cytosolic levels of QAO,
J J, Schlager, G, Powis
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Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2002
Inbred strains of mice remain a valuable resource for genetic dissection of complex traits including responses to drugs and chemicals, particularly alcohol. As a novel source of candidate genes for further analysis, we have used mRNA differential displays to identify genes with differential expression in the brains of ethanol-preferring (C57BL/6J) vs ...
Michelle, Harrison, Shiva M, Singh
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Inbred strains of mice remain a valuable resource for genetic dissection of complex traits including responses to drugs and chemicals, particularly alcohol. As a novel source of candidate genes for further analysis, we have used mRNA differential displays to identify genes with differential expression in the brains of ethanol-preferring (C57BL/6J) vs ...
Michelle, Harrison, Shiva M, Singh
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Archives of Biochemistry and Biophysics, 1992
Rats fed an ethanol-containing diet for 4 weeks showed a 3- to 5-fold increase over isocalorically pair-fed controls with respect to cytosolic NAD(P)H-quinone oxidoreductase (NQOR) (E.C.1.6.99.2) with both menadione and dichlorophenol-indophenol as substrates.
A K, Hajos, G W, Winston
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Rats fed an ethanol-containing diet for 4 weeks showed a 3- to 5-fold increase over isocalorically pair-fed controls with respect to cytosolic NAD(P)H-quinone oxidoreductase (NQOR) (E.C.1.6.99.2) with both menadione and dichlorophenol-indophenol as substrates.
A K, Hajos, G W, Winston
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Substrate specificity of citrus alcohol: NAD oxidoreductase
Journal of Agricultural and Food Chemistry, 1971Joseph H. Bruemmer, Bongwoo. Roe
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Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity
Chemistry - A European Journal, 2021Vasilis Tseliou +2 more
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