Results 181 to 190 of about 917,246 (220)
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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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The Analyst, 1987
Bacterial luciferase and oxidoreductase extracted from Vibrio harveyi were co-immobilised on cyanogen bromide-activated Sepharose 4B and used in a flow injection manifold for the rapid and sensitive determination of ethanol and alcohol dehydrogenase. The detection limits were 30 pmol for ethanol and 0.03 pmol for alcohol dehydrogenase.
Abdul Nabi, Paul J. Worsfold
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Bacterial luciferase and oxidoreductase extracted from Vibrio harveyi were co-immobilised on cyanogen bromide-activated Sepharose 4B and used in a flow injection manifold for the rapid and sensitive determination of ethanol and alcohol dehydrogenase. The detection limits were 30 pmol for ethanol and 0.03 pmol for alcohol dehydrogenase.
Abdul Nabi, Paul J. Worsfold
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Journal of Biochemistry (Tokyo), 2015
Hyperthermophilic bacteria Thermotoga maritima and Thermotoga hypogea produce ethanol as a metabolic end product, which is resulted from acetaldehyde reduction catalysed by an alcohol dehydrogenase (ADH).
M. Eram +3 more
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Hyperthermophilic bacteria Thermotoga maritima and Thermotoga hypogea produce ethanol as a metabolic end product, which is resulted from acetaldehyde reduction catalysed by an alcohol dehydrogenase (ADH).
M. Eram +3 more
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Process Biochemistry, 2010 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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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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Asymmetric chemoenzymatic synthesis of ramatroban using lipases and oxidoreductases.
Journal of Organic Chemistry, 2012A chemoenzymatic asymmetric route for the preparation of enantiopure (R)-ramatroban has been developed for the first time. The action of lipases and oxidoreductases has been independently studied, and both were found as excellent biocatalysts for the ...
E. Busto +2 more
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Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis, 2005 Colorectal cancer (CRC) is one of the most common forms of cancer in Western countries. CRC has been associated with genetic and lifestyle factors. Individual susceptibility to CRC may be due partly to variations in detoxification capacity in the gastrointestinal tract.
Elise M.J. van der Logt +7 more
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Journal of Microbiology, 2020
Glutathione reductase (Glr1) activity controls cellular glutathione and reactive oxygen species (ROS). We previously demonstrated two predominant methylglyoxal scavengers-NAD(H)-linked methylglyoxal oxidoreductase (Mgd1) and alcohol dehydrogenase 1 (Adh1)-in glutathione-depleted γ-glutamyl cysteinyl synthetase-disrupted Candida albicans.
Sa-Ouk Kang, Min-Kyu Kwak
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Glutathione reductase (Glr1) activity controls cellular glutathione and reactive oxygen species (ROS). We previously demonstrated two predominant methylglyoxal scavengers-NAD(H)-linked methylglyoxal oxidoreductase (Mgd1) and alcohol dehydrogenase 1 (Adh1)-in glutathione-depleted γ-glutamyl cysteinyl synthetase-disrupted Candida albicans.
Sa-Ouk Kang, Min-Kyu Kwak
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Molecular characterization of microbial alcohol dehydrogenases.
Critical reviews in microbiology, 1994There is an astonishing array of microbial alcohol oxidoreductases. They display a wide variety of substrate specificities and they fulfill several vital but quite different physiological functions. Some of these enzymes are involved in the production of
Matthew F. Reid, C. A. Fewson
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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.
Gary W. Winston, Antal K.D. Hajos
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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.
Gary W. Winston, Antal K.D. Hajos
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