Results 231 to 240 of about 943,763 (288)

Flow injection procedures for the determination of ethanol and alcohol dehydrogenase using co-immobilised bacterial luciferase and oxidoreductase

open access: closedThe 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
openalex   +3 more sources

Alcohol dehydrogenase 1 and NAD(H)-linked methylglyoxal oxidoreductase reciprocally regulate glutathione-dependent enzyme activities in Candida albicans

open access: closedJournal 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
openalex   +3 more sources

Enantioselective Synthesis of Both Enantiomers of Various Propargylic Alcohols by Use of Two Oxidoreductases

open access: closedEuropean Journal of Organic Chemistry, 2001
The oxidoreductases Lactobacillus brevis alcohol dehydrogenase (LBADH) and Candida parapsilosis carbonyl reductase (CPCR) are suitable catalysts for the reduction of ketones to afford enantiopure sec. alcohols. A broad variety of alkynones (1, 3, and 5) are accepted as substrates and the corresponding propargylic alcohols (2, 4, and 6) are obtained in ...
Thomas Schubert   +3 more
openalex   +2 more sources

Determination of hydride transfer stereospecificity of NADH-dependent alcohol-aldehyde/ketone oxidoreductase from Sulfolobus solfataricus

open access: closedBiochimica 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.
Antonio Trincone   +5 more
openalex   +5 more sources

Role of epoxide hydrolase, NAD(P)H:quinone oxidoreductase, cytochrome P450 2E1 or alcohol dehydrogenase genotypes in susceptibility to colorectal cancer

open access: closedMutation 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
openalex   +4 more sources

Acyclic Monoterpene Primary Alcohol:NADP<sup>+</sup> Oxidoreductase of <italic>Rauwolfia serpentina</italic> Cells: The Key Enzyme in Biosynthesis of Monoterpene Alcohols

open access: closedJournal 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.
Hiromitsu Ikeda   +6 more
openalex   +3 more sources

Cytosolic NAD(P)H:(Quinone‐acceptor)oxidoreductase in human normal and tumor tissue: Effects of cigarette smoking and alcohol

open access: closedInternational 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,
John J. Schlager, Garth Powis
openalex   +3 more sources

Microbial alcohol dehydrogenases: recent developments and applications in asymmetric synthesis.

Organic and biomolecular chemistry, 2023
Alcohol dehydrogenases are a well-known group of enzymes in the class of oxidoreductases that use electron transfer cofactors such as NAD(P)+/NAD(P)H for oxidation or reduction reactions of alcohols or carbonyl compounds respectively.
Anju Chadha   +4 more
semanticscholar   +1 more source

Potential applications of an alcohol-aldehyde/ketone oxidoreductase from thermophilic bacteria

Enzyme and Microbial Technology, 1981
Practical uses of a novel alcohol dehydrogenase from Thermoanaerobium brockii have been examined in crude and purified form. Stoichiometric reduction of NADP (50 mg) was demonstrated with agarose-immobilized enzyme and 0.3 (v/v) 2-propanol solution as reductant.
R.J. Lamed, E. Keinan, J.G. Zeikus
openaire   +1 more source

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