Results 161 to 170 of about 38,854 (208)

Microbial Alcohol, Aldehyde and Formate Ester Oxidoreductases

, 1993
Formation of alcohols by natural processes takes place in the fermentative breakdown of sugars and the oxidative dissimilation of alkanes. In view of the wide-spreadness of these processes, it is understandable that many microbial species have the capacity to degrade these compounds.
Peter W. Van Ophem, Johannis A. Duine
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Structural and Sequence Comparisons of Quinone Oxidoreductase, ζ-Crystallin, and Glucose and Alcohol Dehydrogenases

Archives of Biochemistry and Biophysics, 1996
Quinone oxidoreductase, zeta-crystallin, glucose dehydrogenase, and alcohol dehydrogenase belong to a superfamily of medium-chain dehydrogenase/reductases. The crystal structures of Escherichia coli quinone oxidoreductase (QOR) and Thermoplasma acidophilum glucose dehydrogenase have recently been determined and are compared here with the well-known ...
Karen J. Edwards, John D. Barton, Jamie Rossjohn, Jennifer M. Thorn, G.L. Taylor, David L. Ollis   +5 more
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Microbial Alcohol/Aldehyde Oxidoreductases in Enantioselective Conversions

, 1992
Microbes have an enormous diversity of alcohol and aldehyde oxidoreductases. A brief overview is given of the types known and of some novel ones discovered recently. Except from the classical, NAD-dependent, alcohol dehydrogenase (the long chain, zinc-containing type, EC 1.1.1.1), these enzymes are unexplored with respect to enantioselectivity.
Arie Geerlof, J. Bert A. Van Tol, J. A. Jongejan, Johannis A. Duine   +3 more
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Flow injection procedures for the determination of ethanol and alcohol dehydrogenase using co-immobilised bacterial luciferase and oxidoreductase

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

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

European 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, Werner Hummel, Maria‐Regina Kula, Michael Müller   +3 more
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Alcohol, lactate and glutamate sensors based on oxidoreductases with regeneration of nicotinamide adenine dinucleotide

Analytica Chimica Acta, 1978
Flowthrough enzyme electrodes are reported for determinations of alcohol, lactate and glutamate. Oxidoreductases mixed with immobilized NAD+ cofactor are held between a suitable platinum electrode and a semipermeable membrane. The coenzyme is readily regenerated either directly by electrochemical oxidation or by using phenazine methosulphate (PMS+) as ...
Albertas Malinauskas, Juozas Kulys
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Determination of hydride transfer stereospecificity of NADH-dependent alcohol-aldehyde/ketone oxidoreductase from Sulfolobus solfataricus

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.
Antonio Trincone, Licia Lama, R. Rella, Sabato D’Auria, Carlo A. Raia, Barbara Nicolaus   +5 more
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Role of epoxide hydrolase, NAD(P)H:quinone oxidoreductase, cytochrome P450 2E1 or alcohol dehydrogenase genotypes in susceptibility to colorectal cancer

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, Saskia M. Bergevoet, Hennie M.J. Roelofs, René H. M. te Morsche, Yvo van Dijk, Theo Wobbes, Fokko M. Nagengast, Wilbert H.M. Peters   +7 more
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Acyclic Monoterpene Primary Alcohol:NADP⁺ Oxidoreductase of <italic>Rauwolfia serpentina</italic> Cells: The Key Enzyme in Biosynthesis of Monoterpene Alcohols

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.
Hiromitsu Ikeda, Nobuvoshi Esaki, Shunji NAKAI, Keiji Hashimoto, Shinichi Uesato, Kenji Soda, Tetsuro Fujita   +6 more
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