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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 ...
K J, Edwards   +5 more
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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

Alcohol dehydrogenase (alcohol: NAD oxidoreductase) from the pea seedling

Phytochemistry, 1966
Abstract Alcohol: NAD oxidoreductase (alcohol dehydrogenase, ADH), was partially purified from pea seedlings, and with acetaldehyde gave a Michaelis constant of 4·3 × 10 −4 M. Activity was inhibited by p -chloromercuriphenylsulphonic acid, phenylmercuric acetate, O -iodosobenzoate, ferron, and other metal-binding agents.
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Sjögren-Larsson-like syndrome with bone dysplasia and normal fatty alcohol NAD+ oxidoreductase activity

Pediatric Neurology, 1992
We report a boy and girl with a "new" multiple congenital anomalies/mental retardation syndrome which resemblances Sjögren-Larsson syndrome. Both patients had a concordant pattern of anomalies consisting of congenital lamellar ichthyosis with spontaneous improvement, moderate mental retardation, mild pyramidal involvement, telecanthus, flat facies ...
E, Scalais   +4 more
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Amperometric Methods for Oxidoreductase Enzymes Based on Liquid Chromatography with Electrochemical Detection. Alcohol Dehydrogenase

Journal of Liquid Chromatography, 1979
Abstract Nicotinamide adenine dinucleotide (NAD) is an important cofactor in a number of oxidoreductase enzyme systems. The detection and quantitation of its reduced form (NADH) is the basis for a number of methods which determine both substrates and enzyme activity.
Gregory C. Davis   +2 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.
A, Nabi, P J, Worsfold
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Alcohol: NAD Oxidoreductase (E. C. 1.1.1.1.) from Peas

Journal of Food Science, 1968
SUMMARY– The substrate specificity of the enzyme alcohol: NAD oxidoreductase from seeds and pods of the pea plant ( Pisum sutivum ) was investigated. The enzyme catalyzes the oxidation of primary aliphatic alcohols especially 2‐alken‐1‐01s e.g.
openaire   +1 more source

Regulation of enzyme activity of alcohol dehydrogenase through its interactions with pyruvate-ferredoxin oxidoreductase in Thermoanaerobacter tengcongensis

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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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.
A Trincone   +5 more
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New kinetic and thermodynamic approach of one-pot synthesis of chiral alcohol by oxidoreductase from Candida parapsilosis

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
openaire   +1 more source

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