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Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile [PDF]
Catalysts, 2020 Alcohol dehydrogenases catalyse the conversion of a large variety of ketone substrates to the corresponding chiral products. Due to their high regio- and stereospecificity, they are key components in a wide range of industrial applications. A novel alcohol dehydrogenase from Comamonas testosteroni (CtADH) was identified in silico, recombinantly ...
Daniel Bakonyi +2 more
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Microbial Alcohol, Aldehyde and Formate Ester Oxidoreductases
1993Formation 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.
P W, van Ophem, J A, Duine
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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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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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Quinoprotein oxidoreductases for the oxidation of alcohols, sugars and amines
1994Quinoproteins are enzymes containing a quinone cofactor, that is the non-covalently bound PQQ or the protein-chain-integrated TPQ or TTQ. Quinoprotein dehydrogenases play a role in non-phosphorylative degradation of sugars, alcohols, aldehydes, ketones, and amines by Gram-negative bacteria, providing useful energy to the organism by their capacity to ...
J. A. Duine, J. A. Jongejan, S. de Vries
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Potential applications of an alcohol-aldehyde/ketone oxidoreductase from thermophilic bacteria
Enzyme and Microbial Technology, 1981Practical 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
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Alcohol dehydrogenase (alcohol: NAD oxidoreductase) from the pea seedling
Phytochemistry, 1966Abstract 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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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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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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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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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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Alcohol: NAD Oxidoreductase (E. C. 1.1.1.1.) from Peas
Journal of Food Science, 1968SUMMARY– 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.
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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.
A, Nabi, P 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.
A, Nabi, P J, Worsfold
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