Results 191 to 200 of about 16,608 (226)
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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.
P W, van Ophem, J A, Duine
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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

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.
A. Geerlof   +3 more
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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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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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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.
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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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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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Quinoprotein oxidoreductases for the oxidation of alcohols, sugars and amines

1994
Quinoproteins 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
openaire   +1 more source

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