Results 161 to 170 of about 917,246 (220)
, 1994 The protein super-family of medium-chain alcohol dehydrogenases (and glutathione-dependent formaldehyde dehydrogenase), polyol dehydrogenases, threonine dehydrogenase, archaeon glucose dehydrogenase, and eye lens reductase-active zeta-crystallins also ...
Bengt Persson +2 more
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Journal of Biotechnology, 2019
The development of a bio-refinery industry based on liquid fuels is presumably key to successful replacement of fossil fuels and a reduction of carbon dioxide (CO2) emissions. Ethanol and longer-chain alcohols are supposed to play a key role since they are relatively easy to produce, using microorganisms as whole-cell biocatalysts.
L. Nissen, M. Basen
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The development of a bio-refinery industry based on liquid fuels is presumably key to successful replacement of fossil fuels and a reduction of carbon dioxide (CO2) emissions. Ethanol and longer-chain alcohols are supposed to play a key role since they are relatively easy to produce, using microorganisms as whole-cell biocatalysts.
L. Nissen, M. Basen
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Microbial alcohol, aldehyde and formate ester oxidoreductases.
Advances in Experimental Medicine and Biology, 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. Ophem, J. Duine
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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 ...
Johannis A. Duine +2 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., trans‐2‐hexen‐1‐01, under the conditions used.
Caj Eriksson
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Microbial alcohol dehydrogenases: recent developments and applications in asymmetric synthesis.
Organic and biomolecular chemistry, 2023Alcohol 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
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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.
Yonezo Suzuki
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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 ...
Karen J. Edwards +5 more
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Engineering in Life Sciences, 2006 AbstractBiocatalytic processes are useful methods for the production of chiral intermediates. As an example, alcohol dehydrogenases are applied for the production of chiral alcohols by asymmetric reduction of prochiral ketones. From this class of enzymes alcohol dehydrogenase from Lactobacillus brevis will be described with respect to its industrial ...
Thomas Daußmann +2 more
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