Results 241 to 250 of about 940,087 (264)
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The emerging role of aldehyde:ferredoxin oxidoreductases in microbially-catalyzed alcohol production

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.
Laura Sofie Nissen, Mirko Basen
openaire   +3 more sources

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
openaire   +3 more sources

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, Ehud Keinan, J.G. Zeikus
openaire   +2 more sources

Characterization of the Rhodococcus sp. NI86/21 gene encoding alcohol: N,N′-dimethyl-4-nitrosoaniline oxidoreductase inducible by atrazine and thiocarbamate herbicides

open access: closedArchives of Microbiology, 1995
István Nagy   +7 more
openalex   +2 more sources

Computational Insights into Enzyme‐Substrate Binding Interplay Exhibit Variable Binding Attributes: A Framework for Implementing Oxidoreductase‐Based Applications

ChemistrySelect
Laccase (LAC) is a potent multicopper oxidase that relies on O2 for its catalytic activity. LAC has been affirmed as an environmentally friendly biocatalyst that often catalyzes a wide array of phenolic substrates.
Anil Kumar Singh   +7 more
semanticscholar   +1 more source

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 ...
Emmanuel Scalais   +4 more
openaire   +3 more sources

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
openaire   +5 more sources

A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including zeta-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and other proteins.

European Journal of Biochemistry, 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 ...
B. Persson, J. Zigler, Hans Jörnvall
semanticscholar   +1 more source

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