Results 171 to 180 of about 917,246 (220)

Enantioselective Synthesis of Both Enantiomers of Various Propargylic Alcohols by Use of Two Oxidoreductases

open access: closedEuropean Journal of Organic Chemistry, 2001
The oxidoreductases Lactobacillus brevis alcohol dehydrogenase (LBADH) and Candida parapsilosis carbonyl reductase (CPCR) are suitable catalysts for the reduction of ketones to afford enantiopure sec. alcohols. A broad variety of alkynones (1, 3, and 5) are accepted as substrates and the corresponding propargylic alcohols (2, 4, and 6) are obtained in ...
Thomas Schubert   +3 more
openalex   +3 more sources

Substrate specificity of citrus alcohol: NAD oxidoreductase

open access: closedJournal of Agricultural and Food Chemistry, 1971
J.H. Bruemmer, BONGWOO ROE
openalex   +3 more sources

Coupled oxidoreductase activity of horse liver alcohol dehydrogenase

open access: closedArchives of Biochemistry and Biophysics, 1972
Abstract Two assay procedures were used to study ethanol oxidation by crystalline horse liver alcohol dehydrogenase: (A) Acetaldehyde formed by ethanol oxidation (with and without lactaldehyde) was distilled into a semicarbazide solution and the absorbance of the acetaldehyde semicarbazone formed was measured at 224 nm.
Charles L. Woodley, Naba K. Gupta
openalex   +4 more sources

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

open access: closedBiochemical and Biophysical Research Communications, 2011
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
openalex   +4 more sources

Cytosolic NAD(P)H:(Quinone‐acceptor)oxidoreductase in human normal and tumor tissue: Effects of cigarette smoking and alcohol

open access: closedInternational Journal of Cancer, 1990
AbstractNAD(P)H:(quinone‐acceptor)oxidoreductase (QAO), previously known as DT‐diaphorase, catalyzes the reduction of qui‐nones to hydroquinones. Enhanced activity of the enzyme has been suggested to protect cells against the cellular toxicity and carcinogenicity of quinones, but may activate some cyto‐toxic anti‐tumor quinones. Cytosolic levels of QAO,
John J. Schlager, Garth Powis
openalex   +4 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

Degradation of polystyrene plastics by alkane monooxygenase and alcohol dehydrogenase

Global NEST Journal
The consumption of plastic products has led to the generation of large amounts of plastic waste, which is persistent and difficult to degrade. Polystyrene (PS) is one of the six most important plastics in the world and is difficult to degrade in the ...

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

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.
Karey L. Holland   +2 more
openaire   +2 more sources

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