Results 221 to 230 of about 940,087 (264)

Amperometric Methods for Oxidoreductase Enzymes Based on Liquid Chromatography with Electrochemical Detection. Alcohol Dehydrogenase

Journal of Liquid Chromatography, 1979
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 ...
Gregory C. Davis, Karey Holland, Peter T. Kissinger   +2 more
semanticscholar   +4 more sources

Role of epoxide hydrolase, NAD(P)H:quinone oxidoreductase, cytochrome P450 2E1 or alcohol dehydrogenase genotypes in susceptibility to colorectal cancer

Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis, 2005
Colorectal cancer (CRC) is one of the most common forms of cancer in Western countries. CRC has been associated with genetic and lifestyle factors. Individual susceptibility to CRC may be due partly to variations in detoxification capacity in the gastrointestinal tract.
Elise M.J. van der Logt, Saskia M. Bergevoet, Hennie M.J. Roelofs, René H. M. te Morsche, Yvo van Dijk, Theo Wobbes, Fokko M. Nagengast, Wilbert H.M. Peters   +7 more
semanticscholar   +6 more sources

Sugar oxidoreductases and veratryl alcohol oxidase as related to lignin degradation

Journal of Biotechnology, 1997
Properties of cellobiose:quinone oxidoreductase (CBQ), cellobiose dehydrogenase (CDH), glyoxal oxidase (GLOX), glucose oxidases and veratryl alcohol oxidase (VAO) are reviewed. There is strong evidence that CDH reduces quinones, phenoxy and cation radicals.
Paul Ander, Liberato Marzullo
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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
semanticscholar   +3 more sources

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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Nicotinoprotein Alcohol/Aldehyde Oxidoreductases

, 1996
Enzymes with tightly bound NAD(P), acting as cofactor, have been described in the past. Well known examples include UDP-galactose 4-epimerase from E. coli (Wilson and Hogness, 1964) and lactate-oxaloacetate transhydrogenase from V. alcalescens (Allen, 1966).
Sander R. Piersma, Simon de Vries, Johannis A. Duine   +2 more
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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, J. A. Jongejan, S. de Vries   +2 more
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Aryl-alcohol oxidase protein sequence: a comparison with glucose oxidase and other FAD oxidoreductases

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
Aryl-alcohol oxidase (AAO), an FAD-dependent enzyme involved in lignin degradation, has been cloned from Pleurotus eryngii. The AAO protein is composed of 593 amino acids, 27 of which form a signal peptide. It shows 33% sequence identity with glucose oxidase from Aspergillus niger and lower homology with other oxidoreductases.
Elisa Varela, Marı́a Jesús Martı́nez, Ángel T. Martı́nez   +2 more
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Enantioselective Synthesis of Both Enantiomers of Various Propargylic Alcohols by Use of Two Oxidoreductases

European 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, Werner Hummel, Maria‐Regina Kula, Michael Müller   +3 more
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Coupled oxidoreductase activity of horse liver alcohol dehydrogenase

Archives 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
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