Results 311 to 320 of about 212,542 (335)
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Phytochemistry, 1976
Abstract Alcohol dehydrogenase was prepared from germinating soybean seeds. Specific activity was increased from 511 to 31316 units. The coenzyme is NAD with a K m of 10 −4 M. Allyl alcohol is oxidized faster than ethanol; with the latter substrate, the K m is 1.3 × 10 −2 M, and the pH optimum 8.7.
Eva Perglerová, Sylva Leblová
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Abstract Alcohol dehydrogenase was prepared from germinating soybean seeds. Specific activity was increased from 511 to 31316 units. The coenzyme is NAD with a K m of 10 −4 M. Allyl alcohol is oxidized faster than ethanol; with the latter substrate, the K m is 1.3 × 10 −2 M, and the pH optimum 8.7.
Eva Perglerová, Sylva Leblová
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Alcohol and aldehyde dehydrogenase polymorphisms and the risk for alcoholism
American Journal of Psychiatry, 1995The authors studied a large number of Japanese alcoholic patients and comparison subjects to establish the genotype frequencies of alcohol dehydrogenase-2 (ADH2) and mitochondrial aldehyde dehydrogenase (ALDH2) and to quantify the relative risk for alcoholism from the results.The subjects were 655 alcoholic patients and 461 comparison subjects.
Motoi Hayashida +4 more
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The alcohol dehydrogenase system
1994Alcohol dehydrogenases constitute a complex system of enzymes, classes, isozymes, and allelic variants. The zinc containing, well-known liver enzyme is a class I medium-chain alcohol dehydrogenase. Other classes of this family include the class II protein, the glutathione-dependent formaldehyde dehydrogenase (the class III enzyme), the stomach ...
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1975
Publisher Summary This chapter describes the advances with an emphasis on the structures of the alcohol dehydrogenases and the relationship between structure and function. Yeast and mammalian alcohol dehydrogenase differ in substrate specificity and rate of catalytic activity.
Bo Furugren +3 more
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Publisher Summary This chapter describes the advances with an emphasis on the structures of the alcohol dehydrogenases and the relationship between structure and function. Yeast and mammalian alcohol dehydrogenase differ in substrate specificity and rate of catalytic activity.
Bo Furugren +3 more
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1977
Publisher Summary NAD is the coenzyme of alcohol dehydrogenase. It serves in the reversible enzymic reaction as an acceptor of the hydrogen from the substrate and is converted to NADH. This occurs in a ternary complex of enzyme, pyridine nucleotide, and substrate, in which coenzyme and substrate interact closely with amino acid residues of the enzyme,
Christoph Woenckhaus, Reinhard Jeck
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Publisher Summary NAD is the coenzyme of alcohol dehydrogenase. It serves in the reversible enzymic reaction as an acceptor of the hydrogen from the substrate and is converted to NADH. This occurs in a ternary complex of enzyme, pyridine nucleotide, and substrate, in which coenzyme and substrate interact closely with amino acid residues of the enzyme,
Christoph Woenckhaus, Reinhard Jeck
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Alcohol dehydrogenases and aldehyde dehydrogenases
Biochemical Society Transactions, 1988Hans Jörnvall +6 more
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Amphibian Alcohol Dehydrogenase
1999Alcohol dehydrogenase (ADH) catalyses the reversible interconversion of a variety of alcohols and their corresponding aldehydes and ketones, and is widely distributed in organisms. It has been detected in all animals, in plants, and eukaryotic and prokaryotic microorganisms.
Jaume Farrés +5 more
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ALCOHOL DEHYDROGENASE IN ALCOHOLISM
The Lancet, 1967E. Radaeli, A. Albertini, E. Bonera
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Alcohol Dehydrogenase Variability
1996We have studied many alcohol dehydrogenases and related enzymes with the aim of defining functional properties, structural patterns, and evolutionary relationships. From this, four major conclusions have been drawn: The enzymes are clearly multiple and represent different protein families.
Hans Jörnvall +5 more
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