Results 241 to 250 of about 873,715 (296)
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An alcohol dehydrogenase ribozyme
Nature Structural & Molecular Biology, 2003We report an RNA molecule that exhibits activity analogous to that of alcohol dehydrogenase (ADH). Directed in vitro evolution was used to enrich nicotinamide adenine dinucleotide (NAD+)-dependent redox-active RNAs from a combinatorial pool. The most active ribozyme in the population forms a compact pseudoknotted structure and oxidizes an alcohol seven
Shinya, Tsukiji +2 more
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Alcohol and polyol dehydrogenases
Pharmacology Biochemistry and Behavior, 1983"Long" and "short" alcohol dehydrogenases with different structures and catalytic mechanisms exist and the same sub-grouping appears to apply to polyol dehydrogenases. Mammalian liver sorbitol dehydrogenase is clearly related to "long" alcohol dehydrogenases and has structural properties intermediate between those of mammalian and yeast alcohol ...
H, Jörnvall, M, Carlquist, J, Jeffery
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Secondary alcohol dehydrogenase
Biochimica et Biophysica Acta, 1962Abstract Secondary alcohol dehydrogenase, purified from a species of Pseudomonas , is specific for the DPN-linked oxidation of secondary alcohols and the DPNH-linked reduction of ketones; substrates include isopropanol, cyclohexanol and acetone.
W B, JAKOBY, J, FREDERICKS
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ALCOHOL AND ALDEHYDE DEHYDROGENASE*
Alcohol and Alcoholism, 1990The enzymes mainly responsible for ethanol degradation in humans are liver alcohol dehydrogenases (ADH) and aldehyde dehydrogenases (ALDH). Polymorphisms occur in both enzymes, with marked differences in the steady-state kinetic constants. The Km-values for ethanol of ADH isoenzymes relevant for alcohol degradation range from 49 microM to 36 microM ...
T, Ehrig, W F, Bosron, T K, Li
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Science, 1968
Significant alcohol dehydrogenase activity has been demonstrated in the soluble fraction of rat brain and is very similar to the liver enzyme in kinetic properties and responses to inhibitors. A cerebral mechanism that oxidizes ethanol may play a significant role in local adjustments during exposure to ethanol and in the pathogenesis of the neural ...
N H, Raskin, L, Sokoloff
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Significant alcohol dehydrogenase activity has been demonstrated in the soluble fraction of rat brain and is very similar to the liver enzyme in kinetic properties and responses to inhibitors. A cerebral mechanism that oxidizes ethanol may play a significant role in local adjustments during exposure to ethanol and in the pathogenesis of the neural ...
N H, Raskin, L, Sokoloff
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Alcohol and aldehyde dehydrogenase polymorphisms and alcoholism
Behavior Genetics, 1993The alcohol-flush reaction occurs in Asians who inherit the mutant ALDH2*2 allele that produces an inactive aldehyde dehydrogenase enzyme. In these individuals, high blood acetaldehyde levels are believed to be the cause of the unpleasant symptoms that follow drinking.
H R, Thomasson +3 more
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Induction of Alcohol Dehydrogenase in the Rat
Nature, 1969ETHANOL is metabolized to acetaldehyde by a zinc containing enzyme, alcohol dehydrogenase (ADH)1–4. This is a rate limiting step and is dependent on the presence of nicotine adenine dinucleotide (NAD) which acts as a hydrogen acceptor5,6. Over 90 per cent of the alcohol ingested is oxidized and it is currently assumed that this occurs entirely in the ...
S P, Mistilis, A, Birchall
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The Alcohol Dehydrogenase System
1995Alcohol dehydrogenases of different types are common enzymes in nature. Two of these families, the medium-chain dehydrogenase/reductase family, MDR, and the shortchain dehydrogenase/reductase family, SDR, are well studied and known since long, but have experienced a recent “explosion” of new knowledge, extension and importance.
H, Jörnvall +4 more
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Chemico-Biological Interactions, 2017
Close to 80 years of research have brought MDR alcohol dehydrogenases (ADHs) from unknown molecular concepts to molecules known in exact detail regarding structural, functional and evolutionary properties. They can be traced backwards in at least six stages of development, to essentially the origin of cellular life, and have been monitored in a long ...
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Close to 80 years of research have brought MDR alcohol dehydrogenases (ADHs) from unknown molecular concepts to molecules known in exact detail regarding structural, functional and evolutionary properties. They can be traced backwards in at least six stages of development, to essentially the origin of cellular life, and have been monitored in a long ...
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Isozymes of Alcohol Dehydrogenases
1980Thirty amino acid substitutions are known in eight sets of isozymes or mutants of alcohol dehydrogenases. The replacements are at different positions in the subunits and affect many regions of the protein chains, which is consistent with the variability in properties of isozyme pairs.
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