Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have tested an ethanol reagent strip developed at the Addiction Research Foundation of Ontario. Alcohol dehydrogenase and nicotinamide adenine dinucleotide, in the presence of pyrazole, react with ethanol to yield acetaldehyde plus reduced nicotinamide adenine dinucleotide. The latter reduces iodonitrotetrazolium chloride in the presence of diaphorase, generating an intense red color. The rate of color development is proportional to the concentration of ethanol. Color is compared at a specific time against a calibrated color scale ranging from green (negative) to red, representing alcohol concentrations of 0, 25, 50, 100, 200, and 400 mg/dl (0-0.4%; 0-87 mmol/liter). We were able to interpolate the color observed between the calibrated blocks. When tested on urine, serum/plasma, and saliva, ethanol concentration determined by the reagent strip correlates well with ethanol concentration as determined by gas chromatography or by automated enzymatic analysis (r = 0.92-0.98, p less than 0.001; slope 0.83-1.16). The reagent strip was shown to be used appropriately by nonexperienced individuals following a 1-min explanation (reagent strip values, r = 0.92; p less than 0.001, slope = 0.97, versus gas chromatography). The reagent strip does not react with methanol (wood alcohol), isopropanol (rubbing alcohol), and ethylene glycol (antifreeze) often found in accidental poisonings. In 379 clinical samples obtained without exclusion criteria from 12 hospital emergency rooms and a liver clinic, the sensitivity of the reagent strip in detecting ethanol was 98%. Specificity was 99%. The reagent strip was found to have virtually unlimited stability under refrigeration (4 degrees C) and to be stable for 3 to 4 months at room temperature (22-23 degrees C).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Characteristics of a new urine, serum, and saliva alcohol reagent strip. 159 May 43

Silybin dihemisuccinate produces a decrease in the ethanol metabolic rate of rats. This effect is ascribed to an inhibition of the microsomal ethanol oxidizing system (MEOS). Alcohol dehydrogenase activity, catalase activity and NADPH cytochrome c reductase activity are not affected by the flavonoid. It is proposed that the inhibition of MEOS by silybin dihemisuccinate is related to its antioxidant properties, acting as a scavenger of the free radicals involved in ethanol metabolism by this enzymatic system. This observation may have therapeutical implications because microsomal lipid peroxidation induced by hydroxyl free radicals has been related to the etiology of hepatic alcoholic disease.
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PMID:Effect of silybin dihemisuccinate on the ethanol metabolizing systems of the rat liver. 250 94

The genetic control of NADH dehydrogenase-1 (NDH-1) and aromatic alcohol dehydrogenase-2 (AADH-2) was investigated in Triticum aestivum cv. Chinese Spring. Evidence was obtained that NDH-1 is active as a monomer and is encoded by genes located in the p arms of the homoeologous group 4 chromosomes. The NDH-1 gene loci located in 4Ap, 4Bp, and 4Dp were designated Ndh-A1, Ndh-B1, and Ndh-D1, respectively. Aadh-A2 was previously reported to be located in 6Aq; in this study, Aadh-B2 and Aadh-D2 were localized in 6Bq and 6Dq, respectively. Alcohol dehydrogenase-1 is expressed on AADH-2 zymograms; the presence of a contaminating aliphatic alcohol in one or more reagents is suggested as the probable cause of this phenomenon.
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PMID:Genetic control of NADH dehydrogenase-1 and aromatic alcohol dehydrogenase-2 in hexaploid wheat. 332 6

The antifungal antibiotic flavensomycin inhibited the oxidation of amino acids and of glucose by Penicillium oxalicum. The compound inhibited l-amino acid oxidase (EC 1.4.3.2) activity for l-leucine and l-phenylalanine, and also d-amino acid oxidase (EC 1.4.3.3) in the oxidation for dl-alanine. The addition of flavin adenine dinucleotide, which is a cofactor for this enzyme, antagonized the action of the antibiotic. Glucose oxidase (EC 1.1.3.4) was also inhibited. The antibiotic inhibited the reduced nicotinamide adenine dinucleotide (NADH(2)) cytochrome c reductase (EC 1.6.2.1) as well as the much slower nonenzymatic reduction of this cytochrome by the nucleotide. Reduced cytochrome c was also oxidized nonenzymatically by flavensomycin. The antibiotic completely inhibited the action of rabbit muscle lactic dehydrogenase (EC 1.1.1.27) in promoting the reduction of pyruvate by NADH(2) but only slightly affected the reverse reaction. Alcohol dehydrogenase (EC 1.1.1.1) was also similarly inhibited. Flavensomycin prevented the reduction of nicotinamide adenine dinucleotide phosphate by isocitrate in the presence of isocitrate dehydrogenase (EC 1.1.1.42). The hexokinase (EC 2.7.1.1)-catalyzed phosphorylation of glucose, in which the adenosine triphosphate acts as a phosphate donor, was only slightly affected. Flavensomycin also inhibited the action of yeast lactate dehydrogenase (EC 1.1.2.3) on the reduction of cytochrome c. High concentrations of cytochrome c were antagonistic to this reaction. The results point to an interference with enzymatically controlled hydrogen or electron transfer as the mechanism of the antifungal activity of flavensomycin.
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PMID:Flavensomycin, an inhibitor of enzyme reactions involving hydrogen transfer. 438 33

Endosperms from castor beans (Ricinus communis) germinated for 0 to 6 days were exposed to anoxia for 0 to 15 hours. Ethanol, the only alcohol detected by gas chromatography in the tissue, accumulates to a concentration of 15 millimolar during the first 2 to 4 hours of anoxia and subsequently decreases. The absolute amount of ethanol varies from 10 micromoles per 5-day endosperm after 4 hours anoxia to less than 1 micromole in 2-day endosperm after 4 hours. Lactate content is 2 micromoles or less per endosperm. Alcohol dehydrogenase and pyruvate decarboxylase activities, which are localized in cytosolic fractions, are not greatly affected by anoxia. The recoveries of the marker enzymes and protein in endoplasmic reticulum (ER) and mitochondrial fractions decrease during anoxia. After 15 hours, the recovery of NADPH cytochrome c reductase is 15% of that in controls, fumarase is 50%, and catalase is 75%.Glyoxysomes and ER are capable of converting ethanol to acetaldehyde which was measured using the fluorogenic reagent, 5,5-dimethyl-1,3-cyclohexanedione. The glyoxysomal activity is dependent on a hydrogen peroxide-generating substrate and the ER is dependent on NADPH. However, these activities are less than 3% of the alcohol dehydrogenase activity.
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PMID:Anaerobic stress in germinating castor bean, ethanol metabolism, and effects on subcellular organelles. 1666 75