Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies have usually found that animals with either higher alcohol elimination rates or ADH (alcohol dehydrogenase, EC1.I.I.I) activities have higher voluntary intakes of alcohol than ones with lower elimination rates. This relationship has now been studied in the AA and ANA rat lines genetically developed, respectively, for high and low alcohol consumption. Female AA and ANA rats had their alcohol elimination rate measured before being given a free choice between 10% (v/v) alcohol and water for 3 weeks. The elimination rate was then measured again and liver ADH activity was determined. The alcohol elimination rate was significantly higher in AA than ANA rats before drinking and was increased by alcohol drinking in AA but not ANA rats. ADH activity was similar in both lines and unrelated to either alcohol drinking or elimination rates, suggesting that the enzyme activity is not a rate-limiting factor in the alcohol metabolism of these two lines. The present results support the conclusion that alcohol elimination and alcohol consumption are partially determined by genetics. Furthermore, although alcohol elimination itself probably does not have direct control over drinking, some factor related to the alcohol elimination rate appears to be among the mechanisms influencing the level of alcohol drinking.
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PMID:Alcohol elimination and the regulation of alcohol consumption in AA and ANA rats. 141 14

Aldose reductase ([EC1.1.1.21]: AR) acts on the first step of the polyol metabolic pathway to catalyze the reduction of glucose to sorbitol with NADPH as a coenzyme. Hyperactivity of the pathway in individuals with high blood glucose level is closely related to the onset or progression of diabetic complications. AR inhibitors have therefore been noted as possible pharmacotherapeutic agents for the treatment of diabetic complications. One AR inhibitor has been on the market in Japan, while some potent inhibitors are in clinical trials. Reviewed are the physiological roles of AR, the chemical structures of AR inhibitors, interactions of AR inhibitors with AR using X-ray studies, and the following potencies of AR inhibitors: in vitro activities for AR, in vitro selectivities between AR and aldehyde reductase, their pharmacological effects in vivo, and their effectiveness in clinical trials. Also discussed are directions for the design of future AR inhibitors.
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PMID:Aldose reductase inhibitors. 1216 86

The purpose of the present study was to elucidate the effects of dietary zinc-deficient feeding and its recovery on liver cytosolic alcohol dehydrogenase (ADH; alcohol: NAD(+) oxidoreductase, EC1.1.1.1) activities and plasma zinc levels in rats. The weaned male Sprague Dawley rats were randomly divided into the zinc-deficient diet (ZDF: 1.9 mg zinc/kg diet) group and the control diet (53.5 mg zinc/kg diet) group, and were fed for 4 weeks. In the recovery periods, the rats of two groups were fed with the control diet for 3 weeks. Liver cytosolic protein content per body weight in the zinc-deficiency and its recovery period showed no significant changes between both groups. However, zinc-deficiency decreased significantly liver cytosolic ADH specific activity, total liver cytosolic ADH activity and total liver cytosolic ADH activity/body weight by 50%, 76% and 53%, respectively, as compared with the control diet group. Zinc-deficiency also decreased significantly plasma zinc concentration by 84%, as compared with the control diet group. On the contrary, no significant changes in liver cytosolic ADH specific activity, total liver cytosolic ADH activity and total liver cytosolic ADH activity/body weight in the recovery period were observed between both groups. Plasma zinc concentration in the recovery period was almost recovered to the control level. These results suggest that rat liver cytosolic ADH activity was clearly related to dietary zinc intake levels.
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PMID:Dietary zinc-deficiency and its recovery responses in rat liver cytosolic alcohol dehydrogenase activities. 2129 47

A comparative proteomic approach, using two dimensional gel electrophoresis and mass spectrometry, has been developed to compare and elucidate the differences among the cellular proteomes of four closely related isogenic O/C, SIN, N/R and T, B. clausii strains during both exponential and stationary phases of growth. Image analysis of the electropherograms reveals a high degree of concordance among the four proteomes, some proteins result, however, differently expressed. The proteins spots exhibiting high different expression level were identified, by mass-spectrometry analysis, as alcohol dehydrogenase (ADHA, EC1.2.1.3; ABC0046 isoform) aldehyde dehydrogenase (DHAS, EC 1.2.1.3; ABC0047 isoform) and flagellin-protein of B. clausii KSM-k16. The different expression levels of the two dehydrogenases were confirmed by quantitative RT-PCR and dehydrogenases enzymatic activity. The different patterns of protein expression can be considered as cell proteome signatures of the different strains.
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PMID:Comparative proteomic analysis of four Bacillus clausii strains: proteomic expression signature distinguishes protein profile of the strains. 2181 Apr 90

The use of oxidoreductases (EC1) in non-conventional reaction media has been increasingly explored. In particular, deep eutectic solvents (DESs) have emerged as a novel class of solvents. Herein, an in-depth study of bioreduction with an alcohol dehydrogenase (ADH) in the DES glyceline is presented. The activity and stability of ADH in mixtures of glyceline/water with varying water contents were measured. Furthermore, the thermodynamic water activity and viscosity of mixtures of glyceline/water have been determined. For a better understanding of the observations, molecular dynamics simulations were performed to quantify the molecular flexibility, hydration layer, and intraprotein hydrogen bonds of ADH. The behavior of the enzyme in DESs follows the classic dependence of water activity (aW ) in non-conventional media. At low aW values (<0.2), ADH does not show any activity; at higher aW values, the activity was still lower than that in pure water due to the high viscosities of the DES. These findings could be further explained by increased enzyme flexibility with increasing water content.
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PMID:Modeling Alcohol Dehydrogenase Catalysis in Deep Eutectic Solvent/Water Mixtures. 3160 52