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

Pyrazole has been widely used as an inhibitor of alcohol dehydrogenase both in vivo and in vitro. Very little attention has been paid to the metabolism of this agent and possible biological activity of any metabolites. Several isotopic variants of pyrazole, both stable and radioactive, were used in a study of its metabolic fate by gas chromatography-mass spectrometry. Seven metabolites were structurally identified and included hydroxylated and conjugated derivatives of pyrazole. Two metabolites were conjugated with a pentose, perhaps indicating that pyrazole serves as a substrate in the salvage pathway of purines and pyrimidines forming pyrazole ribosides. The use of d3-pyrazole greatly enhanced structural assignment of the metabolites by revealing the metabolism at or next to a labeled carbon atom.
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PMID:Metabolism of pyrazole. Structure elucidation of urinary metabolites. 1 7

Group N streptococci formed acetaldehyde and ethanol from glucose. As the enzymes aldehyde dehydrogenase, phosphotransacetylase and acetate kinase were present this would enable these organisms to reduce acetyl-CoA to acetaldehyde and convert acetyl-CoA to acetyl phosphate and acetate. A pentose phosphate pathway which converted ribose-5-phosphate to glyceraldehyde-3-phosphate was also present. Acetaldehyde could not be formed via the hexose monophosphate shunt or by direct decarboxylation of pyruvate, as the enzymes phosphoketolase and alpha-carboxylase were absent. Phosphoketolase activity was induced in Streptococcus lactis subsp. diacetylactis after growth on D-xylose. Group N streptococci also contained an NAD-dependent alcohol dehydrogenase which reduced acetaldehyde to ethanol while both NAD- and NADP-dependent alcohol dehydrogenase activities were found in Leuconostoc cremoris.
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PMID:Acetaldehyde: an intermediate in the formation of ethanol from glucose by lactic acid bacteria. 17 70

The mechanism of amphotericin B action was studied with the aid of cytochemical methods providing determination of the activity of the 4 main enzymes characterizing the cell energetics, i. e. succinate dehydrogenase, lactate dehydrogenase, alcohol dehydrogenase and glucose-6-phosphate dehydrogenase inside the cell. With an increase in the concentration of amphotericin B in the medium the activity of all the 4 enzymes decreased, the percentage of the inactive cells being regularly increased. Changes in the fermentative activity of C. albicans as dependent on the incubation time with the antibiotic were studied. Only the respiration activity decreased in 2 hours. As a result of a 4-hour exposure to the polyen in the cells of C. albicans the activity of the lactic acid fermentation, respiration through succinate dehydrogenase and activity of the pentose shunt decreased 1.5--2 times. In 24 hours of incubation the activity of the above decreased 80--90 per cent as compared to the activity of the initial culture.
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PMID:[Effect of amphotericin B on the enzyme system of Candida albicans]. 32 12

The liver cells of 8 rabbits fed for 12 to 16 weeks with a cholesterol diet showed a decrease of RNA and a stronger reactivity for acid phosphatase and beta-glucuronidase. The non-specific esterase showed a weaker reactivity in the cells with a larger amount of cholesterol and a stronger reaction in the cells with a smaller quantity of this substance. Several enzymes such as: diaphorases, those of the pentose shunt and respiratory cycle as well as those related to the metabolism of lipids, proteins and mucopolysaccharides showed a unconspicuous reactivity. The glycogen was found in a lesser amont in 6 out of 8 rabbits but with a higher concentration in 2 of them. The reactivity of UDPG-GT, active phosphorylase, F-1,6-PA, F-1,6-P Ald, LDH and ADH was stronger in the last 2 animals but weaker in the 6 others. In this 8 rabbit group the total phosphorylase and G-6-PA showed respectively always a stronger and a weaker reactivity than their controls. In the liver of 2 cholesterol-fed for 20 weeks rabbits it was observed a centrolobular fibrosis, a smaller amount of RNA and glycogen as well as a global decrease of the enzymatic reactivity.
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PMID:Histochemical reactions of liver cells in cholesterol-fed rabbits. 40 25

The activities of key enzymes that are members of D-glucose metabolic pathways in Schizosaccharomyces pombe undergoing respirative, respirofermentative, and fermentative metabolisms are monitored. The steady-state activities of glycolytic enzymes, except phosphofructokinase, decrease with a reduced efficiency in D-glucose utilization by yeast continuous culture. On the other hand, the enzymic activities of pentose monophosphate pathway reach the maximum when the cell mass production of the cultures is optimum. Enzymes of tricarboxylate cycle exhibit the maximum activities at approximately the washout rate. The steady-state activity of pyruvate dehydrogenase complex increases rapidly when D-glucose is efficiently utilized. By comparison, the activity of pyruvate decarboxylase begins to increase only when ethanol production occurs. Depletion of dissolved oxygen suppresses the activity of pyruvate dehydrogenase complex but facilitates that of pyruvate decarboxylase. Acetate greatly enhances the acetyl CoA synthetase activity. Similarly, ethanol stimulates alcohol dehydrogenase and aldehyde dehydrogenase activities. Evidence for the existence of alcohol dehydrogenase isozymes in the fission yeast is presented.
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PMID:Enzyme activities of D-glucose metabolism in the fission yeast Schizosaccharomyces pombe. 128 48

Efficient utilization of the pentosan fraction of hemicellulose from lignocellulosic feedstocks offers an opportunity to increase the yield and to reduce the cost of producing fuel ethanol. During prehydrolysis (acid hydrolysis or autohydrolysis of hemicellulose), acetic acid is formed as a consequence of the deacetylation of the acetylated moiety of hemicellulose. Recombinant Escherichia coli B (ATCC 11303), carrying the plasmid pLO1297 with pyruvate decarboxylase and alcohol dehydrogenase II genes from Zymomonas mobilis (CP4), converts xylose to ethanol with a product yield that approaches theoretical maximum. Although other pentose-utilizing microorganisms are inhibited by acetic acid, the recombinant E. coli displays a high tolerance for acetic acid. In xylose fermentations with a synthetic medium (Luria broth), where the pH was controlled at 7, neither yield nor productivity was affected by the addition of 10.7 g/L acetic acid. Nutrient-supplemented, hardwood (aspen) hemicellulose hydrolysate (40.7 g/L xylose) was completely fermented to ethanol (16.3 g/L) in 98 h. When the acetic acid concentration was reduced from 5.6 to 0.8 g/L, the fermentation time decreased to 58 h. Overliming, with Ca(OH)2 to pH 10, followed by neutralization to pH 7 with sulfuric acid and removal of insolubles, resulted in a twofold increase in volumetric productivity. The maximum productivity was 0.93 g/L/h. The xylose-to-ethanol conversion efficiency and productivity in Ca(OH)2-treated hardwood prehydrolysate, fortified with only mineral salts, were 94% and 0.26 g/L/h, respectively. The recombinant E. coli exhibits a xylose-to-ethanol conversion efficiency that is superior to that of other pentose-utilizing yeasts currently being investigated for the production of fuel ethanol from lignocellulosic materials.
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PMID:Effect of acetic acid on xylose conversion to ethanol by genetically engineered E. coli. 162 3

1. The response to thermal acclimation of five key rate-limiting enzymes of intermediary metabolism and of six degradative enzymes was measured in tissue extracts of adult Drosophila melanogaster which had been acclimated for 4 days to 15, 25 or 30 degrees C. 2. Three enzymes of intermediary metabolism (HK, alpha-GPDH and CO) showed positive thermal compensation, which is the type of response characteristic of the enzymes involved in energy metabolism in vertebrate ectotherms. 3. The data obtained for CS and G6PDH showed no evidence for increased activity of TCA cycle nor of the pentose phosphate pathway upon cold acclimation in D. melanogaster. 4. Two degradative enzymes, ADH and non-specific esterase, showed inverse thermal compensation which is the type of response characteristic of degradative enzymes in vertebrate ectotherms. 5. In contrast to the situation in vertebrate ectotherms, catalase and the three lysosomal enzymes assayed (APH, acid DNase and acid RNase) displayed positive rather than inverse compensation. 6. The results presented here extend the data on the range of D. melanogaster enzymes which show compensation upon thermal acclimation and on the type of acclimation response which occurs.
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PMID:The effect of acclimation temperature on enzyme activity in Drosophila melanogaster. 165 Dec 3

Efficient utilization of lignocellulosic feedstocks offers an opportunity to reduce the cost of producing fuel ethanol. The fermentation performance characteristics of recombinant Escherichia coli ATCC 11303 carrying the "PET plasmid" (pLOI297) with the lac operon controlling the expression of pyruvate decarboxylase (pdc) and alcohol dehydrogenase II (adhB) genes cloned from Zymomonas mobilis CP4 (Alterthum & Ingram, 1989) were assessed in batch and continuous processes with sugar mixtures designed to mimic process streams from lignocellulosic hydrolysis systems. Growth was pseudoexponential at a rate (generation time) of 1.28 h at pH 6.8 and 1.61 h at pH 6.0. The molar growth yields for glucose and xylose were 17.28 and 7.65 g DW cell/mol, respectively (at pH 6.3 and 30 degrees C), suggesting that the net yield of ATP from xylose metabolism is only 50% compared to glucose. In pH-stat batch fermentations (Luria broth with 6% sugar, pH 6.3), glucose was converted to ethanol 4-6 times faster than xylose, but the glucose conversion rate was much less than can be achieved with comparable cell densities of Zymomonas. Sugar-to-ethanol conversion efficiencies in nutrient-rich, complex LB medium were near theoretical at 98 and 88% for glucose and xylose, respectively. The yield was 10-20% less in a defined-mineral-salts medium. Acetate at a concentration of 0.1M (present in lignocellulosic hydrolysates from thermochemical processing) inhibited glucose utilization (about 50%) much more than xylose, and caused a decrease in product yield of about 30% for both sugars. With phosphate-buffered media (pH 7), glucose was a preferred substrate in mixtures with a ratio of hexose to pentose of 2.3 to 1. Xylose was consumed after glucose, and the product yield was less (0.37 g/g). Under steady-state conditions of continuous culture, the specific productivity ranged from 0.76-1.24 g EtOH/g cell/h, and the maximum volumetric productivity, 2.5 g EtOH/L/h, was achieved with a rich complex LB medium (glucose) at pH 6.0 (30 degrees C) and ethanol at 1.63% (v/v). Growth and fermentation were poor in a buffered-wood (aspen) "hemicellulose hydrolysate" containing 4% xylose and 0.1M acetate with added thiamine and mineral salts.
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PMID:Ethanol production by recombinant Escherichia coli carrying genes from Zymomonas mobilis. 192 64

The activities and isozyme patterns of seven enzymes involved in glycolysis, the malate-aspartate shuttle and the pentose phosphate pathway have been examined in five transplantable murine hepatomas, adult liver and fetal liver. The liver marker enzyme, alcohol dehydrogenase, has also been studied. The developmental expression of the activity and isozyme pattern of these enzymes have been determined. Seven defined loci on six different chromosomes code for these enzymes and isozymes. The tumors express no unique gene product for any of the enzymes examined, but the activities of all the enzymes in the hepatomas are more like fetal liver than adult liver, regardless of whether activities are increased or decreased in hepatomas. The activity of one enzyme is unchanged in hepatomas, and this enzyme has the same activity in fetal and adult liver. The enzyme activities in the five hepatomas vary more than the enzyme activities in liver and fetal liver of the three inbred strains of mice examined.
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PMID:Analysis of genetically defined liver enzymes in transplantable hepatomas and developing liver of the mouse. 629 Sep 57

The spectra and activities of isozymes of hexokinase and alcohol dehydrogenase (enzymes that catalyse glucose and ethanol assimilation), glucose-6-phosphate dehydrogenase (the key enzyme of the pentose phosphate shunt) and malate dehydrogenase (an enzyme of the tricarboxylic acid cycle) were comparatively studied in Pichia pinus haploid (MH4) and autodiploid (D4) strains. Differences in the qualitative composition of the isoenzyme spectra and activities suggest that the intensity and the role of the studied metabolic pathways and cycles differ between the haploid and autodiploid strains of Pichia pinus.
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PMID:[Comparative study of the spectra and activities of isoenzymes in haploid and autodiploid strains of Pichia pinus]. 634 87


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