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)

1) A lysosomal protease, a new cathepsin that inactivates glucose-6-phosphate dehydrogenase [EC 1.1.1.49] and some other enzymes and differs from cathepsin B [EC 3.4.22.1] was purified about 2,200-fold from crude extracts of rat liver by cell-fractionation, freezing and thawing, acetone treatment, gel filtration, and DEAE Sephadex and CM-Sephadex column chromatographies. 2) The new cathepsin was markedly activated by the thiol-reagent, 2-mercaptoethanol and inhibited by monoiodoacetate. 3) The molecular weight of the new cathepsin was found by Sephadex G-75 column chromatography to be 22,000, which is smaller than that of cathepsin B. 4) The optimum pH of the enzyme for inactivation of glucose-6-phosphate dehydrogenase was pH 5.0--5.5. The enzyme was unstable in alkali and on heat treatment. 5) The rates of inactivation of glucose-6-phosphate dehydrogenase, apo-ornithine aminotransferase [EC 2.6.1.13], apo-tyrosine aminotransferase [EC 2.6.1.5], apo-cystathionase [EC 4.4.1.1], glucokinase [EC 2.7.1.2], glyceraldehyde-3-phosphate dehydrogenase [EC 1.2.1.12], and malate dehydrogenase [EC 1.1.1.37] by the new cathepsin were higher than those by cathepsin B. However aldolase [EC 4.1.2.13] was inactivated more rapidly by cathepsin B than by the new cathepsin. Lactate dehydrogenase [EC 1.1.1.27], glutamate dehydrogenase [EC 1.4.1.2] and alcohol dehydrogenase [EC 1.1.1.1] were not inactivated by either cathepsin. Unlike cathepsin B, the new cathepsin scarcely hydrolyzes N-substituted derivatives of arginine.
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PMID:Purification and properties of a new cathepsin from rat liver. 3 59

The levels of several enzymes have been studied during sporulation of Saccharomyces cerevisia. The specific activities of ribonuclease and aminopeptidase I raised several-fold after transfer of the cells to sporulation medium, whereas the specific activities of phosphofructokinase, glucose-6-phosphate dehydrogenase, tryptophan synthase and pyruvate decarboxylase were not significantly altered. The specific activities of NAD-dependent glutamate dehydrogenase, isocitrate lyase, malate dehydrogenase and fructose bisphosphatase all decreased from the onset of sporulation. The inactivation of these latter enzymes was inhibited by cycloheximide and by inhibitors of energy metabolism. Hexokinase, alcohol dehydrogenase and glutamate oxaloacetate transaminase were partially lost from the cells during the period of ascus maturation. None of the enzyme changes observed proved to be 'sporulation-specific' in that it occurred exclusively in sporulating diploid yeast cells. Therefore it is postulated that the meiotic events and the metabolic changes required for ascospore formation are under separate genetic control in this organism. During sporulation, the cellular content of cytochromes b, c, and aa3 was reduced to 20% or less of that present in vegetative derepressed cells. Since the relative percentage of total to cycloheximide-insensitive mitochondrial protein synthesis was not significantly altered throughout sporulation, and the pattern of mitochondrially synthesized polypeptides was rather similar both in vegetative and in sporulating cells, it appeared that not only degradation but also synthesis and therefore turnover of the mitochondrially coded polypeptides of cytochromes b and aa3 took place during sporulation. The activity ratio of cytochrome c oxidase to F1-ATPase in submitochondrial particles isolated from vegetative cells and from purified asci was almost identical. This indicates that the loss of membrane-bound mitochondrial cytochromes during sporulation is probably due to a nonselective degradation of inner mitochondrial membrane proteins.
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PMID:Protein degradation during yeast sporulation. Enzyme and cytochrome patterns. 18 44

Interaction of several enzymes (pyruvate kinase, myokinase, creatine kinase, aldolase, malate dehydrogenase, lactate dehydrogenase, alcohol dehydrogenase and glucose-6-phosphate dehydrogenase) and other proteins (bovine serum albumin and ovalbumin) with Blue Dextran was studied by means of affinity electrophoresis in polyacrylamide gels. A decrease of electrophoretic mobility of enzymes in affinity gels was dependent on Blue Dextran concentration and in some cases, dissociation constants of the protein-immobilized dye complexes could be calculated. Affinity electrophoresis in the presence of Blue Dextran reveals in some cases additional bands of isoenzymes, as compared with the control gels (without Blue Dextran).
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PMID:Affinity electrophoresis of proteins interacting with Blue dextran. 20 48

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 denaturation of eight purified yeast enzymes, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, alcohol dehydrogenase, beta-fructosidase, hexokinase and glucose-6-phosphate isomerase, promoted under controlled conditions by the free fatty acids myristic and oleic, is selective. Glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate:NADP+ 1 oxidoreductase, EC 1.1.1.49) is extremely sensitive to destabilization and was studied in greater detail. Results show that chain length and degree of unsaturation of fatty acids are important to their destabilizing effect, and that ligands of the enzyme can afford protection. The denaturation process results in more than one altered form. These results can be viewed in the perspective of the possibility that amphipathic substances, and in particular free fatty acids, may play a role for enzyme degradation in vivo, by initiating steps of selective denaturation.
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PMID:Selective denaturation of several yeast enzymes by free fatty acids. 35 87

Dehydrogenase activity of the tissue form cells of C. albicans during the infection process in albino mice with and without amphotericin B treatment was studied. The strength of the metabolic reactions resulting in accumulation of ATP was evident from the activity of 4 main enzymes, i.e. succinate dehydrogenase, lactate dehydrogenase, alcohol dehydrogenase and glucose-6-phosphate dehydrogenase. The enzymatic activity was determined by the tetrasol method based on formation of diphormazan. Investigation of the fungal cells 10 minutes after the infection showed that preliminary intravenous or intraperitoneal administration of amphotericin B did not change the activity of the tissue forms. The cytochemical characteristics of the fungal cells remained the same as that in the untreated animals. Six hours after infection of the animals treated with amphotericin B administered intravenously the fungus vegetation decreased from 52 to 38 per cent, while in the animals treated with amphotericin B administered intraperitoneally it was suppressed completely. Simultaneously the energy metabolism was also suppressed, the activity of alcohol dehydrogenase being suppressed most significantly. The activity of this enzyme in the cells of C. albicans isolated from the animals treated with the antibiotic administered intraperitoneally was 14 times lower than that in the cells of the culture isolated from the control animals.
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PMID:[Effect of amphotericin B on the energy metabolism of tissue forms of Candida albicans]. 38 38

The activity and electrophoretic spectrum of glucose-6-phosphate dehydrogenase, alcohol dehydrogenase, and malate dehydrogenase in Saccharomyces cerevisiae 14 depended on the conditions of cultivation, i. e. the sources of carbon and their concentration, the content of nitrogen, and aeration of the medium. A heterogeneous tris-buffer protein fraction was isolated after disintegration of the cells; the dehydrogenases were represented by several molecular forms whose number, electrophoretic mobility, and activity depended on the conditions of cultivation.
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PMID:[Effect of cultivation conditions on the electrophoretic spectrum of various dehydrogenases in Saccharomyces cerevisiae]. 76 85

The activities of twelve enzymes were measured in crude extracts from cells of Escherichia coli K-10 grown aerobically or anaerobically in a defined medium in the presence or absence of nitrate. The activities of isocitrate dehydrogenase, aconitate hydratase, 2-oxoglutarate dehydrogenase, malate dehydrogenase, malic enzyme, and D-lactate dehydrogenase (NAD+-independent) were found to be higher in cells grown in nitrate respiration than in those in fermentation, but lower than in those in respiration. This finding may explain the incomplete oxidation in nitrate respiration and, on the other hand, suggests the operation of the tricarboxylic acid even under these conditions. The activities of succinate dehydrogenase and alcohol dehydrogenase in relation to the formation of fermentation product were as high in cells grown in fermentation as in those in respiration and were low in those in nitrate respiration. However, that ratio of the activities in the latter case to the activities in respiration was the same as the ratio for most enzymes in the tricarboxylic acid cycle. The level of lactate dehydrogenase (NAD+-dependent) was not affected by nitrate respiration but its activity in the extract was inhibited by nitrate and nitrite. The absence of lactate in the anaerobic culture with nitrate may be due to this inhibition as well as NADH oxidation by nitrate. Levels of glucose-6-phosphate dehydrogenase and glutamate dehydrogenase were not altered by the growth conditions and that of pyruvate dehydrogenase was low only in cells grown in fermentation.
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PMID:Effect of nitrate reduction on the enzyme levels in carbon metabolism in Escherichia coli. 77 52

Vestigial wing and wild type populations of Drosophila melanogaster were exposed to 5%, 20%, and 60% oxygen at normal atmospheric pressure. Adult mortality rates, larval production, and allele frequency changes in four gene-enzymes were examined in the populations. All flies in 60% oxygen survived as well as controls until day 20 and then died out within the next 10 to 12 d. In 5% oxygen, vestigial wing flies had mortality rates greater than the 20% controls initially, but the rate eventually approached that of the controls. Wild type flies in 5% oxygen survived as well as controls. Larval production and rate of eclosure in 60% oxygen were similar to controls, but reduced in 5% oxygen. Allele frequency shifts to 6-phosphogluconate dehydrogenase and phosphoglucomutase were observed in 5% oxygen, and a shift of alpha-glycerophosphate dehydrogenase allele frequencies occurred in 60% oxygen. There was no evidence of in vivo inactivation of ADH, 6-PGD, alpha-GPD or PGM in 60% oxygen.
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PMID:Survivorship and gene frequencies of Drosophila melanogaster populations in abnormal oxygen atmospheres. 81 44

Thermophilic bacilli, contrary to mesophilic, grow equally well under aerobic and anaerobic conditions. This may be due to the presence of more active anaerobic dehydrogenases in thermophilic organisms. The activity of glucose-6-phosphate dehydrogenase and alcohol dehydrogenase, and the content of ATP, increased in the cells of thermophilic Bac. stearothermophilus 159 and mesophilic Bac. megaterium M strains growing at temperatures close to maximal. The activity of glutamate dehydrogenase under these conditions was inhibited.
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PMID:[The physiology of thermophilic and mesophilic bacilli during development at optimal and submaximal temperatures]. 81 61


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