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)

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

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

The polymorphism observed among the enzymes involved in the respiratory metabolism (lactate dehydrogenase, malate dehydrogenase, phosphoglucomutase, phosphohexoseisomerase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase fructose 1-6 diphosphate dehydrogenase) is less important than that of the enzymes physiologically less essential, such as the various esterases, the alkaline phosphatase, the alcohol dehydrogenase, and of the non-enzymatic proteins (ovalbumin, ovoglobulins, ovomucoid, conalbumin, transferrin, etc.).
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PMID:[Biochemical polymorphism of Japanese quail (Coturnix coturnix japonica): comparison of functionally different proteins (author's transl)]. 114 Mar 13

Electrophoretic mobilities in polyacrylamide gel of five dehydrogenases: NADP-dependent malate dehydrogenase (NADP-MDH), 6-phosphogluconate dehydrogenase (6PGD), alcohol dehydrogenase (ADH), glucose-6-phosphate dehydrogenase (G6PD) and glutamate dehydrogenase (GDH) were investigated in a series of mouse X Chinese hamster somatic cell hybrids. Seven hybrid lines with different ratio of chromosome sets of hamster and mouse: 1:1, 2:1, 3:1 and 1:2 respectively were studied. NADP-MDH and 6PGD of both parental species and intermediate hybrid bands were present in all hybrids except two lines. These lines had only hamster MDH due to the elimination of mouse chromosomes. A correlation was found between the gene dose and the intensity of the expression of the MDH bands. The mouse type ADH was detected in all hybrids. The hamster ADH was found in one of the hybrid lines that lost all mouse chromosomes during cultivation. It is suggested that hamster ADH activity was suppressed in hybrids by the mouse genome. The species origin of GDH and G6PD could not be established due to similarity of electrophoretic mobilities of respective enzymes in parental cells.
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PMID:[Characteristics of somatic cell hybrids (mouse X Chinese hamster) with different ratios of parental species chromosome sets. IV. Electrophoretic analysis of several enzymes of the dehydrogenase class]. 123 30

Electrophoretic mobilities in polyacrylamide gel of five dehydrogenases: NADP-dependent malate dehydrogenase (NADP-MDH), 6-phosphogluconate dehydrogenase (6PGD), alcohol dehydrogenase (ADH), glucose-6-phosphate dehydrogenase (G6PD) and glutamate dehydrogenase (GDH) were investigated in a series of mouse X Chinese hamster somatic cell hybrids. Seven hybrid lines with different ratio of chromosome sets of hamster and mouse: 1 : 1, 2 : 1, 3 : 1 and 1 : 2 respectively were studied. NADP-MDH and 6PGD of both parental species and intermediate hybrid hands were present in all hybrids except two lines. These lines had only hamster MDH due to the elimination of mouse chromosomes. A correlation was found between the gene dose and the intensity of the expression of the MDH bands. The mouse type ADH was detected in all hybrids. The hamster ADH was found in one of the hybrid lines that lost all mouse chromosomes during cultivation. It is suggested that hamster ADH activity was suppressed in hybrids by the mouse genome. The species origin of GDH and G6PD could not be established due to similarity of electrophoretic mobilities of respective enzymes in parenteral cells.
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PMID:[Characteristics of somatic cell hybrids (mouse X Chinese hamster) with ratios of chromosome sets different from the parent species. IV. An electrophoretic analysis of several enzymes of the dehydrogenase class]. 124 45

The expression of selected X-linked and autosomal genes was examined in metafemales (3X:2A) compared to diploid sisters. Three enzyme activities (glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, beta-hydroxyacid dehydrogenase) encoded by X-linked genes are not significantly different in the two classes of flies. In contrast, three autosomally encoded enzyme activities (alcohol dehydrogenase, alpha-glycerophosphate dehydrogenase, isocitrate dehydrogenase) are reduced in metafemales. Protein and DNA comparisons between metafemales and diploid sisters show a lowered level of total protein whereas the total DNA measurements are similar. Thus, the total cell number in metafemales is basically unchanged but gene expression is reduced. Phenotypic analysis of three autosomal loci, glass (gl), purple (pr) and pink-peach (pp), show that all three have lowered expression in metafemales while the X-linked loci, white-apricot (wa) and Bar (B), are dosage compensated. Quantitative dot blot analysis of messenger RNA levels of the second chromosomal locus, alcohol dehydrogenase (Adh), and the X chromosomal locus, rudimentary (r), show that Adh has reduced expression and r is partially compensated per total RNA in metafemales. It is proposed that the increased dosage of the X chromosome inversely affects both the X and autosomal gene expression but the simultaneous increased dosage of the structural genes on the X results in dosage compensation. The reduced levels of expression of autosomal genes could contribute to the great inviability of metafemales.
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PMID:Gene expression in adult metafemales of Drosophila melanogaster. 250 26

Some enzymatic activities of the glycolytic and hexose monophosphate pathways of Candida parapsilosis, a yeast lacking alcohol dehydrogenase but able to grow on high glucose concentrations, were compared to those of Saccharomyces cerevisiae. Cells were grown either on 8% glucose or on 2% glycerol and activities measured under optimal conditions. Results were as follows: glycolytic enzymes of C. parapsilosis, except glyceraldehyde 3-phosphate dehydrogenase, exhibited an activity weaker than that of S. cerevisiae, especially when yeasts were grown on glycerol. Fructose-1,6 bisphosphatase, an enzyme implicated in gluconeogenesis and in the hexose monophosphate pathway, and known to be very sensitive to catabolite repression in S. cerevisiae, was always active in C. parapsilosis even when cells were grown on 8% glucose. However, the allosteric properties towards AMP and fructose-2,6-bisphosphate were the same in both strains. Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, two other enzymes of the hexose monophosphate pathway, exhibited a higher activity in C. parapsilosis than in S. cerevisiae. Regulation of two important control points of the glycolytic flux, phosphofructokinase and pyruvate kinase, was investigated. In C. parapsilosis phosphofructokinase was poorly sensitive to ATP but fructose-2,6-bisphosphate completely relieved the light ATP inhibition. Pyruvate kinase did not require fructose-1,6-bisphosphate for its activity, and by this way, did not regulate the glycolytic flux.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Comparative studies on the glycolytic and hexose monophosphate pathways in Candida parapsilosis and Saccharomyces cerevisiae. 283 96

Interspecific F1 hybrids of Peromyscus maniculatus (deermice) and P. polionotus (oldfield mice) were backcrossed to P. maniculatus. Backcross progeny were electrophoretically typed for 11 variant protein markers: albumin, transferrin, leucine aminopeptidase, amylase, 6-phosphogluconate dehydrogenase, nucleoside phosphorylase, dipeptidase, tripeptidase, glutamate oxaloacetate transaminase, alcohol dehydrogenase, and sorbitol dehydrogenase. Genetic variation for each protein was attributed to a single autosomal locus. The alcohol dehydrogenase (Adh), salivary amylase (Amy), and albumin (Alb) loci appeared to be linked in the sequence of Adh-11.5 cM-Amy-33.3 cM-Alb. The tripeptidase locus, Pep-2, also may be loosely linked to Alb in this group. Variants at all other loci assorted independently. These and other known linkage relationships in Peromyscus correspond closely to those of the house mouse, Mus musculus. The available evidence in Peromyscus further supports the concept of linkage conservation by natural selection.
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PMID:Linkage relationships among eleven biochemical loci in Peromyscus. 620 Jan 3

A biochemical study has been made of the effects of low doses of alpha chlorohydrin on all the glycolytic enzymes and two key enzymes of phosphogluconate pathway i.e. glucose-6-phosphate dehydrogenase (G-6-PDH) and 6-phosphogluconate dehydrogenase (6-PGDH) of rat testis and epididymis. All the glycolytic enzymes of testis and epididymis are decreased after treatment with alpha chlorohydrin. G-6-PDH and 6-PGDH are decreased only in epididymis and not in the testis. LDH, ADH and glucose-6-phosphatase were also studied histochemically to show that the drug affects the glycolytic enzymes of epididymal cells and various testicular cell types of testis. Possible significance of these results is discussed.
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PMID:Effect of low doses of alpha chlorohydrin on the enzymes of glycolytic and phosphogluconate pathways in the rat testis and epididymis. 626 79

Protease B [EC 3.4.22.9] was purified from baker's yeast by plasmolysis of yeast, acid activation, acid precipitation, and column chromatographies on QAE-Sephadex, SP-Sephadex, D-tryptophan methyl ester-Sepharose 4B and Sephadex G-100. The purified enzyme was inhibited by phenylmethylsulfonyl fluoride and sulfhydryl-blocking reagents. Chymostatin and antipain at extremely low concentrations (1 micro M) inhibited the protease B. The effects of the enzyme on various yeast enzymes were examined by measuring their inactivation. The enzyme inactivated 6-phosphogluconate dehydrogenase [EC 1.1.1.44] and uricase [EC 1.7.3.3], but not malate dehydrogenase [EC 1.1.1.37], alcohol dehydrogenase [EC 1.1.1.1], glutamate dehydrogenase [EC 1.4.1.3], glucose-6-phosphate dehydrogenase [EC 1.1.1.49] or hexokinase [EC 2.7.1.1].
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PMID:Purification and characterization of yeast protease B. 699 57


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