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)

Yeast mutants with glucose-insensitive formation of mitochondrial enzymes were isolated starting with a strain completely lacking alcohol dehydrogenase activity. The mutations could uniquely be attributed to a single nuclear gene, designated CCR80. They were largely dominant. Glucose-resistant enzyme formation was most prominent with regard to mitochondrial enzymes succinate dehydrogenase and NADH: cytochrome c oxidoreductase. The effect of CCR80r mutations was rather small but significant on the gluconeogenetic enzymes isocitrate lyase, malate synthase and fructose-1,6-bisphosphatase and on invertase synthesis. The repressive effect of maltose in CCR80r mutants was also reduced showing that glucose-resistance is not caused by a mere hexose uptake defect. This regulatory disorders were not accompanied by reduced levels of glycolytic enzymes or drastically altered levels of glycolytic intermediates. Aerobic fermentation of glucose was almost completely inhibited in the mutants; anaerobic glucose degradation was reduced but not completely abolished. Therefore, the mutants appear to be altered in the regulation of glycolysis. A largely glucose-resistant synthesis of respiratory enzymes is obviously a corollary of this alteration.
Mol Gen Genet 1978 Feb 27
PMID:A yeast mutant with glucose-resistant formation of mitochondrial enzymes. 20 62

Mutants altered in carbon catabolite regulation have been isolated by selecting for mutants of the areA217 strain capable of using acetamide as the sole nitrogen source in the presence of sucrose. In addition to creA mutants described previously be Arst and Cove, strains with mutations in two new genes, creB and cre C, have been found. The creB and creC mutants grow poorly on some sole carbon sources and have low levels of some enzymes of carbon catabolism e.g. beta-galactosidase and D-quinate dehydrogenase. The creB and creC mutants are hypersensitive to fluoroacetate, fluoroacetamide and allyl alcohol in the presence of glucose or sucrose but not glycerol; and the enzymes, acetamidase and alcohol dehydrogenase, are less sensitive to carbon catabolite repression than the wild-type strain. Extracellular protease and alpha-glucosidase enzyme activities are elevated in creB and creC mutants, while L-proline and L-glutamate uptake capacities are lower in both the presence and absence of glucose. Interactions between creA, B and C mutations have been investigated in double mutants, and the dominance properties of creB and creC mutants determined. The results indicate that the creB and creC genes may have a regulatory role in the control of carbon catabolism.
Mol Gen Genet 1977 Jan 18
PMID:Pleiotropic mutants of Aspergillus nidulans altered in carbon metabolism. 32 Apr 55

Starting with yeast cells lacking the constitutive alcohol dehydrogenase activity (ADHI), mutants with partially glucose-insensitive formation of ADHII were isolated. Genetic analysis showed that four mutants (designated ADR3c) were linked to the ADHII-structural gene, ADR2, and were cis-dominant. On derepression, two of them produced elevated ADHII-levels, indicating a promotor function of the altered controlling site. The other ADR3c-mutant alleles affected the ADHII-subunit association in diploids carrying two electrophoretically distinct alleles of the structural gene ADR2. Twelve semidominant constitutive mutants could be attributed to gene ADR1 (ADR1c-alleles) previously identified by recessive mutants with blocked derepression. This suggested a positive regulatory role of the ADR1 gene product on the expression of the ADHII-structural gene. A pleiotropic mutation ccr1 (Ciriacy, 1977) was epistatic over glucose-resistant ADHII-formation caused by ADR1c-alleles. From this it was concluded that CCR1 specifies for a product co-activating the structural gene or modifying the ADR1-gene product. A further regulatory element (gene designation ADR4) not linked to the structural gene could be identified upon isolation of recessive constitutive mutants adr4 from a ccr1 ADR1c-double mutant.
Mol Gen Genet 1979 Nov
PMID:Isolation and characterization of further cis- and trans-acting regulatory elements involved in the synthesis of glucose-repressible alcohol dehydrogenase (ADHII) in Saccharomyces cerevisiae. 39 42

Seven suppressor mutations have been isolated in Aspergillus nidulans by coreversion of alleles in physiologically unrelated genes namely, alX, sB, alcA, putative structural genes for allantoinase, sulphate permease and alcohol dehydrogenase respectively. The suppressors are allele specific, gene unspecific. Those described map in four loci, suaA, B, C, D. suaA and suaB are on linkage group III, suaC and suaD on VII. suaB111, suaD103 and suaD108 are semi-dominant in their suppression of alX4 and sB43, suaA101, suaA105 and suaC10. are recessive and have a pleiotropic effect on morphology. SuaC109 is cold sensitive for growth as is sua115, an unmapped mutation on linkage group III which is similar in morphology to suaC109. The two mutations, suaA101 and suaA105 have different spectra of suppression and morphologies. suaA105 weakly suppresses alX4 and sB43 whereas suaA101 strongly suppresses these and alcA125. suaD103 and suaD108 have the same spectrum of suppression. The properties of these suppressors are consistent with their being informational suppressors are consistent with their being informational suppressors of the nonsense type.
Mol Gen Genet 1979
PMID:Allele specific, gene unspecific suppressors in Aspergillus nidulans. 39 16

Glutamate induced the synthesis of 2-oxoglutarate dehydrogenase 50-fold during anaerobic growth of Citrobacter freundii and, in the absence of glutamate, this enzyme was even more active in cultures sparged with N2/CO2(95:5, v/v). Enzyme synthesis was partially repressed when the inlet gas was passed through heated copper but totally repressed when the inlet gas was passed through alkaline pyrogallol and reduced benzyl viologen (a treatment which would remove CO2 as well as O2). Fumarate hydratase activity also decreased but alcohol dehydrogenase and the sum of the succinate dehydrogenase and fumarate reductase activities increased when residual O2 was removed from the sparging gas. Soluble cytochromes a1 and c552.5 were detected in rigorously anaerobic cultures. Thus traces of O2 which contaminate commercial compressed N2 are sufficient to induce 2-oxoglutarate dehydrogenase synthesis and to affect significantly the synthesis and incorporation of respiratory chain components into the cytoplasmic membrane.
J Gen Microbiol 1979 Oct
PMID:Regulation of 2-oxoglutarate dehydrogenase synthesis in Citrobacter freundii by traces of oxygen in commercial nitrogen gas and by glutamate. 54 60

The formation of ADHII in Saccharomyces cerevisiae is regulated by carbon catabolite repression. There are two genes involved in the formation of ADHII: ADR2, the structural gene as identified by electrophoretic variants and ADR1, possibly a regulatory gene. A new genetic element involved in the regulation of ADHII was identified by three allelic mutants insensitive to strong glucose repression. They were called ADR3c (wild type designation ADR3) and found to be tightly linked to the structural gene, ADR2. The alcohol dehydrogenase found in ADR3c mutants could not be distinguished electrophoretically from the ADHII of the glucose-sensitive wild type, ADR3. Dominance relations between ADR3c and ADR3 were established in diploids heterozygous for ADR3 and the two alleles of ADR2 (ADR2-S: slow ADHII, ADR2-F: fast ADHII). During growth on 10% glucose, an ADR3c adr2-F/ADR3 ADR2-Sheterozygous diploid formed only the fast ADHII variant wheras an ADR3c ADR2-S/ADR3 ADR2-F heterozygote produced only the slow form. This was taken as evidence of the cis-dominance of all ADR3c alleles. The cis-effect of ADR3c was also demonstrated in glucose-derepressed diploids. The ADR3c mutations do not only cause glucose-insensitive ADHII frmation, but also reduce the activity of the adjacent structural gene during derepression. Thus ADR3c alleles were considered to be controlling site mutations. No pleiotropic effects were observed on the formation of enzymes related to the function of ADHII. An adr1 ADR2 ADR3 single mutant did not form ADHII. In contrast to this, an adr1 ADR2 ADR3c double mutant formed ADHII at a similar level as double mutant formed ADHII at a similar level as an ADR1 ADR2 ADR3c mutant. This showed that ADR3c was epistatic over adr1 (previously suggested as a positive regulatory gene). From this it was concluded that ADR1 is the fact a positive regulatory gene the function of which is required for the expression of the structural gene for ADHII, ADR2. ADR3 is the controlling site for the structural gene ADR2. Mutations at this site, ADR3c, alleviate the requirement for the ADR2 gene product. Adr3c is discussed as a promotor or operator site.
Mol Gen Genet 1976 Jun 15
PMID:Cis-dominant regulatory mutations affecting the formation of glucose-repressible alcohol dehydrogenase (ADHII) in Saccharomyces cerevisiae. 78 20

Increases in transepithelial solute permeability were elicited in the frog skin with external hypertonic urea, theophylline, and vasopressin (ADH). In external hypertonic urea, which is known to increase the permeability of the extracellular (paracellular) pathway, the unidirectional transepithelial fluxes of Na (passive), K, Cl, and urea increased substantially while preserving a linear relationship to each other. The same linear relationship was also observed for the passive Na and urea fluxes in regular Ringer and under stimulation with ADH or 10 mM theophylline, indicating that their permeation pathway was extracellular. A linear relationship between Cl and urea fluxes could be demonstrated if the skins were separated according to their open circuit potentials; parallel lines were obtained with increasing intercepts on the Cl axis as the open circuit potential decreased. The slopes of the Cl vs. urea lines were not different from that obtained in external hypertonic urea, indicating that this relationship described the extracellular movement of Cl. The intercept on the ordinate was interpreted as the contribution from the transcellular Cl movement. In the presence of 0.5 mM theophylline or 10 mU/ml of ADH, mainly the transcellular movement of Cl increased, whereas 10 mM theophylline caused increases in both transcellular and extracellular Cl fluxes. These and other data were interpreted in terms of a possible intracellular control of the theophylline-induced increase in extracellular fluxes. The changes in passive solute permeability were shown to be independent of active transport. The responses of the active transport system, the transcellular and paracellular pathways to theophylline and ADH could be explained in terms of the different resulting concentrations of cyclic 3'-5'-AMP produced by each of these substances in the tissue.
J Gen Physiol 1975 May
PMID:Actions of external hypertonic urea, ADH, and theophylline on transcellular and extracellular solute permeabilities in frog skin. 108 Jul 96

Two unlinked loci controlling the glucose-repressible alcohol dehydrogenase (ADH II) in Saccharomyces cerevisiae were investigated. One locus (AD R2) was characterized by electrophoretically slow and fast alleles and by inactive adr2 mutant alleles. The ADH II pattern of heteroallelic slow X fast diploids indicates a tetrameric structure of the enzyme. AD R2 was considered as the structural gene, which codes for the ADH II subunits. Allelic adr2-f mutants could be classified by their response to the slow wild type allele (AD RS-S) in heterozygous diploids. In most cases, only the slow band appeared. In three adr2-f/ADR2-S crosses hybrid enzymes between inactive fast and active slow enzymes were formed. It was demonstrated, that allelic interactions at the protein level are not restricted to electrophoretical behaviour of hybrid enzymes. They also influence specific activities and substrate affinities. The other locus investigated, AD R1, was characterized by ADH II negative mutants (adr1) and by allelic mutants which generate only very low activity (ADR1-L). ADR1 does not influence the electrophoretic properties of slow and fast ADH II proteins. adr1 mutants have an intact structural gene, which is not expressed. The gene has probably a regulatory function with respect to ADH II synthesis.
Mol Gen Genet 1975
PMID:Genetics of alcohol dehydrogenase in Saccharomyces cerevisiae. II. Two loci controlling synthesis of the glucose-repressible ADH II. 110 50

Twenty transformed lines have been isolated as a result of the germ line insertion of a 3.2 kb alcohol dehydrogenase (Adh) gene fragment into an Adh negative strain of Drosophila melanogaster by P element-mediated transformation. More than half of these lines exhibited abnormal ADH expression. The level of ADH expression ranges from zero in some lines to near normal levels in others, and the pattern of ADH expression in the larval gut is also abnormal in many of these lines. Each of the abnormal tissue-specific patterns is stable and characterized by the absence or reduction of ADH expression in certain tissues. High levels of ectopic expression were not observed. In two of these lines, the pattern of ADH staining is highly restricted: it is limited to the medial midgut in line MM-50, and to the gastric caecae and the proventriculus in line GC-1. In heterozygotes between these two lines ADH is expressed in both of these tissues. To test the hypothesis that this abnormal expression is due to position effects, inserts were mobilized to new locations. The mobilized inserts exhibited new patterns of tissue-specific expression associated with new cytological insert locations, showing that the abnormal expression in lines MM-50 and GC-1 is due to tissue-specific position effects and not to mutations. The results are discussed in the context of chromatin structure as a possible cause of these position effects.
Mol Gen Genet 1992 Mar
PMID:Tissue-specific position effects on alcohol dehydrogenase expression in Drosophila melanogaster. 131 45

1. Indomethacin injected subcutaneously at a single "ulcerogenic" dose decreased aminooxidase and leucine aminopeptidase activity and did not change alcohol dehydrogenase and ceruloplasmin activity. 2. Indomethacin administered at an oral "therapeutic" dose inhibited aminooxidase activity in small intestinal mucosa but not in liver and did not change leucine aminopeptidase activity in blood, liver and intestinal mucosa; it, however, increased alcohol dehydrogenase and ceruloplasmin activity. 3. The decreased activity of ceruloplasmin and alcohol dehydrogenase by metal deficiency increased after oral indomethacin treatment, reaching the control values when indomethacin was chelated with copper. 4. The results suggest the participation of endogenous metals in the indomethacin effect.
Gen Pharmacol 1992 Sep
PMID:In vivo effects of indomethacin on the activity of metal-containing enzymes. 135 44


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