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)

Phenothiazines and W7, calmodulin antagonists, inhibit the water flow response produced by ADH, exogenous cyclic AMP, phosphodiesterase inhibition and serosal hypertonicity. Calmodulin antagonists had no effect on osmotic water movement in the absence of hormone. Calmodulin was isolated and localized by immunofluorescence in bladder epithelial cells. Phenothiazines inhibited toad bladder calmodulin activation of phosphodiesterase and prevented fluorescent antibody recognition. The results suggest that the calcium-calmodulin process plays a role in the hydro-osmotic response to ADH and that produced by serosal hypertonicity. The calmodulin common site occurs subsequent to cyclic AMP formation, perhaps on the microtubule-microfilament system.
Gen Pharmacol 1985
PMID:Inhibition of the hydro-osmotic response to vasopressin and hypertonicity by phenothiazines and W7, calmodulin antagonists. 299 93

Drosophila melanogaster flies were transformed with a yp1-Adh fusion gene with 890 bp of yp1 5' flanking sequence. In an Adh- background these flies show a stage, tissue and sex-specific pattern of alcohol dehydrogenase (ADH) activity characteristic of yolk protein genes. ADH activity is not present in dsxD/dsx pseudomales indicating that this fragment contains sites where the dsx gene product exerts its effect. Transformed male flies do not exhibit ADH activity when injected with 20-hydroxyecdysone while synthesis of native yolk proteins is induced. Thus the hormone inducibility and sex regulation have been separated in this construct.
Mol Gen Genet 1987 Nov
PMID:Separate DNA sequences are required for normal female and ecdysone-induced male expression of Drosophila melanogaster yolk protein 1. 312 86

1. Forskolin, an activator of adenyl-cyclase in a receptor-independent manner, mimics the ADH effect on the urea and thiourea permeabilities across the toad bladder. 2. However, differently from ADH, forskolin increases the erythritol permeability across the tissue and this effect is not reproduced by two substances increasing the urea permeability (8-BrcAMP and isoprenaline). Most probably this effect of forskolin does not involve the cAMP generating system.
Gen Pharmacol 1988
PMID:Action of forskolin on non-electrolyte permeability across the urinary bladder of Bufo bufo as compared to that of various hormones. 313 18

Until recently the alcohol dehydrogenase of Drosophila melanogaster was thought to act only in the first step of primary alcohol oxidation, producing an aldehyde. Instead, acetic acid is the main product of a two-step process. A rapid procedure was developed for the isolation and purification of two allozymes. The thermostability of the purified enzymes was found to be very different, t 1/2 at 35 degrees C, being 45 min and 130 min for ADH-F and ADH-71k respectively. The kinetic parameters of ethanol oxidation by the two purified allozymes were determined within physiological substrate and coenzyme ranges. The use of artificial electron acceptors has a notable influence on the ethanol oxidation: the apparent Michaelis constants increase; the oxidation rate with ADH-71k increases, whereas it decreases with ADH-F. Purified ADH is shown to be able to catalyze the oxidation of acetaldehyde solely in the presence of NAD+, and PMS and MTT as artificial electron acceptors. From the kinetic data the relative in vivo oxidation rates of ethanol by both ADH allozymes were calculated. ADH-F turned out to be somewhat less effective (30%-40%) than ADH-71k. The physiological consequences of these differences are discussed.
Mol Gen Genet 1985
PMID:Dual function of the alcohol dehydrogenase of Drosophila melanogaster: ethanol and acetaldehyde oxidation by two allozymes ADH-71k and ADH-F. 315 99

The dosage of the transcriptional activator ADR1 was varied in order to study the regulation of the glucose-repressible alcohol dehydrogenase (ADH II) from Saccharomyces cerevisiae. ADH II activity during glucose growth conditions was shown to increase linearly with increasing ADR1 gene dosage. In contrast, under derepressed growth conditions a 100-fold increase in ADR1 copy number resulted in only a 4-fold increase in ADH II expression. Saturation of ADH II gene expression by ADR1 under derepressed conditions was shown not to result from decreased ADR1 transcription. Increases in ADH2 gene dosage in conjunction with high ADR1 gene dosages resulted in increased ADH II activity, indicating that ADH2 was the limiting factor during derepression. Under glucose-repressed conditions the activator CCR1 was not required for ADR1 activity. During derepression increasing ADR1 dosage could partially compensate for a CCR1 defect. Increasing CCR1 gene dosage, however, had no effect on ADH2 expression regardless of the ADR1 allele present. These results suggest that CCR1 acts through ADR1 in controlling ADH2 expression. It was also observed that high numbers of ADR1, or a few copies of ADR1-5c, substantially increased the cell doubling time under ethanol growth conditions, indicating that increased ADR1 activity is toxic.
Mol Gen Genet 1987 Jun
PMID:The effects of ADR1 and CCR1 gene dosage on the regulation of the glucose-repressible alcohol dehydrogenase from Saccharomyces cerevisiae. 330 3

The effect of the glucose analogue 5-thio-D-glucose (5TG) on the yeast Saccharomyces cerevisiae was studied. Derepression of mitochondrial respiratory chain cytochromes, alcohol dehydrogenase (isoenzyme II), NADH dehydrogenase and maltase was inhibited by 0.5-2 mM-5TG. Growth rate was only slightly affected. Ethanol was efficiently produced with 2 mM-5TG in medium initially containing 0.25% glucose. Mutants resistant to the growth inhibitory effects of 5TG on glycerol medium showed resistance to the catabolite repressing effects of glucose. Other mutants, known to be catabolite repression resistant, showed resistance to 5TG. The analogue seems to inhibit derepression of glucose repressible enzymes with greater potency than glucose itself.
J Gen Microbiol 1986 Dec
PMID:Catabolite repressive effects of 5-thio-D-glucose on Saccharomyces cerevisiae. 330 35

Antisera were raised against several purified, high specific activity isozymes of maize alcohol dehydrogenase (ADH1). The various antisera had different effects on the activity of immunoprecipitated ADH. One antiserum completely inactivated maize ADH. This inactivation could be blocked by preincubation of the enzyme with NAD+, its cofactor, or with NADP. The different antisera were used to analyze variant forms of ADH1. Isozymes having lowered specific activity were activated to wild-type levels by precipitation of the enzymes with noninactivating antisera. Isozymes having no detectable ADH activity (CRM+ nulls) were activated by immunoprecipitation with noninactivating antisera when preincubated with NAD+ or NADP. All of the CRM+ nulls were shown to be unable to bind NAD+, a flaw which can account for their lack of activity. The results indicate that a conformational equilibrium between active and inactive forms of maize ADH in solution controls the specific activity of the various isozymes. Both NAD+ and antibodies raised against high specific activity enzymes can interact with low activity isozymes to shift the balance of the equilibrium toward the active form, thus increasing their specific activity.
Mol Gen Genet 1987 Jun
PMID:Activation of low and null activity isozymes of maize alcohol dehydrogenase by antibodies. 347 28

The denV gene of bacteriophage T4 was reconstituted from two overlapping DNA fragments cloned in M13 vectors. The coding region of the intact gene was tailored into a series of plasmid vectors containing different promoters suitable for expression of the gene in E. coli and in yeast. Induction of the TAC promoter with IPTG resulted in overexpression of the gene, which was lethal to E. coli. Expression of the TACdenV gene in the absence of IPTG, or the use of the yeast GAL1 or ADH promoters resulted in partial complementation of the UV sensitivity of uvrA, uvrB, uvrC and recA mutants of E. coli and rad1, rad2, rad3, rad4 and rad10 mutants of S. cerevisiae. The extent of denV-mediated reactivation of excision-defective mutants was approximately equal to that of photoreactivation of such strains. Excision proficient E. coli cells transformed with a plasmid containing the denV gene were slightly more resistant to ultraviolet (UV) radiation than control cells without the denV gene. On the other hand, excision proficient yeast cells were slightly more sensitive to killing by UV radiation following transformation with a plasmid containing the denV gene. This effect was more pronounced in yeast mutants of the RAD52 epistasis group.
Mol Gen Genet 1986 Apr
PMID:Partial complementation of the UV sensitivity of E. coli and yeast excision repair mutants by the cloned denV gene of bacteriophage T4. 352 Feb 42

Mutants of Escherichia coli resistant to chloroethanol or to chloroacetaldehyde were selected. Such mutants were found to lack the fermentative coenzyme A (CoA) linked acetaldehyde dehydrogenase activity. Most also lacked the associated fermentative enzyme alcohol dehydrogenase. Both types of mutants, those lacking acetaldehyde dehydrogenase alone or lacking both enzymes, mapped close to the regulatory adhC gene at 27 min on the E. coli genetic map. The previously described acd mutants which lack acetaldehyde dehydrogenase and which map at 63 min were shown to be pleiotropic, affecting respiration and growth on a variety of substrates. It therefore seems likely that the structural genes for both the acetaldehyde and alcohol dehydrogenases lie in the adhCE operon. This interpretation was confirmed by the isolation of temperature sensitive chloracetaldehyde-resistant mutants, some of which produced thermolabile acetaldehyde dehydrogenase and alcohol dehydrogenase and were also found to map at the adh locus. Reversion analysis indicated that mutants lacking one or both enzymes carried single mutations. The gene order in the adh region was determined by three point crosses to be trp-zch::Tn10-adh-galU-bglY-tyrT-chlC.
Mol Gen Genet 1986 Dec
PMID:The use of suicide substrates to select mutants of Escherichia coli lacking enzymes of alcohol fermentation. 355 Mar 85

The present study deals with an analysis of specific traits of cell vacuolation induced by water flow and ADH. During incubation of frog urinary bladders in Ringer's solution diluted 2-fold, the water content of the bladder wall increased by an average of 19%. In case of ADH-stimulated water flow the water content increased by an average of 15.7%. Cell swelling induced by hypotonic conditions on the serosal side resulted in a drastic decrease of the response to the hydroosmotic action of ADH. Electron microscopy revealed significant differences between cells hydrated in the above conditions. Two-fold hypotonicity of the serosal solution caused a slight swelling of all types of cells accompanied by a narrowing of intercellular spaces. With ADH stimulation of water transport (at maximal water movement) granular cells were characterized by the presence of irregularly shaped giant vacuoles with processes. The limiting membranes of the vacuoles were closely connected with microtubules and microfilaments. The electron microscopic study of these cells by the freeze-substitution method revealed, in addition to giant vacuoles, a highly complex system of microtubules 35-40 nm in diameter. A morphological similarity was observed between the vacuolar systems of these granular cells and the contractile vacuole complex of protozoans. Possible mechanisms for the participation of giant vacuoles, electron-dense canaliculi, microtubules and microfilaments in transcellular water flow across epithelium are discussed.
Gen Physiol Biophys 1985 Dec
PMID:Specific vacuolation of frog urinary bladder granular cell after ADH stimulation of water transport. 387 15


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