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)

An alcohol dehydrogenase of broad specificity was purified 43-fold from extracts of Mycobacterium tuberculosis var. bovis (BCG) grown on Sauton medium. It was also present in cells grown in Dubos medium and Tween 80 and bovine serum albumin. The enzyme, which appeared to be soluble, acted as an oxidoreductase in the system butan-1-ol-NADP. It was eluted from Sephadex G-200, hydroxylapatite and DEAE-cellulose in a single peak. The molecular weight, as determined by gel filtration on Sephadex G-200, was about 75,000. Results of electrophoresis in sodium dodecyl sulphate-polyacrylamide gels were compatible with the existence of two subunits each of molecular weight 37,500. The optimum pH was about 8.5 when the enzyme catalysed the oxidation of butan-1-ol, and about 8.2 for the reverse reaction. The apparent Km was 0.125 mM for butyraldehyde and 0.22 M for butan-1-ol. The dehydrogenase activity was maintained after heat treatment (40 min at 55 degrees C) in the presence of 30% (W/V) glycerol, but was abolished by heating (40 min at 55 degrees C) in the presence of 0.1 M-EDTA. The activity of enzyme inactivated by heat and EDTA could be fully restored at room temperature in the presence of 2 mM-Zn2+.
J Gen Microbiol 1981 Jun
PMID:Partial purification and characterization of an alcohol dehydrogenase of Mycobacterium tuberculosis var. bovis (BCG). 703 14

1. Female rats were placed on water, 5% ethanol (ET), or 20% ET drinking solutions for 8 weeks. The last 2 weeks, the rats received orally either ethinyl estradiol (EE), norethindrone acetete (NED), or a combination of both. 2. Luteinizing hormone decreased due to ET drinking and was undetectable subsequent to the steroidal treatment. 3. Prolactin increased after steroid treatment and alcohol drinking in the controls. 4. Ethanol (5%) plus EE increased prolactin as did the steroidal combination, whereas ET (20%) likewise increased prolactin in conjunction with NED over water controls. 5. Hepatic alcohol dehydrogenase was inhibited due to EE when compared to water-controls in the 5% ET drinking animal, whereas aldehyde dehydrogenase was induced in combination with NED in both the 5% and 20% ET drinking rats.
Gen Pharmacol 1982
PMID:The effect of oral contraceptives on reproductive function during semichronic exposure to ethanol by the female rat. 703 30

In Drosophila melanogaster transformants, the alcohol dehydrogenase (Adh) genes from D. affinidisjuncta and D. grimshawi show similar levels of expression except in the adult midgut where the D. affinidisjuncta gene is expressed about 10- to 20-fold more strongly. To study the arrangement of cis-acting sequences responsible for this regulatory difference, homologous restriction sites were used to create a series of chimeric genes that switched fragments from the 5' and 3' flanking regions of these two genes. Chimeric genes were introduced into the germ-line of D. melanogaster, and Adh gene expression was analyzed by measuring RNA levels. Various gene fragments in the promoter region and elsewhere influence expression in the adult midgut and in whole larvae and adults. Comparison of these results with earlier studies involving chimeras between the D. affinidisjuncta and D. hawaiiensis genes indicates that expression in the adult midgut is influenced by multiple regulatory sequences and that distinct arrangements of regulatory sequences can result in similar levels of expression both in the adult midgut and in the whole organism.
Mol Gen Genet 1993 Jul
PMID:Similar tissue-specific expression of the Adh genes from different Drosophila species is mediated by distinct arrangements of cis-acting sequences. 768 66

Open reading frames longer than 300 bases were observed in the antisense strands of the genes coding for the glycolytic enzymes phosphoglucose isomerase, phosphoglycerate mutase, pyruvate kinase and alcohol dehydrogenase I. The open reading frames on both strands are in codon register. It has been suggested that proteins coded in codon register by complementary DNA strands can bind to each other. Consequently, it was interesting to investigate whether the open reading frames in the antisense strands of glycolytic enzyme genes are functional. We used oligonucleotide-directed mutagenesis of the PGI1 phosphoglucose isomerase gene to introduce pairs of closely spaced base substitutions that resulted in stop codons in one strand and only silent replacements in the other. Introduction of the two stop codons into the PGI1 sense strand caused the same physiological defects as already observed for pgil deletion mutants. No detectable effects were caused by the two stop codons in the antisense strand. A deletion that removed a section from -31 bp to +109 bp of the PGI1 gene but left 83 bases of the 3' region beyond the antisense open reading frame had the same phenotype as a deletion removing both reading frames. A similar pair of deletions of the PYK1 gene and its antisense reading frame showed identical defects. Our own Northern experiments and those reported by other authors using double-stranded probes detected only one transcript for each gene. These observations indicate that the antisense reading frames are not functional. On the other hand, evidence is provided to show that the rather long reading frames in the antisense strands of these glycolytic enzyme genes could arise from the strongly selective codon usage in highly expressed yeast genes, which reduces the frequency of stop codons in the antisense strand.
Mol Gen Genet 1994 May 25
PMID:Open reading frames in the antisense strands of genes coding for glycolytic enzymes in Saccharomyces cerevisiae. 820 80

1. A brief overview of gonadal alcohol dehydrogenase (ADH) and aldehyde-dehydrogenase (ALDH) is presented and their relationships to gonadal toxicity of ethanol has been discussed. 2. The distributions of ADH and ALDH among major reproductive tissues of rodents, their subcellular localization and kinetic properties were summarized. 3. The sensitivity of testicular ADH and ALDH to ethanol intake, various psychoactive agents and steroidal compounds was assessed and the implication of these enzymes in gonadal ethanol-drug interaction has been suggested. 4. The possible role of testicular ALDH in tumorigenesis and in high altitude endocrine sensitivity to ethanol has been addressed.
Gen Pharmacol 1993 Sep
PMID:Pharmacological aspects of gonadal alcohol and aldehyde-dehydrogenase. 827 Jan 62

Valine aminotransferase, a key enzyme in both biosynthesis and breakdown of branched-chain amino acids, showed consistently higher activity in Candida utilis grown in continuous culture than in Saccharomyces cerevisiae, while pyruvate decarboxylase and alcohol dehydrogenase, the other two enzymes of the Ehrlich pathway of branched-chain alcohol formation, were lower in activity. By spheroplast lysis, it was shown that valine aminotransferase followed the distribution of pyruvate decarboxylase in being located in the cytosol. Replacement of ammonium as nitrogen source by valine during conditions of carbon or nitrogen limitation caused increased specific activities of these three enzymes in S. cerevisiae, but (with one exception) decreased those of C. utilis. Of the metabolites accumulating in the culture medium, little or no ethanol or branched-chain alcohols were present during carbon-limited growth of either organism, but the change to nitrogen limitation resulted in increases in concentration of 20- to 100-fold in pyruvate, acetate and non-pyruvate keto acids as well as the accumulation of branched-chain alcohols in both organisms, and of ethanol, ethyl acetate and glycerol in S. cerevisiae. When valine was the limiting nitrogen source, there was an increase in non-pyruvate keto acids and a 10- to 16-fold increase in 2-methylpropanol. Total branched-chain alcohols formed under nitrogen limitation were 2-fold higher in S. cerevisiae than in C. utilis, irrespective of nitrogen source. Accumulation of branched-chain alcohols, ethanol, acetate and glycerol was also observed during carbon-limited growth of S. cerevisiae with valine as nitrogen source at dilution rates above the critical rate for transition to respirofermentative growth. Less than 70% of the valine carbon metabolized during growth of S. cerevisiae and only 15% of that used during growth of C. utilis was recovered in identified metabolic products. Even allowing for losses by volatilization during aeration, this suggests that a significant amount of the valine is being metabolized by a route or routes other than the Ehrlich pathway, possibly via the action of branched-chain 2-keto acid dehydrogenase. The molar growth yield for the nitrogen source under either carbon or nitrogen limitation was significantly lower for growth on valine than for growth on ammonium, suggesting that breakdown of valine requires more energy. It is evident that not all the enzymes involved in branched-chain amino acid metabolism in yeasts have yet been identified, nor are their interactions properly understood.
J Gen Microbiol 1993 Nov
PMID:Activities of the enzymes of the Ehrlich pathway and formation of branched-chain alcohols in Saccharomyces cerevisiae and Candida utilis grown in continuous culture on valine or ammonium as sole nitrogen source. 827 58

The transcription factor ALCR of the ethanol utilisation pathway in Aspergillus nidulans contains a zinc binuclear motif (CysX2CysX6CysX16CysX2CysX6Cys), within the DNA-binding domain located in the N-terminal region of the ALCR protein. Specific targets have been localised in the promoter of the alcR gene, involved in the autoregulation process, and in the promoter of the structural gene alcA (encoding alcohol dehydrogenase I), which is also under the control of ALCR. The DNA-binding domain has been expressed in-Escherichia coli as a GST-ALCR (7-58*) fusion protein and also obtained as an ALCR (7-58*) peptide. Both the ALCR fusion protein and the ALCR peptide are able to bind 65Zn(II) in vitro, if reduction of cysteines occurs prior to the addition of zinc. Competition experiments showed that Cd(II), Co(II) and Cu(II) are efficient competitors for the zinc binding sites. The ALCR DNA-binding domain was shown to contain 2 mol of tightly bound Zn(II) per mole of fusion protein. Removal of the intrinsic Zn(II) requires treatment with Chelex. This treatment abolishes the ability of the protein to bind to the targets of ALCR located in the alcA and alcR promoters. The apo-ALCR DNA-binding motif could be reconstituted with Zn(II) or Cd(II), restoring specific DNA binding to both types of targets. Thus a direct relationship was shown to exist between the zinc content of ALCR and its DNA-binding activity.
Mol Gen Genet 1994 Jan
PMID:Relationship between zinc content and DNA-binding activity of the DNA-binding motif of the transcription factor ALCR in Aspergillus nidulans. 827 45

1. Breast fed maternally-mediated developmental LiCl toxicity was determined in mice offspring as a function of offspring's gender and duration of maternal intake of LiCl (1 mEq). 2. The female offspring were more sensitive than the males to major organ weight changes by maternal exposure to LiCl. 3. Maternal intake of LiCl from preconception until weaning of the nurslings induced offspring hepatic alcohol dehydrogenase and heart lactate dehydrogenase in both sexes which was isoenzyme specific for the latter. 4. The offspring also showed induction of liver aldehyde dehydrogenase but only as consequences of postnatal exposure to LiCl. 5. The results indicate offspring developmental toxicity as a consequence of maternal exposure to Li salts and breast feeding.
Gen Pharmacol 1993 Jan
PMID:Maternally-mediated developmental lithium toxicity in the mouse. 848 9

The lactose-utilizing yeast Kluyveromyces lactis is an essentially aerobic organism in which both respiration and fermentation can coexist depending on the sugar concentration. Despite a low fermentative capacity as compared to Saccharomyces cerevisiae, four structural genes encoding alcohol dehydrogenase (ADH) activities are present in this yeast. Two of these activities, namely K1ADH III and K1ADH IV, are located within mitochondria and their presence is dependent on the carbon sources in the medium. In this paper we demonstrate by transcription and activity analysis that KlADH3 is expressed in the presence of low glucose concentrations and in the presence of respiratory carbon sources other than ethanol. Indeed ethanol acts as a strong repressor of this gene. On the other hand, KlADH4 is induced by the presence of ethanol and not by other respiratory carbon sources. We also demonstrate that the presence of KLADH III and KLADH IV in K. lactis cells is dependent on glucose concentration, glucose uptake and the amount of ethanol produced. As a consequence, these activities can be used as markers for the onset of respiratory and fermentative metabolism in this yeast.
Mol Gen Genet 1995 Dec 20
PMID:Two mitochondrial alcohol dehydrogenase activities of Kluyveromyces lactis are differently expressed during respiration and fermentation. 854 32

The acvA gene from Aspergillus nidulans encoding delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) synthetase was overexpressed by replacing the wild-type acvA promoter with the ethanol dehydrogenase promoter, alcAp, from A. nidulans. The expression level of alcAp was determined using a strain in which the reporter gene, lacZ, is under the control of alcAp, and was found to be up to 100 times greater than that from the acvA promoter when induced in fermentation conditions. Penicillin yields were found to increase by as much as 30-fold when the acvA gene was overexpressed. Glucose, which strongly represses transcription from alcAp, also repressed penicillin biosynthesis in the overexpression strain. These results prove that ACV synthetase is a rate limiting enzyme for penicillin production in A. nidulans.
Mol Gen Genet 1996 Nov 27
PMID:delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase is a rate limiting enzyme for penicillin production in Aspergillus nidulans. 900 3


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