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Indrati, Retno, Junko Naito, and Yoshiyuki Ohta. "Coenzyme-dependent alcohol dehydrogenases in Candida guilliermondii Y4." Canadian Journal of Microbiology 37, no. 11 (November 1, 1991): 803–7. http://dx.doi.org/10.1139/m91-139.
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Candida guilliermondii Y4 is capable of synthesizing two different alcohol dehydrogenases. ADH1 is constitutive on different carbon sources under shaking or settling conditions and its activity is prominent on gel electrophoresis. ADH2 is only synthesized under shaking condition. Two types of mutants were isolated using an allyl alcohol selection technique. ADH1-deficient mutants had 2.7% ADH activity of the wild type, while ADH2-deficient mutants had an ADH activity as high as that of the wild-type ADH activity. The alcohol dehydrogenases of the mutants differ from those of the wild type in their relative oxidation rates of alcohols. ADH1 appears to possess a functional role mainly in the production of ethanol from acetaldehyde, while ADH2 functions mainly in the oxidation of ethanol to acetaldehyde. However, both enzymes seem to be capable of carrying out the reverse reactions, since mutants lacking either of them still grew satisfactorily on different carbon sources. Key words: Candida guilliermondii, alcohol dehydrogenase, ADH1-deficient mutant, ADH2-deficient mutant.
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Burdette, D., and J. G. Zeikus. "Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenase (2° Adh) as a bifunctional alcohol dehydrogenase-acetyl-CoA reductive thioesterase." Biochemical Journal 302, no. 1 (August 15, 1994): 163–70. http://dx.doi.org/10.1042/bj3020163.
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The purification and characterization of three enzymes involved in ethanol formation from acetyl-CoA in Thermoanaerobacter ethanolicus 39E (formerly Clostridium thermohydrosulfuricum 39E) is described. The secondary-alcohol dehydrogenase (2 degrees Adh) was determined to be a homotetramer of 40 kDa subunits (SDS/PAGE) with a molecular mass of 160 kDa. The 2 degrees Adh had a lower catalytic efficiency for the oxidation of 1 degree alcohols, including ethanol, than for the oxidation of secondary (2 degrees) alcohols or the reduction of ketones or aldehydes. This enzyme possesses a significant acetyl-CoA reductive thioesterase activity as determined by NADPH oxidation, thiol formation and ethanol production. The primary-alcohol dehydrogenase (1 degree Adh) was determined to be a homotetramer of 41.5 kDa (SDS/PAGE) subunits with a molecular mass of 170 kDa. The 1 degree Adh used both NAD(H) and NADP(H) and displayed higher catalytic efficiencies for NADP(+)-dependent ethanol oxidation and NADH-dependent acetaldehyde (identical to ethanal) reduction than for NADPH-dependent acetaldehyde reduction or NAD(+)-dependent ethanol oxidation. The NAD(H)-linked acetaldehyde dehydrogenase was a homotetramer (360 kDa) of identical subunits (100 kDa) that readily catalysed thioester cleavage and condensation. The 1 degree Adh was expressed at 5-20% of the level of the 2 degrees Adh throughout the growth cycle on glucose. The results suggest that the 2 degrees Adh primarily functions in ethanol production from acetyl-CoA and acetaldehyde, whereas the 1 degree Adh functions in ethanol consumption for nicotinamide-cofactor recycling.
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Wolszczak-Biedrzycka, Blanka, Elżbieta Zasimowicz-Majewska, Anna Bieńkowska, Grzegorz Biedrzycki, Justyna Dorf, and Wojciech Jelski. "Activity of Total Alcohol Dehydrogenase, Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase in the Serum of Patients with Alcoholic Fatty Liver Disease." Medicina 58, no. 1 (December 24, 2021): 25. http://dx.doi.org/10.3390/medicina58010025.
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Background and objectives: The aim of the current study was to assess the use of determinations of total alcohol dehydrogenase and the activity of its isoenzymes as well as aldehyde dehydrogenase in the serum of patients with alcohol liver disease. Materials and Methods: The testing was performed on the serum of 38 patients with alcoholic fatty liver (26 males and 12 females aged 31–75). The total activity of ADH was determined by the colorimetric method. The activity of ADH I and ADH II, as well as ALDH, was determined by the spectrofluorometric method using fluorogenic specific substrates. The activity of isoenzymes of other classes was determined by spectrophotometric methods using substrates. Results: A statistically significantly higher ADH I activity was noted in the serum of patients with alcoholic fatty liver (4.45 mIU/L) compared to the control group (2.04 mIU/L). A statistically significant increase in the activity was also noted for the class II alcohol dehydrogenase isoenzyme (29.21 mIU/L, control group: 15.56 mIU/L) and the total ADH (1.41 IU/L, control group: 0.63 IU/L). Conclusions: The obtained results imply the diagnostic usefulness of the determination of AHD total, ADH I, and ADH II activity in the serum of patients with alcoholic fatty liver.
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Agarwal, Dharam P., and H. Werner Goedde. "Pharmacogenetics of alcohol dehydrogenase (ADH)." Pharmacology & Therapeutics 45, no. 1 (January 1990): 69–83. http://dx.doi.org/10.1016/0163-7258(90)90008-p.
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Lin, Guang-Huey, Ming-Chuan Hsieh, and Hung-Yu Shu. "Role of Iron-Containing Alcohol Dehydrogenases in Acinetobacter baumannii ATCC 19606 Stress Resistance and Virulence." International Journal of Molecular Sciences 22, no. 18 (September 14, 2021): 9921. http://dx.doi.org/10.3390/ijms22189921.
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Most bacteria possess alcohol dehydrogenase (ADH) genes (Adh genes) to mitigate alcohol toxicity, but these genes have functions beyond alcohol degradation. Previous research has shown that ADH can modulate quorum sensing in Acinetobacter baumannii, a rising opportunistic pathogen. However, the number and nature of Adh genes in A. baumannii have not yet been fully characterized. We identified seven alcohol dehydrogenases (NAD+-ADHs) from A. baumannii ATCC 19606, and examined the roles of three iron-containing ADHs, ADH3, ADH4, and ADH6. Marker-less mutation was used to generate Adh3, Adh4, and Adh6 single, double, and triple mutants. Disrupted Adh4 mutants failed to grow in ethanol-, 1-butanol-, or 1-propanol-containing mediums, and recombinant ADH4 exhibited strongest activity against ethanol. Stress resistance assays with inorganic and organic hydroperoxides showed that Adh3 and Adh6 were key to oxidative stress resistance. Virulence assays performed on the Galleria mellonella model organism revealed that Adh4 mutants had comparable virulence to wild-type, while Adh3 and Adh6 mutants had reduced virulence. The results suggest that ADH4 is primarily involved in alcohol metabolism, while ADH3 and ADH6 are key to stress resistance and virulence. Further investigation into the roles of other ADHs in A. baumannii is warranted.
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Young, E. T., and D. Pilgrim. "Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae." Molecular and Cellular Biology 5, no. 11 (November 1985): 3024–34. http://dx.doi.org/10.1128/mcb.5.11.3024-3034.1985.
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The Saccharomyces cerevisiae nuclear gene, ADH3, that encodes the mitochondrial alcohol dehydrogenase isozyme ADH III was cloned by virtue of its nucleotide homology to ADH1 and ADH2. Both chromosomal and plasmid-encoded ADH III isozymes were repressed by glucose and migrated heterogeneously on nondenaturing gels. Nucleotide sequence analysis indicated 73 and 74% identity for ADH3 with ADH1 and ADH2, respectively. The amino acid identity between the predicted ADH III polypeptide and ADH I and ADH II was 79 and 80%, respectively. The open reading frame encoding ADH III has a highly basic 27-amino-acid amino-terminal extension relative to ADH I and ADH II. The nucleotide sequence of the presumed leader peptide has a high degree of identity with the untranslated leader regions of ADH1 and ADH2 mRNAs. A strain containing a null allele of ADH3 did not have a detectably altered phenotype. The cloned gene integrated at the ADH3 locus, indicating that this is the structural gene for ADH III.
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Young, E. T., and D. Pilgrim. "Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae." Molecular and Cellular Biology 5, no. 11 (November 1985): 3024–34. http://dx.doi.org/10.1128/mcb.5.11.3024.
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The Saccharomyces cerevisiae nuclear gene, ADH3, that encodes the mitochondrial alcohol dehydrogenase isozyme ADH III was cloned by virtue of its nucleotide homology to ADH1 and ADH2. Both chromosomal and plasmid-encoded ADH III isozymes were repressed by glucose and migrated heterogeneously on nondenaturing gels. Nucleotide sequence analysis indicated 73 and 74% identity for ADH3 with ADH1 and ADH2, respectively. The amino acid identity between the predicted ADH III polypeptide and ADH I and ADH II was 79 and 80%, respectively. The open reading frame encoding ADH III has a highly basic 27-amino-acid amino-terminal extension relative to ADH I and ADH II. The nucleotide sequence of the presumed leader peptide has a high degree of identity with the untranslated leader regions of ADH1 and ADH2 mRNAs. A strain containing a null allele of ADH3 did not have a detectably altered phenotype. The cloned gene integrated at the ADH3 locus, indicating that this is the structural gene for ADH III.
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Winberg, J. O., R. Hovik, J. S. McKinley-McKee, E. Juan, and R. Gonzalez-Duarte. "Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis." Biochemical Journal 235, no. 2 (April 15, 1986): 481–90. http://dx.doi.org/10.1042/bj2350481.
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Purified Drosophila lebanonensis alcohol dehydrogenase (Adh) revealed one enzymically active zone in starch gel electrophoresis at pH 8.5. This zone was located on the cathode side of the origin. Incubation of D. lebanonensis Adh with NAD+ and acetone altered the electrophoretic pattern to more anodal migrating zones. D. lebanonensis Adh has an Mr of 56,000, a subunit of Mr of 28 000 and is a dimer with two active sites per enzyme molecule. This agrees with a polypeptide chain of 247 residues. Metal analysis by plasma emission spectroscopy indicated that this insect alcohol dehydrogenase is not a metalloenzyme. In studies of the substrate specificity and stereospecificity, D. lebanonensis Adh was more active with secondary than with primary alcohols. Both alkyl groups in the secondary alcohols interacted hydrophobically with the alcohol binding region of the active site. The catalytic centre activity for propan-2-ol was 7.4 s-1 and the maximum velocity of most secondary alcohols was approximately the same and indicative of rate-limiting enzyme-coenzyme dissociation. For primary alcohols the maximum velocity varied and was much lower than for secondary alcohols. The catalytic centre activity for ethanol was 2.4 s-1. With [2H6]ethanol a primary kinetic 2H isotope effect of 2.8 indicated that the interconversion of the ternary complexes was rate-limiting. Pyrazole was an ethanol-competitive inhibitor of the enzyme. The difference spectra of the enzyme-NAD+-pyrazole complex gave an absorption peak at 305 nm with epsilon 305 14.5 × 10(3) M-1 × cm-1. Concentrations and amounts of active enzyme can thus be determined. A kinetic rate assay to determine the concentration of enzyme active sites is also presented. This has been developed from active site concentrations established by titration at 305 nm of the enzyme and pyrazole with NAD+. In contrast with the amino acid composition, which indicated that D. lebanonensis Adh and the D. melanogaster alleloenzymes were not closely related, the enzymological studies showed that their active sites were similar although differing markedly from those of zinc alcohol dehydrogenases.
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Indrati, Retno, and Yoshiyuki Ohta. "Purification and properties of alcohol dehydrogenase from a mutant strain of Candida guilliermondii deficient in one form of the enzyme." Canadian Journal of Microbiology 38, no. 9 (September 1, 1992): 953–57. http://dx.doi.org/10.1139/m92-153.
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Alcohol dehydrogenase (ADH1) was purified from Candida guilliermondii strain B10-05 to homogeneity, using affinity chromatography on triazine dyes and gel filtration. The enzyme was tetrameric, with a subunit molecular weight of 38 000. The purified enzyme oxidized primary and secondary alcohols, although it preferred primary alcohols. Its activity toward secondary alcohols was better than those of other yeast ADH; however, the enzyme was less sensitive toward inhibitors. Kinetic studies indicated that C. guilliermondii ADH1 oxidized ethanol by an ordered bi–bi mechanism, with NAD as the first substrate fixed. Key words: Candida guilliermondii, alcohol dehydrogenase, ADH1, tetrameric.
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Sha, Chong, Qiang Wang, Hongcheng Wang, Yilan Duan, Chongmao Xu, Lian Wu, Kesen Ma, Weilan Shao, and Yu Jiang. "Characterization of Thermotoga neapolitana Alcohol Dehydrogenases in the Ethanol Fermentation Pathway." Biology 11, no. 9 (September 5, 2022): 1318. http://dx.doi.org/10.3390/biology11091318.
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Hyperthermophilic Thermotoga spp. are candidates for cellulosic ethanol fermentation. A bifunctional iron-acetaldehyde/alcohol dehydrogenase (Fe-AAdh) has been revealed to catalyze the acetyl-CoA (Ac-CoA) reduction to form ethanol via an acetaldehyde intermediate in Thermotoga neapolitana (T. neapolitana). In this organism, there are three additional alcohol dehydrogenases, Zn-Adh, Fe-Adh1, and Fe-Adh2, encoded by genes CTN_0257, CTN_1655, and CTN_1756, respectively. This paper reports the properties and functions of these enzymes in the fermentation pathway from Ac-CoA to ethanol. It was determined that Zn-Adh only exhibited activity when oxidizing ethanol to acetaldehyde, and no detectable activity for the reaction from acetaldehyde to ethanol. Fe-Adh1 had specific activities of approximately 0.7 and 0.4 U/mg for the forward and reverse reactions between acetaldehyde and ethanol at a pHopt of 8.5 and Topt of 95 °C. Catalyzing the reduction of acetaldehyde to produce ethanol, Fe-Adh2 exhibited the highest activity of approximately 3 U/mg at a pHopt of 7.0 and Topt of 85 °C, which were close to the optimal growth conditions. These results indicate that Fe-Adh2 and Zn-Adh are the main enzymes that catalyze ethanol formation and consumption in the hyperthermophilic bacterium, respectively.
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Chervin, Christian, Janyce K. Truett, and Jim Speirs. "Alcohol Dehydrogenase Expression and Alcohol Production during Pear Ripening." Journal of the American Society for Horticultural Science 124, no. 1 (January 1999): 71–75. http://dx.doi.org/10.21273/jashs.124.1.71.
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Regulation of alcohol dehydrogenase (ADH), activity of pyruvate decarboxylase (PDC) and accumulation of acetaldehyde and ethanol in `Packham's Triumph' pears (Pyrus communis, L.) subsequent to different storage regimes were investigated. Pears were stored for two months at -1 °C either in air (Air) or under hypoxia at 3 kPa O2 (Hyp) and subsequently warmed and allowed to ripen in air at 20 °C. One set of fruit stored in air at -1 °C was subjected to 3 days of hypoxia at -1 °C (Air+Hyp) before ripening in air. Acetaldehyde, ethanol and methanol levels increased in all fruit in a similar fashion during ripening and did not reflect differences in storage treatments. During ripening, ADH activities in posthypoxic samples were generally twice that of air samples. PDC activities increased for ≈6 days during ripening then declined slightly but did not differ significantly among treatments. Upon transfer to 20 °C in air, slightly higher levels of Adh mRNA were observed in samples treated with hypoxia than in air controls. Over the following 2 days at 20 °C, the Adh transcription was markedly induced in Air and Air+Hyp samples. Although all Adh mRNAs returned to control levels within 4 days, ADH activities remained higher in hypoxia-treated fruit than in controls for up to 18 days. These results suggest that, in ripening pears, ADH does not limit ethanol production, and that the expression of this enzyme comprises post-transcriptional regulations. GenBank accession numbers of the Adh cDNAs are AFO 31899 and AFO 31900.
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Becker, Aileen, Dominique Böttcher, Werner Katzer, Karsten Siems, Lutz Müller-Kuhrt, and Uwe T. Bornscheuer. "An ADH toolbox for raspberry ketone production from natural resources via a biocatalytic cascade." Applied Microbiology and Biotechnology 105, no. 10 (May 2021): 4189–97. http://dx.doi.org/10.1007/s00253-021-11332-9.
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Abstract Raspberry ketone is a widely used flavor compound in food and cosmetic industry. Several processes for its biocatalytic production have already been described, but either with the use of genetically modified organisms (GMOs) or incomplete conversion of the variety of precursors that are available in nature. Such natural precursors are rhododendrol glycosides with different proportions of (R)- and (S)-rhododendrol depending on the origin. After hydrolysis of these rhododendrol glycosides, the formed rhododendrol enantiomers have to be oxidized to obtain the final product raspberry ketone. To be able to achieve a high conversion with different starting material, we assembled an alcohol dehydrogenase toolbox that can be accessed depending on the optical purity of the intermediate rhododendrol. This is demonstrated by converting racemic rhododendrol using a combination of (R)- and (S)-selective alcohol dehydrogenases together with a universal cofactor recycling system. Furthermore, we conducted a biocatalytic cascade reaction starting from naturally derived rhododendrol glycosides by the use of a glucosidase and an alcohol dehydrogenase to produce raspberry ketone in high yield. Key points • LB-ADH, LK-ADH and LS-ADH oxidize (R)-rhododendrol • RR-ADH and ADH1E oxidize (S)-rhododendrol • Raspberry ketone production via glucosidase and alcohol dehydrogenases from a toolbox Graphical abstract
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MODIG, Tobias, Gunnar LIDÉN, and Mohammad J. TAHERZADEH. "Inhibition effects of furfural on alcohol dehydrogenase, aldehyde dehydrogenase and pyruvate dehydrogenase." Biochemical Journal 363, no. 3 (April 24, 2002): 769–76. http://dx.doi.org/10.1042/bj3630769.
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The kinetics of furfural inhibition of the enzymes alcohol dehydrogenase (ADH; EC 1.1.1.1), aldehyde dehydrogenase (AlDH; EC 1.2.1.5) and the pyruvate dehydrogenase (PDH) complex were studied in vitro. At a concentration of less than 2mM furfural was found to decrease the activity of both PDH and AlDH by more than 90%, whereas the ADH activity decreased by less than 20% at the same concentration. Furfural inhibition of ADH and AlDH activities could be described well by a competitive inhibition model, whereas the inhibition of PDH was best described as non-competitive. The estimated Km value of AlDH for furfural was found to be about 5μM, which was lower than that for acetaldehyde (10μM). For ADH, however, the estimated Km value for furfural (1.2mM) was higher than that for acetaldehyde (0.4mM). The inhibition of the three enzymes by 5-hydroxymethylfurfural (HMF) was also measured. The inhibition caused by HMF of ADH was very similar to that caused by furfural. However, HMF did not inhibit either AlDH or PDH as severely as furfural. The inhibition effects on the three enzymes could well explain previously reported in vivo effects caused by furfural and HMF on the overall metabolism of Saccharomyces cerevisiae, suggesting a critical role of these enzymes in the observed inhibition.
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Maria-Solano, Miguel A., Adrian Romero-Rivera, and Sílvia Osuna. "Exploring the reversal of enantioselectivity on a zinc-dependent alcohol dehydrogenase." Organic & Biomolecular Chemistry 15, no. 19 (2017): 4122–29. http://dx.doi.org/10.1039/c7ob00482f.
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Mitchell, William C., and Gojko Jelenkovic. "Characterizing NAD- and NADP-dependent Alcohol Dehydrogenase Enzymes of Strawberries." Journal of the American Society for Horticultural Science 120, no. 5 (September 1995): 798–801. http://dx.doi.org/10.21273/jashs.120.5.798.
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The NAD-dependent and NADP-dependent alcohol dehydrogenase activities of strawberries (Fragaria xananassa Duch.) were found to have broad substrate specificities including those alcohols and aldehydes responsible for strawberry aroma and flavor either directly or through their ester products. NAD-dependent activities were greatest against short-chained alcohols, whereas the NADP-dependent activities were most active against aromatic and terpene alcohols. Differences were seen in substrate specificity between receptacle and achene alcohol dehydrogenase activities. Alcohol dehydrogenase activities were found to be developmentally regulated in receptacle tissue and increased during the period of fruit maturation and ripening. Isoelectric focusing of NAD-dependent ADH activities showed that several isozymes of this enzyme exist, that they differ between receptacle and achene tissues, and that they vary among specific genotypes. Our results suggest that NAD- and NADP-dependent ADH activities are integral components of flavor and fragrance volatile production in ripening strawberries.
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Tvrdý, Václav, Marcel Hrubša, Eduard Jirkovský, David Biedermann, Michal Kutý, Kateřina Valentová, Vladimír Křen, and Přemysl Mladěnka. "Silymarin Dehydroflavonolignans Chelate Zinc and Partially Inhibit Alcohol Dehydrogenase." Nutrients 13, no. 12 (November 25, 2021): 4238. http://dx.doi.org/10.3390/nu13124238.
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Silymarin is known for its hepatoprotective effects. Although there is solid evidence for its protective effects against Amanita phalloides intoxication, only inconclusive data are available for alcoholic liver damage. Since silymarin flavonolignans have metal-chelating activity, we hypothesized that silymarin may influence alcoholic liver damage by inhibiting zinc-containing alcohol dehydrogenase (ADH). Therefore, we tested the zinc-chelating activity of pure silymarin flavonolignans and their effect on yeast and equine ADH. The most active compounds were also tested on bovine glutamate dehydrogenase, an enzyme blocked by zinc ions. Of the six flavonolignans tested, only 2,3-dehydroderivatives (2,3-dehydrosilybin and 2,3-dehydrosilychristin) significantly chelated zinc ions. Their effect on yeast ADH was modest but stronger than that of the clinically used ADH inhibitor fomepizole. In contrast, fomepizole strongly blocked mammalian (equine) ADH. 2,3-Dehydrosilybin at low micromolar concentrations also partially inhibited this enzyme. These results were confirmed by in silico docking of active dehydroflavonolignans with equine ADH. Glutamate dehydrogenase activity was decreased by zinc ions in a concentration-dependent manner, and this inhibition was abolished by a standard zinc chelating agent. In contrast, 2,3-dehydroflavonolignans blocked the enzyme both in the absence and presence of zinc ions. Therefore, 2,3-dehydrosilybin might have a biologically relevant inhibitory effect on ADH and glutamate dehydrogenase.
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Liu, Xueqian, Yanpeng Dong, Jing Zhang, Aixiang Zhang, Lei Wang, and Lu Feng. "Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2." Microbiology 155, no. 6 (June 1, 2009): 2078–85. http://dx.doi.org/10.1099/mic.0.027201-0.
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Two alkyl alcohol dehydrogenase (ADH) genes from the long-chain alkane-degrading strain Geobacillus thermodenitrificans NG80-2 were characterized in vitro. ADH1 and ADH2 were prepared heterologously in Escherichia coli as a homooctameric and a homodimeric protein, respectively. Both ADHs can oxidize a broad range of alkyl alcohols up to at least C30, as well as 1,3-propanediol and acetaldehyde. ADH1 also oxidizes glycerol, and ADH2 oxidizes isopropyl alcohol, isoamylol, acetone, octanal and decanal. The best substrate is ethanol for ADH1 and 1-octanol for ADH2. For both ADHs, the optimum assay condition is at 60 °C and pH 8.0, and both NAD and NADP can be used as the cofactor. Sequence analysis reveals that ADH1 and ADH2 belong to the Fe-containing/activated long-chain ADHs. However, the two enzymes contain neither Fe nor other metals, and Fe is not required for the activity, suggesting a new type of ADH. The ADHs characterized here are potentially useful in crude oil bioremediation and other bioconversion processes.
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Duester, G., M. L. Shean, M. S. McBride, and M. J. Stewart. "Retinoic acid response element in the human alcohol dehydrogenase gene ADH3: implications for regulation of retinoic acid synthesis." Molecular and Cellular Biology 11, no. 3 (March 1991): 1638–46. http://dx.doi.org/10.1128/mcb.11.3.1638-1646.1991.
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Retinoic acid regulation of one member of the human class I alcohol dehydrogenase (ADH) gene family was demonstrated, suggesting that the retinol dehydrogenase function of ADH may play a regulatory role in the biosynthetic pathway for retinoic acid. Promoter activity of human ADH3, but not ADH1 or ADH2, was shown to be activated by retinoic acid in transient transfection assays of Hep3B human hepatoma cells. Deletion mapping experiments identified a region in the ADH3 promoter located between -328 and -272 bp which confers retinoic acid activation. This region was also demonstrated to confer retinoic acid responsiveness on the ADH1 and ADH2 genes in heterologous promoter fusions. Within a 34-bp stretch, the ADH3 retinoic acid response element (RARE) contains two TGACC motifs and one TGAAC motif, both of which exist in RAREs controlling other genes. A block mutation of the TGACC sequence located at -289 to -285 bp eliminated the retinoic acid response. As assayed by gel shift DNA binding studies, the RARE region (-328 to -272 bp) of ADH3 bound the human retinoic acid receptor beta (RAR beta) and was competed for by DNA containing a RARE present in the gene encoding RAR beta. Since ADH catalyzes the conversion of retinol to retinal, which can be further converted to retinoic acid by aldehyde dehydrogenase, these results suggest that retinoic acid activation of ADH3 constitutes a positive feedback loop regulating retinoic acid synthesis.
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Duester, G., M. L. Shean, M. S. McBride, and M. J. Stewart. "Retinoic acid response element in the human alcohol dehydrogenase gene ADH3: implications for regulation of retinoic acid synthesis." Molecular and Cellular Biology 11, no. 3 (March 1991): 1638–46. http://dx.doi.org/10.1128/mcb.11.3.1638.
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Retinoic acid regulation of one member of the human class I alcohol dehydrogenase (ADH) gene family was demonstrated, suggesting that the retinol dehydrogenase function of ADH may play a regulatory role in the biosynthetic pathway for retinoic acid. Promoter activity of human ADH3, but not ADH1 or ADH2, was shown to be activated by retinoic acid in transient transfection assays of Hep3B human hepatoma cells. Deletion mapping experiments identified a region in the ADH3 promoter located between -328 and -272 bp which confers retinoic acid activation. This region was also demonstrated to confer retinoic acid responsiveness on the ADH1 and ADH2 genes in heterologous promoter fusions. Within a 34-bp stretch, the ADH3 retinoic acid response element (RARE) contains two TGACC motifs and one TGAAC motif, both of which exist in RAREs controlling other genes. A block mutation of the TGACC sequence located at -289 to -285 bp eliminated the retinoic acid response. As assayed by gel shift DNA binding studies, the RARE region (-328 to -272 bp) of ADH3 bound the human retinoic acid receptor beta (RAR beta) and was competed for by DNA containing a RARE present in the gene encoding RAR beta. Since ADH catalyzes the conversion of retinol to retinal, which can be further converted to retinoic acid by aldehyde dehydrogenase, these results suggest that retinoic acid activation of ADH3 constitutes a positive feedback loop regulating retinoic acid synthesis.
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Crabb, David W., Michinaga Matsumoto, David Chang, and Min You. "Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related pathology." Proceedings of the Nutrition Society 63, no. 1 (February 2004): 49–63. http://dx.doi.org/10.1079/pns2003327.
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Alcohol dehydrogenase (ADH) and mitochondrial aldehyde dehydrogenase (ALDH2) are responsible for metabolizing the bulk of ethanol consumed as part of the diet and their activities contribute to the rate of ethanol elimination from the blood. They are expressed at highest levels in liver, but at lower levels in many tissues. This pathway probably evolved as a detoxification mechanism for environmental alcohols. However, with the consumption of large amounts of ethanol, the oxidation of ethanol can become a major energy source and, particularly in the liver, interferes with the metabolism of other nutrients. Polymorphic variants of the genes for these enzymes encode enzymes with altered kinetic properties. The pathophysiological effects of these variants may be mediated by accumulation of acetaldehyde; high-activity ADH variants are predicted to increase the rate of acetaldehyde generation, while the low-activity ALDH2 variant is associated with an inability to metabolize this compound. The effects of acetaldehyde may be expressed either in the cells generating it, or by delivery of acetaldehyde to various tissues by the bloodstream or even saliva. Inheritance of the high-activity ADH β2, encoded by the ADH2*2 gene, and the inactive ALDH2*2 gene product have been conclusively associated with reduced risk of alcoholism. This association is influenced by gene–environment interactions, such as religion and national origin. The variants have also been studied for association with alcoholic liver disease, cancer, fetal alcohol syndrome, CVD, gout, asthma and clearance of xenobiotics. The strongest correlations found to date have been those between the ALDH2*2 allele and cancers of the oro-pharynx and oesophagus. It will be important to replicate other interesting associations between these variants and other cancers and heart disease, and to determine the biochemical mechanisms underlying the associations.
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Promden, Worrawat, Alisa S. Vangnai, Hirohide Toyama, Kazunobu Matsushita, and Piamsook Pongsawasdi. "Analysis of the promoter activities of the genes encoding three quinoprotein alcohol dehydrogenases in Pseudomonas putida HK5." Microbiology 155, no. 2 (February 1, 2009): 594–603. http://dx.doi.org/10.1099/mic.0.021956-0.
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The transcriptional regulation of three distinct alcohol oxidation systems, alcohol dehydrogenase (ADH)-I, ADH-IIB and ADH-IIG, in Pseudomonas putida HK5 was investigated under various induction conditions. The promoter activities of the genes involved in alcohol oxidation were determined using a transcriptional lacZ fusion promoter-probe vector. Ethanol was the best inducer for the divergent promoters of qedA and qedC, encoding ADH-I and a cytochrome c, respectively. Primary and secondary C3 and C4 alcohols and butyraldehyde specifically induced the divergent promoters of qbdBA and aldA, encoding ADH-IIB and an NAD-dependent aldehyde dehydrogenase, respectively. The qgdA promoter of ADH-IIG responded well to (S)-(+)-1,2-propanediol induction. In addition, the roles of genes encoding the response regulators exaE and agmR, located downstream of qedA, were inferred from the properties of exaE- or agmR-disrupted mutants and gene complementation tests. The gene products of both exaE and agmR were strictly necessary for qedA transcription. The mutation and complementation studies also suggested a role for AgmR, but not ExaE, in the transcriptional regulation of qbdBA (ADH-IIB) and qgdA (AGH-IIG). A hypothetical scheme describing a regulatory network, which directs expression of the three distinct alcohol oxidation systems in P. putida HK5, was derived.
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Zan, Rong, Ling Zhu, Gangcheng Wu, and Hui Zhang. "Identification of Novel Peptides with Alcohol Dehydrogenase (ADH) Activating Ability in Chickpea Protein Hydrolysates." Foods 12, no. 8 (April 7, 2023): 1574. http://dx.doi.org/10.3390/foods12081574.
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Alcohol dehydrogenase (ADH) is one of the main rate-limiting enzymes in alcohol metabolism. Food protein-derived peptides are thought to have ADH activating ability. We verified for the first time that chickpea protein hydrolysates (CPHs) had the ability to activate ADH and identified novel peptides from them. CPHs obtained by hydrolysis with Alcalase for 30 min (CPHs-Pro-30) showed the highest ADH activating ability, and the ADH activation rate could still maintain more than 80% after in vitro simulated gastrointestinal digestion. We have verified four peptides with activation ability to ADH: ILPHF, MFPHLPSF, LMLPHF and FDLPALRF (concentration for 50% of maximal effect (EC50): 1.56 ± 0.07 µM, 1.62 ± 0.23 µM, 1.76 ± 0.03 µM and 9.11 ± 0.11 µM, respectively). Molecular docking showed that the mechanism for activating ADH was due to the formation of a stable complex between the peptide and the active center of ADH through hydrogen bonding. The findings suggest that CPHs and peptides with ADH activating ability may be developed as natural anti-alcoholic ingredients to prevent alcoholic liver disease (ALD).
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Aquadro, C. F., H. Tachida, C. H. Langley, K. Harada, and T. Mukai. "Increased variation in ADH enzyme activity in Drosophila mutation-accumulation experiment is not due to transposable elements at the Adh structural gene." Genetics 126, no. 4 (December 1, 1990): 915–19. http://dx.doi.org/10.1093/genetics/126.4.915.
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Abstract We present here a molecular analysis of the region surrounding the structural gene encoding alcohol dehydrogenase (Adh) in 47 lines of Drosophila melanogaster that have each accumulated mutations for 300 generations. While these lines show a significant increase in variation of alcohol dehydrogenase enzyme activity compared to control lines, we found no restriction map variation in a 13-kb region including the complete Adh structural gene and roughly 5 kb of both 5' and 3' sequences. Thus, the rapid accumulation of ADH activity variation after 28,200 allele generations does not appear to have been due to the mobilization of transposable elements into or out of the Adh structural gene region.
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Johnston, C., J. B. Saunders, A. H. Barnett, B. R. Ricciardi, D. A. Hopkinson, and D. A. Pyke. "Chlorpropamide–alcohol flush reaction and isoenzyme profiles of alcohol dehydrogenase and aldehyde dehydrogenase." Clinical Science 71, no. 5 (November 1, 1986): 513–17. http://dx.doi.org/10.1042/cs0710513.
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1. To investigate the enzymatic basis of the chlorpropamide–alcohol flush reaction (CPAF) we compared the isoenzyme profiles of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) from liver biopsies, and of ALDH alone from erythrocytes and leucocytes, in CPAF-positive and CPAF-negative subjects. 2. No differences were seen in ADH or ALDH phenotypes, or in the relative activities of the isoenzymes, between the two groups before chlorpropamide was given; in particular, no subjects showed the ‘null’ ALDH phenotype that is associated with the alcohol flush reaction in oriental subjects. 3. There was a significant decrease in erythrocyte ALDH activity after 7 days' treatment with chlorpropamide in CPAF-positive individuals but no such difference was seen in CPAF-negative subjects. 4. These results indicate that CPAF has a different enzymatic basis from the alcohol flush reaction of oriental subjects and suggest that in CPAF-positive subjects erythrocyte ALDH may be particularly susceptible to inhibition by chlorpropamide.
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Kinlaw, C. S., D. E. Harry, and R. R. Sederoff. "Isolation and characterization of alcohol dehydrogenase cDNAs from Pinusradiata." Canadian Journal of Forest Research 20, no. 9 (September 1, 1990): 1343–50. http://dx.doi.org/10.1139/x90-178.
Full textAbstract:
Three alcohol dehydrogenase (ADH) cDNAs were isolated from Pinusradiata. Two of the cDNAs appear to correspond to alleles of one ADH locus, and the third cDNA appears to correspond to a second ADH locus. Nucleotide and amino acid sequences of the coding region of ADH genes from the following species were compared: Pinusradiata, Zeamays, Hordeumvulgare, Triticumaestivum, Oryza sativa, Pisumsativum, and Arabidopsisthaliana. A phylogenetic tree was constructed of coding sequences of pine and angiosperm ADH genes. This tree shows three plant ADH clusters: monocot, dicot, and pine. The distance between pine and the two angiosperms is only slightly greater than the distance between either angiosperm, supporting the fossil evidence that suggests that monocots and dicots diverged from each other shortly after angiosperms diverged from gymnosperms. The structure of pine ADH genes was investigated by Southern blot analysis. The restriction fragment pattern of ADH genes from pines is more complex than the pattern from angiosperm genes, suggesting that pine ADH genes are either larger or more numerous than their angiosperm counterparts.
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BOLLE, Xavier De, Carla VINALS, Jacques FASTREZ, and Ernest FEYTMANS. "Bivalent cations stabilize yeast alcohol dehydrogenase I." Biochemical Journal 323, no. 2 (April 15, 1997): 409–13. http://dx.doi.org/10.1042/bj3230409.
Full textAbstract:
The thermostability of yeast alcohol dehydrogenase (ADH) I is strongly dependent on the presence of NaCl, a salt that is almost neutral on the Hofmeister scale, which suggests that solvent-accessible electrostatic repulsion might play a role in the inactivation of the enzyme. Moreover, CaCl2 and MgCl2 are able to stabilize the enzyme at millimolar concentrations. Ca2+ stabilizes yeast ADH I by preventing the dissociation of the reduced form of the enzyme and by preventing the unfolding of the oxidized form of the enzyme. An analysis of several chimaeric ADHs suggests that Ca2+ is fixed by the Asp-236 and Glu-101 side chains in yeast ADH I, but that Ca2+ can be displaced by replacing Met-168 by an Arg residue, as suggested by a three-dimensional model of the enzyme structure. These results indicate that electrostatic repulsion can cause protein unfolding and/or dissociation. It is proposed that yeast ADH I binds Mg2+in vivo.
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Walker, JRL. "Spectrophotometric determination of enzyme activity: alcohol dehydrogenase (ADH)." Biochemical Education 20, no. 1 (January 1992): 42–43. http://dx.doi.org/10.1016/0307-4412(92)90021-d.
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Sheehan, M. C., C. J. Bailey, B. C. A. Dowds, and D. J. McConnell. "A new alcohol dehydrogenase, reactive towards methanol, from Bacillus stearothermophilus." Biochemical Journal 252, no. 3 (June 15, 1988): 661–66. http://dx.doi.org/10.1042/bj2520661.
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An NAD+-dependent alcohol dehydrogenase (ADH) was purified to homogeneity from an aerobic strain of Bacillus stearothermophilus, DSM 2334 (ADH 2334), and compared with the ADH from B. stearothermophilus NCA 1503 (ADH 1503). When an antibody raised against ADH 2334 was used, no cross-reactivity with ADH 1503 was observed on Western blots; by means of an enzyme-linked-immunoabsorbent-assay (‘e.l.i.s.a.’) procedure, it was found that ADH 1503 had less than 6% of the antigenic activity of ADH 2334. Amino acid analyses detected very small differences in composition, equivalent to about 40 sequence changes, between the two enzymes. The new enzyme has the same six-amino-acid N-terminal sequence as ADH 1503. ADH 2334, but not ADH 1503, is reactive towards methanol; both enzymes can oxidize ethanol, propan-1-ol, butan-1-ol and butan-2-ol. The new enzyme has a distinctive pH optimum at pH 5.5-6 and has significantly lower KEthanolm and kEthanolcat. values than those of ADH 1503. From steady-state kinetic parameters of the reaction with ethanol, propan-1-ol and butan-1-ol, it was shown that ADH 2334 has an ordered mechanism in both directions, with NAD+ being the compulsory first substrate in alcohol oxidation and NADH release being the rate-limiting step. ADH 1503 has an ordered addition of NAD+ and alcohol, but NADH release is not rate-limiting.
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Jelski, Wojciech, and Maciej Szmitkowski. "Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) in the cancer diseases." Clinica Chimica Acta 395, no. 1-2 (September 2008): 1–5. http://dx.doi.org/10.1016/j.cca.2008.05.001.
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Chenevert, S. W., N. G. Fossett, S. H. Chang, I. Tsigelny, M. E. Baker, and W. R. Lee. "Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase." Biochemical Journal 308, no. 2 (June 1, 1995): 419–23. http://dx.doi.org/10.1042/bj3080419.
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We have determined the nucleotide sequences of eight ethyl methanesulphonate-induced mutants in Drosophila alcohol dehydrogenase (ADH), of which six were previously characterized by Hollocher and Place [(1988) Genetics 116, 253-263 and 265-274]. Four of these ADH mutants contain a single amino acid change: glycine-17 to arginine, glycine-93 to glutamic acid, alanine-159 to threonine, and glycine-184 to aspartic acid. Although these mutants are inactive, three mutants (Gly17Arg, Gly93Glu and Gly184Asp) form stable homodimers, as well as heterodimers with wild-type ADH, in which the wild-type ADH subunit retains full enzyme activity [Hollocher and Place (1988) Genetics 116, 265-274]. Interestingly, the Ala159Thr mutant does not form either stable homodimers or heterodimers with wild-type ADH, suggesting that alanine-159 is important in stabilizing ADH dimers. The mutations were analysed in terms of a three-dimensional model of ADH using bacterial 20 beta-hydroxysteroid dehydrogenase and rat dihydropteridine reductase as templates. The model indicates that mutations in glycine-17 and glycine-93 affect the binding of NAD+. It also shows that alanine-159 is part of a hydrophobic anchor on the dimer interface of ADH. Replacement of alanine-159 with threonine, which has a larger side chain and can hydrogen bond with water, is likely to reduce the strength of the hydrophobic interaction. The three-dimensional model shows that glycine-184 is close to the substrate binding site. Replacement of glycine-184 with aspartic acid is likely to alter the position of threonine-186, which we propose hydrogen bonds to the carboxamide moiety of NAD+. Also, the negative charge on the aspartic acid side chain may interact with the substrate and/or residues in the substrate binding site. These mutations provide information about ADH catalysis and the stability of dimers, which may also be useful in understanding homologous dehydrogenases, which include the human 17 beta-hydroxysteroid, 11 beta-hydroxysteroid and 15-hydroxyprostaglandin dehydrogenases.
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ANIGBORO, A. A., and A. A. UWAKWE. "TEMPERATURE AND PH DEPENDENCE ACTIVITY OF CRUDE ALCOHOL DEHYDROGENASE ISOLATED FROM YEAST (Saccharomyces cerevisiae) OF Raphia hookeri AND Elaeis guineensis SAPS IN SELECTED LOCATIONS IN NIGER DELTA REGION OF NIGERIA." Nigerian Journal of Life Sciences (ISSN: 2276-7029) 5, no. 1 (March 25, 2022): 20–30. http://dx.doi.org/10.52417/njls.v5i1.204.
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Alcohol dehydrogenase (E.C 1.1.1.1) is an enzyme that catalyses the reduction of acetaldehyde to ethanol during fermentation. In this study, the activity of crude alcohol dehydrogenase (ADH) isolated from yeast (Saccharomyces cerevisiae) of fresh Raphia hookeri and Elaeis guineensis palm wine(saps) from Niger Delta region (Akwa Ibom, Bayelsa, Cross River, Delta, Edo, Imo and River States) was determined at a temperature range of 25-70°C and pH 5.0-9.0. The results showed that the activity of alcohol dehydrogenase (ADH) of yeasts from both R. hookeri and E. guineensis palm saps increased in all the states as the temperature increased from 25-30oC but decreased with further increase in temperature from 40-700C. The optimum activity of the enzyme was recorded at an optimum temperature 300C for all the locations, with yeast ADH from Delta State exhibiting the highest activity (0.00025?mole/min). The study also showed that at various temperatures (30 -70°C), the ADH activities of yeasts isolated from E. guineensis sap were higher than those from R. hookeri sap. The activity of yeast ADH from R. hookeri sap in all the locations increased with increasing pH till 8.0 and declined markedly at pH 9.0. A similar trend was observed in the activity of yeast ADH from E. guineensis sap in all the states.The optimum pH of the enzyme was found to be 8.0 in yeasts from both R. hookeri and E. guineensis saps across all the locations. It is concluded that ADH from S. cerevisae isolated from R. hookeri and E. guineensis saps in the Niger-Delta region of Nigeria could be applied by alcohol-producing industries for alcoholic fermentation at an optimum temperature 30°C and pH 8.0, especially ADH from E. guineensis sap yeasts.
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Holmes, Roger S., Roland A. H. van Oorschot, and John L. Vandeberg. "Genetics of alcohol dehydrogenase and aldehyde dehydrogenase from Monodelphis domestica cornea: further evidence for identity of corneal aldehyde dehydrogenase with a major soluble protein." Genetics Research 56, no. 2-3 (October 1990): 259–65. http://dx.doi.org/10.1017/s0016672300035369.
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SummaryA didelphid marsupial, the gray short-tailed opossum (Monodelphis domestica), was used as a model species to study the biochemical genetics of alcohol dehydrogenases (ADHs) and aldehyde dehydrogenase (ALDH) in corneal tissue. Isoelectric point variants of corneal ALDH (designated ALDH3) and a major soluble protein in corneal extracts were observed among eight families of animals used in studying the genetics of these proteins. Both phenotypes exhibited identical patterns following PAGE-IEF and were inherited in a normal Mendelian fashion, with two alleles at a single locus (ALDH3) showing codominant expression. The data provided evidence for genetic identity of corneal ALDH with this major soluble protein, and supported biochemical evidence, recently reported for purified bovine corneal ALDH, that this enzyme constitutes a major portion of soluble corneal protein (Abedinia et al. 1990). Isoelectric point variants for corneal ADH were also observed, with patterns for the two major forms (ADH3 and ADH4) and one minor form (ADH5) being consistent with the presence of two ADH subunits (designated γ and δ), and variant phenotypes existing for the γ subunit. The genetics of this enzyme was studied in the eight families, and the results were consistent with codominant expression of two alleles at a single locus (designated ADH3). It is relevant that a major detoxification function has been proposed for corneal ADH and ALDH, in the oxidoreduction of peroxidic aldehydes induced by available oxygen and UV-B light (Holmes & VandeBerg, 1986a). In addition, a direct role for corneal ALDH as a UV-B photoreceptor in this anterior eye tissue has also been proposed (Abedinia et al. 1990).
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Matzkin, Luciano M., and Walter F. Eanes. "Sequence Variation of Alcohol Dehydrogenase (Adh) Paralogs in Cactophilic Drosophila." Genetics 163, no. 1 (January 1, 2003): 181–94. http://dx.doi.org/10.1093/genetics/163.1.181.
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Abstract This study focuses on the population genetics of alcohol dehydrogenase (Adh) in cactophilic Drosophila. Drosophila mojavensis and D. arizonae utilize cactus hosts, and each host contains a characteristic mixture of alcohol compounds. In these Drosophila species there are two functional Adh loci, an adult form (Adh-2) and a larval and ovarian form (Adh-1). Overall, the greater level of variation segregating in D. arizonae than in D. mojavensis suggests a larger population size for D. arizonae. There are markedly different patterns of variation between the paralogs across both species. A 16-bp intron haplotype segregates in both species at Adh-2, apparently the product of an ancient gene conversion event between the paralogs, which suggests that there is selection for the maintenance of the intron structure possibly for the maintenance of pre-mRNA structure. We observe a pattern of variation consistent with adaptive protein evolution in the D. mojavensis lineage at Adh-1, suggesting that the cactus host shift that occurred in the divergence of D. mojavensis from D. arizonae had an effect on the evolution of the larval expressed paralog. Contrary to previous work we estimate a recent time for both the divergence of D. mojavensis and D. arizonae (2.4 ± 0.7 MY) and the age of the gene duplication (3.95 ± 0.45 MY).
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Barth, G., and W. Künkel. "Alcohol dehydrogenase (ADH) in yeasts II. NAD+-and NADP+-dependent alcohol dehydrogenases in Saccharomycopsis lipolytica." Zeitschrift für allgemeine Mikrobiologie 19, no. 6 (January 24, 2007): 381–90. http://dx.doi.org/10.1002/jobm.19790190603.
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Chen, Zhi-wei, Petra Baruch, F. Scott Mathews, Kazunobu Matsushita, Tetsuo Yamashita, Hirohide Toyama, and Osao Adachi. "Crystallization and preliminary diffraction studies of two quinoprotein alcohol dehydrogenases (ADHs): a soluble monomeric ADH from Pseudomonas putida HK5 (ADH-IIB) and a heterotrimeric membrane-bound ADH from Gluconobacter suboxydans (ADH-GS)." Acta Crystallographica Section D Biological Crystallography 55, no. 11 (November 1, 1999): 1933–36. http://dx.doi.org/10.1107/s0907444999010744.
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Crystals of a soluble monomeric quinocytochrome alcohol dehydrogenase (ADH-IIB) and of a trimeric membrane-associated quinocytochrome alcohol dehydrogenase (ADH-GS) have been obtained. The ADH-IIB crystals are triclinic, with one monomer in the unit cell, and were obtained in the presence of PEG 8000, sodium citrate, HEPES buffer and 2-propanol. X-ray data were collected at 110 K to 1.9 Å resolution (R merge = 6.4%) and the orientation of a methanol dehydrogenase search molecule (from Methylophilus methylotrophus W3A1) was obtained by molecular replacement. Preliminary refinement of this model (10.0–3.0 Å resolution, R = 0.37, R free = 0.40) led to tentative identification of the two highest peaks in a native anomalous difference Fourier map as the Fe atom of the heme and a calcium ion interacting with the PQQ prosthetic group. The ADH-GS crystals are tetragonal, displaying six similar lattices, both primitive and centered, and were grown by the sitting-drop method after replacement of Triton X-100 by dodecylmaltoside or octaethylene glycol monododecyl ether in the presence of ammonium sulfate and sodium acetate buffer, with and without PEG 3500 and calcium ion. The best diffraction is obtained at 110 K where the resolution extends to about 4 Å in the a and b directions and about 3 Å in the c direction.
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Choi, Eun-Ju, and Wi-Young So. "Effects of Exercise Intensity on Alcohol Dehydrogenase Gene Expression in the Rat Large Intestine." Journal of Men's Health 14, no. 2 (March 13, 2018): e8-e13. http://dx.doi.org/10.22374/1875-6859.14.2.2.
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Background and Objective
The aim of this study was to examine the relationship between the intensity of treadmill exercise and alcohol dehydrogenase (ADH) expression in the large intestine.
Material and Methods
Thirty Sprague-Dawley white male rats were randomly assigned to a control group (CON; no exercise), low-intensity exercise group (LIG; 30-min exercise at 8 m/min 5 times a week for 4 weeks), or high-intensity exercise group (HIG; 30-min exercise at 28 m/min 5 times a week for 4 weeks).
Results
Microarray analysis was conducted to evaluate ADH gene expression levels in large intestinal tissue, significant changes in the expression of four ADH genes (Adh1, Adh4, Adh6a, and Adh7) related to exercise intensity. In addition, pooled samples of the exercise groups showed decreased expression levels of these four genes compared with those of the control group. These findings were confirmed by reverse transcription-polymerase chain reaction. In addition, differences were detected with respect to exercise intensity: Adh1, Adh4, and Adh6a levels were significantly decreased in the LIG compared with those in the HIG, whereas Adh7 expression showed an opposite trend.
Conclusion
In conclusion, this study suggests that regular exercise can decrease the incidence of alcohol-related disease by suppressing ADH production in the digestive system.
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Wang, Caroline H., and Shiva M. Singh. "Genetic considerations in the effects of ethanol in mice. I. Genotype-dependent alterations in alcohol dehydrogenase activity." Canadian Journal of Genetics and Cytology 27, no. 2 (April 1, 1985): 158–64. http://dx.doi.org/10.1139/g85-024.
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Most genetic studies on individual and racial differences in sensitivity to alcohol intoxication have concentrated on genetic variations associated with structural genes for the enzymes involved in alcohol metabolism, including alcohol dehydrogenase (ADH; E.C. 1.1.1.1). We studied the ethanol-induced regulation of ADH following chronic administration of ethanol in mice. Newly weaned males from six inbred strains (BALB/c, C3H/HeSnJ, C3H/S, C57BL/6J, S.W., and 129/ReJ) were subjected to ethanol administration. Alterations in the level of liver ADH activity, relative to matched littermate controls, were evaluated. The change in ADH activity was found to be strain (genotype) specific, which may explain the contradictory results in the literature. Strains which showed induction of ADH activity, in general, reflected a strain-specific time-dependent profile. Strains which showed repression, however, were independent in the degree of repression to the duration of ethanol exposure. Such variable, ethanol-induced regulatory responses (induction/repression) in ADH activity of different genotypes may account for individual and population variations in response to alcohol. Additional work, however, is needed to establish the molecular bases of ADH inducibility and its specific role in relative susceptibility to alcohols.Key words: alcohol dehydrogenase, mice, ethanol effects.
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Heinstra, Pieter W. H., Willem Scharloo, and George E. W. Thörig. "Physiological Significance of the Alcohol Dehydrogenase Polymorphism in Larvae of Drosophila." Genetics 117, no. 1 (September 1, 1987): 75–84. http://dx.doi.org/10.1093/genetics/117.1.75.
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ABSTRACT This study deals with biochemical and metabolic-physiological aspects of the relationship between variation in in vivo alcohol dehydrogenase activity and fitness in larvae homozygous for the alleles Adh71k, AdhF, AdhS, of Drosophila melanogaster, and for the common Adh allele of Drosophila simulans. The Adh genotypes differ in the maximum oxidation rates of propan-2-ol into acetone in vivo. There are smaller differences between the Adh genotypes in rates of ethanol elimination. Rates of accumulation of ethanol in vivo are negatively associated with larval-to-adult survival of the Adh genotypes. The rank order of the maximum rates of the ADHs in elimination of propan-2-ol, as well as ethanol, is ADH-71k > ADH-F > ADH-S- > simulans-ADH. The ratio of this maximum rate to ADH quantity reveals the rank order of ADH-S > ADH-F > ADH-71k > simulans-ADH, suggesting a compensation for allozymic efficiency by the ADH quantity in D. melanogaster.—Our findings show that natural selection may act on the Adh polymorphism in larvae via differences in rates of alcohol metabolism.
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Birchler, J. A., J. C. Hiebert, and K. Paigen. "Analysis of autosomal dosage compensation involving the alcohol dehydrogenase locus in Drosophila melanogaster." Genetics 124, no. 3 (March 1, 1990): 677–86. http://dx.doi.org/10.1093/genetics/124.3.677.
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Abstract An example of autosomal dosage compensation involving the expression of the alcohol dehydrogenase (Adh) locus is described. Flies trisomic for a quarter of the length of the left arm of chromosome two, including Adh, have diploid levels of enzyme activity and alcohol dehydrogenase messenger RNA. Subdivision of the compensating trisomic into smaller ones revealed a region that exerts an inverse regulatory effect on alcohol dehydrogenase activity and messenger RNA levels and a smaller region surrounding the structural gene that exhibits a direct gene dosage response. The two opposing effects are of sufficient magnitude that they cancel when simultaneously present resulting in the observed compensation in the larger aneuploid. An Adh promoter-white structural gene fusion construct is affected by the inverse regulatory region indicating that the effect is mediated through the Adh promoter sequences. The role of autosomal dosage compensation in understanding aneuploid syndromes and karyotype evolution in Drosophila species is discussed.
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Chen, Wei J., E. W. Loh, Yun-Pung P. Hsu, Chiao-Chicy Chen, Jeng-Ming Yu, and Andrew T. A. Cheng. "Alcohol-Metabolising Genes and Alcoholism Among Taiwanese Han Men: Independent Effect of ADH2, ADH3 and ALDH2." British Journal of Psychiatry 168, no. 6 (June 1996): 762–67. http://dx.doi.org/10.1192/bjp.168.6.762.
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BackgroundPrevious population association studies have indicated that certain alleles of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) may reduce the risk of alcoholism in Asian populations. The association of ALDH2 and ADH2 with the development of alcoholism was found to be independent of each other and has been replicated in different Asian populations, while the effect of ADH3 is less studied.MethodWe genotyped the alcohol metabolism genes among Han men with alcohol dependence (n=46) and their ethnically matched normal controls (n=63) in Taiwan. Multiple logistic regression was then applied to assess the contribution of ADH3 to alcoholism by controlling the effect of ALDH2 and ADH2.ResultsThe results of multivariate analyses demonstrated that the odds ratios for an increment of one allele of ADH2∗1, ADH3∗2 and ALDH2∗1 in the development of alcoholism were 4.18, 3.82, and 6.89, respectively.ConclusionsThese findings clearly indicate that all three alcohol-metabolising genes contribute to susceptibility to alcoholism.
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Duan, Jinhong, Grant E. McFadden, Anthony J. Borgerding, Faye L. Norby, Bonnie H. Ren, Gang Ye, Paul N. Epstein, and Jun Ren. "Overexpression of alcohol dehydrogenase exacerbates ethanol-induced contractile defect in cardiac myocytes." American Journal of Physiology-Heart and Circulatory Physiology 282, no. 4 (April 1, 2002): H1216—H1222. http://dx.doi.org/10.1152/ajpheart.00780.2001.
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Alcoholic cardiomyopathy is characterized by impaired ventricular function although its toxic mechanism is unclear. This study examined the impact of cardiac overexpression of alcohol dehydrogenase (ADH), which oxidizes ethanol into acetaldehyde (ACA), on ethanol-induced cardiac contractile defect. Mechanical and intracellular Ca2+properties were evaluated in ventricular myocytes from ADH transgenic and wild-type (FVB) mice. ACA production was assessed by gas chromatography. ADH myocytes exhibited similar mechanical properties but a higher efficiency to convert ACA compared with FVB myocytes. Acute exposure to ethanol depressed cell shortening and intracellular Ca2+ in the FVB group with maximal inhibitions of 23.3% and 23.4%, respectively. Strikingly, the ethanol-induced depression on cell shortening and intracellular Ca2+ was significantly augmented in the ADH group, with maximal inhibitions of 43.7% and 40.6%, respectively. Pretreatment with the ADH inhibitor 4-methylpyrazole (4-MP) or the aldehyde dehydrogenase inhibitor cyanamide prevented or augmented the ethanol-induced inhibition, respectively, in the ADH but not the FVB group. The ADH transgene also substantiated the ethanol-induced inhibition of maximal velocity of shortening/relengthening and unmasked an ethanol-induced prolongation of the duration of shortening/relengthening, which was abolished by 4-MP. These data suggest that elevated cardiac ACA exposure due to enhanced ADH expression may play an important role in the development of alcoholic cardiomyopathy.
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Azmi, Liyana, Eilis C. Bragginton, Ian T. Cadby, Olwyn Byron, Andrew J. Roe, Andrew L. Lovering, and Mads Gabrielsen. "High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE." Acta Crystallographica Section F Structural Biology Communications 76, no. 9 (August 19, 2020): 414–21. http://dx.doi.org/10.1107/s2053230x20010237.
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The bifunctional alcohol/aldehyde dehydrogenase (AdhE) comprises both an N-terminal aldehyde dehydrogenase (AldDH) and a C-terminal alcohol dehydrogenase (ADH). In vivo, full-length AdhE oligomerizes into long oligomers known as spirosomes. However, structural analysis of AdhE is challenging owing to the heterogeneity of the spirosomes. Therefore, the domains of AdhE are best characterized separately. Here, the structure of ADH from the pathogenic Escherichia coli O157:H7 was determined to 1.65 Å resolution. The dimeric crystal structure was confirmed in solution by small-angle X-ray scattering.
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Mitchell, L. E., E. S. Dennis, and W. J. Peacock. "Molecular analysis of an alcohol dehydrogenase (Adh) gene from chromosome 1 of wheat." Genome 32, no. 3 (June 1, 1989): 349–58. http://dx.doi.org/10.1139/g89-454.
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We have cloned and determined the nucleotide sequence of a gene encoding alcohol dehydrogenase (Adh) from Triticum aestivum cv. Millewa. Southern analysis using cv. Chinese Spring nullisomic–tetrasomic and ditelosomic lines established that the cloned gene mapped to the long arm of chromosome 1A and does not correspond to any previously identified wheat Adh locus. Southern analysis also provided evidence for triplicate copies of this Adh gene on the homoeologous group 1 chromosomes, while Northern blots indicated that the homoeologous group 1 Adh genes, like several other plant Adh genes, are transcribed under anaerobic conditions. Sequence analysis indicates that the cloned gene has a structure similar to both monocot and dicot Adh genes with an open reading frame encoding a polypeptide of 379 amino acids. Sequences important for eucaryotic gene expression such as the TATA box, polyadenylation signal, and intron splice sites were found in the expected positions. The open reading frame is interrupted by 8 introns which are in identical positions with 8 of the 9 introns in maize and pea Adh genes, suggesting that during evolution there are processes occurring that result in the loss of introns. Sequence analysis also revealed that the cloned wheat Adh gene shared extensive homology with the barley Adh3 gene not only in the coding region but also in the noncoding regions. However, this homology is discontinuous as a result of a 1.8-kbp insertion (TLM), which is present in the cloned wheat Adh gene and absent in the barley Adh3 gene. Sequence analysis of this insertion reveals features characteristic of the short terminal inverted repeat class of eucaryotic transposable elements. We have no evidence for the transposition of the TLM element. However, Southern blots reveal multiple copies of sequences related to TLM in the wheat genome and in other closely related species, suggesting that transposition may once have played an important role in the evolution of the Gramineae family.Key words: Triticum aestivum, alcohol dehydrogenase, Adh, chromosome 1, anaerobic induction, insertion element, transposable element.
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Dolferus, R., J. C. Osterman, W. J. Peacock, and E. S. Dennis. "Cloning of the Arabidopsis and Rice Formaldehyde Dehydrogenase Genes: Implications for the Origin of Plant ADH Enzymes." Genetics 146, no. 3 (July 1, 1997): 1131–41. http://dx.doi.org/10.1093/genetics/146.3.1131.
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This article reports the cloning of the genes encoding the Arabidopsis and rice class III ADH enzymes, members of the alcohol dehydrogenase or medium chain reductase/dehydrogenase superfamily of proteins with glutathione-dependent formaldehyde dehydrogenase activity (GSH-FDH). Both genes contain eight introns in exactly the same positions, and these positions are conserved in plant ethanolactive Adh genes (class P). These data provide further evidence that plant class P genes have evolved from class III genes by gene duplication and acquisition of new substrate specificities. The position of introns and similarities in the nucleic acid and amino acid sequences of the different classes of ADH enzymes in plants and humans suggest that plant and animal class I11 enzymes diverged before they duplicated to give rise to plant and animal ethanol-active ADH enzymes. Plant class P ADH enzymes have gained substrate specificities and evolved promoters with different expression properties, in keeping with their metabolic function as part of the alcohol fermentation pathway.
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Zorzano, Antonio, Luis Ruiz del Arbol, and Emilio Herrera. "Effect of liver disorders on ethanol elimination and alcohol and aldehyde dehydrogenase activities in liver and erythrocytes." Clinical Science 76, no. 1 (January 1, 1989): 51–57. http://dx.doi.org/10.1042/cs0760051.
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1. Liver biopsies were performed in healthy control subjects and in subjects with alcoholic and non-alcoholic liver disease in order to examine alcohol dehydrogenase (ADH; EC 1.1.1.1) and aldehyde dehydrogenase [ALDH; aldehyde dehydrogenase (NAD+); EC 1. 2. 1. 3] activities. Erythrocyte ALDH and ethanol metabolism were also investigated in the same subjects. 2. Fifteen per cent of the subjects studied (seven of 48 subjects tested) presented atypical ADH activity, characterized by elevated activity at pH 7.4 or 8.8 compared with that found in subjects with the usual ADH form. However, the ethanol elimination curves obtained in two subjects with atypical ADH were indistinguishable from the kinetics of the group with normal ADH. Subjects displaying atypical ADH activity showed normal liver and erythrocyte ALDH activities. 3. Considering only the subjects with the normal ADH form, hepatic ADH activity was unaltered in subjects with non-alcoholic liver disease (chronic hepatitis or cirrhosis) and in those with alcoholic steatosis. Subjects with alcoholic hepatitis or alcoholic cirrhosis showed a lower ADH activity compared with the healthy control group. 4. In spite of the changes detected in subjects with alcoholic liver disease, curves of blood ethanol concentration after oral administration of 0.4 g of ethanol/kg were indistinguishable between the alcoholic hepatitis group and the control group. 5. Hepatic ALDH activity, assayed at 300 μmol/l acetaldehyde, was found to be diminished in all liver pathologies investigated, regardless of their aetiology. Nevertheless, erythrocyte ALDH activity was not modified in subjects with non-alcoholic or alcoholic liver disease. As a result of these findings, no relationship was found between hepatic and erythrocyte ALDH. 6. In summary, our data demonstrate that (a) marked modifications in ADH activity, as found in patients with atypical ADH or in subjects with alcoholic liver disease, are not accompanied by parallel alterations in the kinetics of ethanol disappearance, suggesting that ADH activity per se does not limit ethanol metabolism in vivo, (b) hepatic high-Km ALDH activity is decreased in patients with liver disease independent of alcoholism, and therefore decreased ALDH activity cannot be considered as a primary defect in alcoholism but as a consequence of liver damage, and (c) erythrocyte ALDH does not reflect hepatic high-Km ALDH.
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Wee, Ching Ching, and Hairul Azman Roslan. "Isolation of Alcohol Dehydrogenase cDNA and Basal Regulatory Region from Metroxylon sagu." ISRN Molecular Biology 2012 (August 26, 2012): 1–9. http://dx.doi.org/10.5402/2012/839427.
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Alcohol dehydrogenase (Adh) is a versatile enzyme involved in many biochemical pathways in plants such as in germination and stress tolerance. Sago palm is plant with much importance to the state of Sarawak as one of the most important crops that bring revenue with the advantage of being able to withstand various biotic and abiotic stresses such as heat, pathogens, and water logging. Here we report the isolation of sago palm Adh cDNA and its putative promoter region via the use of rapid amplification of cDNA ends (RACE) and genomic walking. The isolated cDNA was characterized and determined to be 1464 bp long encoding for 380 amino acids. BLAST analysis showed that the Adh is similar to the Adh1 group with 91% and 85% homology with Elaeis guineensis and Washingtonia robusta, respectively. The putative basal msAdh1 regulatory region was further determined to contain promoter signals of TATA and AGGA boxes and predicted amino acids analyses showed several Adh-specific motifs such as the two zinc-binding domains that bind to the adenosine ribose of the coenzyme and binding to alcohol substrate. A phylogenetic tree was also constructed using the predicted amino acid showed clear separation of Adh from bacteria and clustered within the plant Adh group.
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Yuan, Chuanxun, Yan Li, Qingchuan Li, Risheng Jin, and Lili Ren. "Purification of Tea saponins and Evaluation of its Effect on Alcohol Dehydrogenase Activity." Open Life Sciences 13, no. 1 (April 10, 2018): 56–63. http://dx.doi.org/10.1515/biol-2018-0008.
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AbstractTea saponins, extracted from a Camellia oleifera cake, were found to have a potent effect on de-alcoholic activity. To obtain highly pure tea saponins, which can better maintain the activity of alcohol dehydrogenase (ADH), this paper presents an extraction method for tea saponins using deionized water as the extraction agent and a two-stage precipitation method, including ethanol precipitation and CaO precipitation. The optimum conditions for ethanol precipitation were 95% alcohol, a duration of 1.5h and a solid/liquid ratio of 1:4; while the optimum conditions for CaO precipitation were a duration of 2h and an NH4HCO3/CaO ratio of 2:1. Under the optimum conditions, the content of saponins was 87.58%. The results showed that the greater the amount of tea saponins and the higher its purity, the more significant its activating effect on ADH. When the purity of tea saponins was above 75%, it activated ADH. It indicated that the de-alcoholic mechanism of tea saponins is associated with the activity of ADH. Furthermore, the study characterized the structure of tea saponins by UV absorption and Fourier Transform Infrared (FTIR) spectrometry and LC-MS.
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Colic, Slavica, Vera Rakonjac, Milica Fotiric-Aksic, Dragan Nikolic, Vladislav Ognjanov, and Dragan Rahovic. "Dehydrogenase isoenzyme polymorphism in genus Prunus, subgenus Cerasus." Genetika 44, no. 3 (2012): 619–32. http://dx.doi.org/10.2298/gensr1203619c.
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Dehydrogenase polymorphism was studied in 36 sour cherry (Prunus cerasus L.), sweet cherry (Prunus avuim L.), mahaleb (Prunus mahaleb L.), ground cherry (Prunus fruticosa Pall.), duke cherry (Prunus gondounii Redh.), Japanese flowering cherry (Prunus serrulata Lindl.) and four iterspecific hybrids (standard cherry rootstocks ?Gisela 5?, ?Gisela 6?, ?Max Ma? and ?Colt?). Inner bark of one-year-old shoots, in dormant stage, was used for enzyme extraction. Vertical PAGE was used for isoenzyme analysis: alcohol dehydrogenase (ADH), formate dehydrogenase (FDH), glutamate dehydrogenase (GDH), isocitrate dehydrogenaze (IDH), malate dehydrogenase (MDH), phosphogluconate dehydrogenase (PGD), and shikimate dehydrogenase (SDH). All studied systems were polymorphic at 10 loci: Adh -1 (3 genotypes) and Adh-2 (5 genotypes), Fdh-1 (2 genotypes), Gdh-1 (3 genotypes), Idh-1 (4 genotypes) i Idh -2 (5 genotypes), Mdh-1 (3 genotypes), Pgd-1 (4 genotypes), Sdh-1 (1 genotype) i Sdh-2 (3 genotypes). Cluster analysis was used to construct dendrogram on which four groups of similar genotypes were separated. Obtained results indicate that studied enzyme systems can be used for determination of genus Prunus, subgenus Cerasus. Among studied enzyme systems ADH, IDH and SDH were the most polymorphic and most useful to identify genetic variability. Polymorphism of FDH and GDH in genus Prunus, subgenus Cerasus was described first time in this work. First results for dehydrogenase variability of Oblacinska indicate that polymorphism of loci Idh-2 and Sdh-2 can be useful for discrimination of different clones.
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Rowan, Robert G., Mark D. Brennan, and W. J. Dickinson. "DEVELOPMENTALLY REGULATED RNA TRANSCRIPTS CODING FOR ALCOHOL DEHYDROGENASE IN DROSOPHILA AFFINIDISJUNCTA." Genetics 114, no. 2 (October 1, 1986): 405–33. http://dx.doi.org/10.1093/genetics/114.2.405.
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ABSTRACT The organization of the gene coding for alcohol dehydrogenase (Adh) in Drosophila affinidisjuncta has been determined by physically mapping Adh RNA transcripts to cloned genomic DNA. Two distinct transcript types accumulate with developmental specificity. Because only a single genomic Adh locus is detected in D. affinidisjuncta, and since all Adh transcripts appear to be identical except at their termini, the two Adh RNA types are products of the same gene. One type of transcript, abundant in adults, contains a small 5' terminal exon that is completely lacking in the other type of transcript, which accumulates in larvae. This 5' end difference suggests that the D. affinidisjuncta Adh gene, like the homologous gene from the distantly related species D. melanogaster, is expressed from two promoters. According to the transcription map, these D. affinidisjuncta promoters are separated by approximately 560 base pairs of genomic DNA sequence. D. affinidisjuncta Adh transcripts also resemble D. melanogaster Adh transcripts in both their overall organization and their developmental distribution. Multiple 3' ends are responsible for the size heterogeneity of both types of D. affinidisjuncta Adh RNA, and some of these also appear with stage specificity.
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Mitchell, William C., and Gojko Jelenkovic. "NAD-DEPENDENT AND NADP-DEPENDENT ALCOHOL DEHYDROGENASE ENZYMES: ANALYSIS OF THEIR FUNCTIONAL SIGNIFICANCE IN STRAWBERRY FRUITS." HortScience 27, no. 6 (June 1992): 654c—654. http://dx.doi.org/10.21273/hortsci.27.6.654c.
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Assays of enzyme activity, in vivo inhibition studies and the developmental analysis of strawberry (Fragaria × ananassa Duch.) fruit alcohol dehydrogenases (ADH) suggest that both the NAD-(E.C. 1.1.1.1) and the NADP-dependent (E.C. 1.1.1.2) forms of ADH enzymes play integral roles in the development and ripening of fruits. One role of ADH enzymes appears to be the evocation of changes in sugar, soluble solids, acidity and volatile compounds necessary for the normal organoleptic character of strawberry fruits. The data presented includes: 1.) The wide substrate specificity of both ADH enzymes for the “fragrance and flavor alcohols and aldehydes” synthesized by ripe strawberry fruits, 2.) the effect of inhibitors of ADH activity upon strawberry fruit ripening, and 3.) the comparative regulation of NAD- and NADP-ADH enzymes including 4.) the developmental control of ADH enzymes in strawberry fruits.