• Journal of Microbiology
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• v.33 no.2
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• pp.126-127
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• 1995

A Zymomonas mobilis DNA fragment consisting of 207 nucleotides, which corresponded to the 5'-flanking region of an adhB gene encoding alcohol dehydrogenase II, was fused to the structural gene coding for a Bacillus endo-.betha.--1, 4-glucanase. The Z. mobilis DNA framgment waw identified to promote 50-fold increase in the expression of endo-.betha.1. 4 glucanase gene in Escherichia coli.

• Microbiology and Biotechnology Letters
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• v.17 no.4
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• pp.301-306
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• 1989

A genomic library of Zymomonas mobilis DNA was constructed in Escherichia coli using plasmid pUC9 Allyl alcohol was used to screen a genomic clone expressing alcohol dehydrogenase. The plasmids isolated from two clones, which were sensitive to allyl alcohol, were found to be related and to share a common 2.6 kb fragment encoding alcohol dehydrogenase II identified as one of two isozymes in Z. mobilis by staining for alcohol dehydrogenase activity on polyacrylamide gel and spectrophotometric analysis of several substrate oxidations.

• Journal of Plant Biotechnology
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• v.38 no.1
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• pp.77-86
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• 2011

Alcohol dehydrogenase (E.C.1.1.1.1) is an enzyme present in higher plants involved in the anaerobic fermentation pathway that catalyzes the reduction of pyruvate to ethanol, resulting in continuous $NAD^+$ regeneration. It also plays an important role in many plant developments including tolerance to anoxia condition. Here, a cDNA clone encoding alcohol dehydrogenase (ADH) was isolated from Chinese cabbage (Brassica rapa) seedlings. The gene named Bradh1 had a total length of 1,326 bp that contains a single open reading frame of 1,140 bp. The predicted protein consists of 379 amino acid residues with a calculated molecular mass of 41.17 kDa. Expression pattern analysis revealed a tissue-specific expressing gene in different tissues and strongly expressed in the shoot, roots and seeds of Chinese cabbage. Agrobacterium transformation of full-length cDNA Bradh1 into rice Gopumbyeo showed high efficiency. Furthermore, induction of ADH in transgenic rice enhanced tolerance to anaerobiosis stresses and elevated mRNA transcripts. The overexpression of Bradh1 in rice increases germination under anaerobiosis stresses, implying the possibility of developing new varieties suited for direct seeding or flood-prone rice field.

• Environmental Analysis Health and Toxicology
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• v.24 no.2
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• pp.107-117
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• 2009

Metal pollution of aquatic ecosystems is a problem of economic and health importance. Information regarding molecular responses to metal exposure is sorely needed in order to identify potential biomarkers. To determine the effects of heavy metals on chironomids, the full-length cDNA of alcohol dehydrogenase (ADH3) from Chironomus riparius was determined through molecular cloning and rapid amplification of cDNA ends (RACE). The expression of ADH3 was analyzed under various cadmium and copper concentrations. A comparative and phylogenetic study among different orders of insects and vertebrates was carried out through analysis of sequence databases. The complete cDNA sequence of the ADH3 gene was 1134 bp in length. The sequence of C. riparius ADH3 shows a low degree of amino acid identity (around 70%) with homologous sequences in other insects. After exposure of C. riparius to various concentrations of copper, ADH3 gene expression significantly decreased within 1 hour. The ADH3 gene expression was also suppressed in C. riparius after cadmium exposure for 24 hour. However, the effect of cadmium on ADH3 gene expression was transient in C. riparius. The results show that the suppression of ADH3 gene by copper exposure could be used as a possible biomarker in aquatic environmental monitoring and imply differential toxicity to copper and cadmium in C. riparius larvae.

• Korean Journal of Microbiology
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• v.28 no.3
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• pp.181-187
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• 1990

STA gene coding glucoamylase was introduced into haploid Saccharomyces cerevisiae SHY3 and polyploid Saccharomyces cerevisiae 54. We constructed the recombinant plasmid by substituting the promoter region of alcohol dehydrogenase isoenzyme I gene for that of STA gene to increase the expression of STA gene and found that the activity of glucoamylase was increased in transformants. The plasmid stability was improved remarkably when we got the STA gene into the plasmid which had centromere. The activity of glucoamylase and transformation frequency of it, however, was decreased because of low copy number. Industrial polyploid strain was transformed with the recombinant plasmid having the $2\mu$ origin of replication and STA gene. It produced more alcohol than host when fermented in liquefied starch media. The industrial strain, however, was not transformed with the autonomously replicating plasmid containing centromere.

• Analytical Science and Technology
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• v.12 no.6
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• pp.565-570
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• 1999

The alcohol dehydrogenase (ADH) gene from Bacillus stearothermopilus was amplified by the polymerase chain reaction. The amplified DNA was inserted into the expression vector pGEX-KG, and expressed it as a fusion protein with glutathione S-transferase (GST) in E. coli. The recombinant ADH was produced by induction with 1 mM isopropyl-${\beta}$-D-thiogalactopyranoside at $37^{\circ}C$ and purified by glutathione affinity chromatography. The recombinant ADH exhibited high substrate specificity for ethanol. The activity of the recombinant ADH proceeded optimally at pH 9.0 and $70^{\circ}C$. The recombinant ADH was highly stable against high temperature. This thermostable alcohol dehydrogenase can be used for the enzymatic determination of alcohol and for the industrial production of alcohol.

• Microbiology and Biotechnology Letters
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• v.18 no.3
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• pp.268-272
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• 1990

The structural gene (zadhII) encoding an alcohol dehydrogenase II from Zyrnornonas mobilis was cloned into Escherichia coli in our laboratory (Yoon et al., 1989. Kor. J. Microbiol. Biotechnol.). From E. coli (pADS93) carrying the zadhII gene, the Z mobilis alcochol dehydrogenase II (ZADH-II) was purified by sonication, $(NH_4)_2SO_4$, fractionation, and chromatography. The ZADH-I1 enzyme produced by Z. mobilis cell was also purified to compare to the enzyme produced by E. coli (pADS93). The purified enzyme from cell extract of E. coli (pADS93) was identified to be a tetramer being composed of four identical subunits having molecular weight of 40, 000 dalton like that of Z. mobilis. The pH optimum for the reaction oxidizing ethanol to acetaldehyde was 10.0 while the optimum for the reverse reaction was 7.5-8.5. The apparent $K_m$ values for ethanol and NAD + were $1.2 \times 10^{-1}M$and $5.1\times 10^{-5}M$, respectively. In addition, it was found that the $K_m$ value for acetaldehyde was very lower than that for ethanol.

• Korean Journal of Medicinal Crop Science
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• v.17 no.4
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• pp.266-272
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• 2009

Cinnamyl alcohol dehydrogenase (CAD, EC 1.1.1.95), catalyzes the reduction of hydroxycinnamaldehydes to give hydroxycinnamyl alcohols, or "monolignols," the monomeric precursors of lignin. Lignins are important components of cell walls and lignified secondary cell walls play crucial roles in long distance transport of water and nutrients during plant growth and development and in plant defense against biotic and abiotic stresses. Here a cDNA clone containing a CAD gene, named as PgCAD, was isolated from a commercial medicinal plant Panax ginseng. PgCAD is predicted to encode a precursor protein of 177 amino acid residues, and its sequence shares high homology with a number of other plant CADS. The expression of PgCAD in adventitious roots and hairy roots of P. ginseng was analyzed using reverse transcriptase (RT)-PCR under various abiotic stresses such as salt, salicylic acid, wounding and chilling treatment that triggered a significant induction of PgCAD at different time points within 2-48 h post-treatment. This study revealed that PgCAD may help the plants to survive against various abiotic stresses.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.521.3-522
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• 1986

A gene encoding alcohol dehydrogenase (ADH) in Zymomonas mobilis was cloned into E. coli JM 83 with plasmid pUC 9. The ADH produced by the E. coli transformant was purified bysonication, (NH$^4$)2SO4 fractionation, Affi-Gel blue and hydroxylapatite chromatography. The ADH produced by Z. mobilis was also purified by the same procedures. The two enzyme preparations were characterized and compared. It was found that the E. coli ADH was identical to one of two ADH isozymes of Z. mobilis. Analytical gel filtrations led to the conclusion that the molecule of E. coli ADH was composedv of four subunits having molecular weight of 40,000 (+1,000) dalton each The effect of metal ions on ADH activity and optimum pH were investigated.

• Proceedings of the Zoological Society Korea Conference
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• 2000.04a
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• pp.50.2-50
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• 2000

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