Characterization of the two alcohol dehydrogenases of Zymomonas mobilis

Wills, Christopher; Kratofil, Paul; Londo, David; Martin, Tracy

doi:10.1016/0003-9861(81)90245-9

Cited by 75 publications

(54 citation statements)

References 16 publications

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“…mobilis AdhB has high specificity for ethanol over acetaldehyde [22] as a substrate [22,25,26], thus, it is thought to be involved in ethanol degradation [22] and may be important for lowering the ethanol level inside cells. Active staining experiments indicated that the AdhB activity significantly increased in the stationary phase, where ethanol was accumulated.…”

Section: Discussionmentioning

confidence: 99%

Thermotolerant Zymomonas mobilis: Comparison of Ethanol Fermentation Capability with that of an Efficient Type Strain

Sootsuwan¹,

Irie²,

Murata³

et al. 2007

TOBIOTJ

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Abstract:Zymomonas mobilis is an alternative microorganism to Saccharomyces cerevisiae for ethanol production. To find a thermotolerant Z. mobilis strain, the growth and ethanol production of four isolates in Thailand were compared with those of the efficient strain ZM4 (NRRL B-14023) at different temperatures. One of the selected strains, TISTR 405, was found to grow and produce ethanol even at 39˚C to an extent similar to that at 30˚C, and the growth and ethanol productivity at 39˚C were better than those of ZM4 at 30˚C, suggesting that TISTR 405 is suitable for ethanol fermentation at high temperatures. Analysis of genes directly related to ethanol formation or degradation, adhA, adhB and pdc, encoding alcohol dehydrogenase (Adh) A, AdhB and pyruvate decarboxylase, respectively, revealed that these genes were highly conserved in both strains. Comparison of their gene expression and activity of the products in both TISTR 405 and ZM4 at different temperatures or growth phases indicated that there was not a great difference at the transcriptional level, but the total activity of AdhA and AdhB in TISTR 405 was higher than that in ZM4. Both strains showed a significant increase in AdhB activity in the stationary phase.

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Section: Discussionmentioning

confidence: 99%

Thermotolerant Zymomonas mobilis: Comparison of Ethanol Fermentation Capability with that of an Efficient Type Strain

Sootsuwan¹,

Irie²,

Murata³

et al. 2007

TOBIOTJ

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“…Zymomonas mobilis, an O 2 -tolerant and obligately ethanologenic anaerobe (62), has two alcohol oxidoreductases, one is Fe 2ϩ -dependent and the other dependent on Zn 2ϩ (16,(63)(64)(65). As one would expect, the Zn 2ϩ enzyme is MCO-resistant, but the Fe 2ϩ enzyme is susceptible to MCO damage (66).…”

Section: Discussionmentioning

confidence: 99%

Evolution of an Escherichia coli Protein with Increased Resistance to Oxidative Stress

Lü¹,

Cabiscol²,

Obradors³

et al. 1998

Journal of Biological Chemistry

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-dependent enzyme which is subject to metalcatalyzed oxidation (MCO). Mutants acquiring the ability to grow aerobically on propanediol as sole carbon and energy source can be readily selected. These mutants express the fucO gene constitutively, as a result of an IS5 insertion in the promoter region. In this study we show that continued selection for aerobic growth on propanediol resulted in mutations in the oxidoreductase conferring increased resistance to MCO. In two independent mutants, the resistance of the protein was respectively conferred by an Ile 7 3 Leu and a Leu 8 3 Val substitution near the NAD-binding consensus amino acid sequence. A site-directed mutant protein with both substitutions showed an MCO resistance greater than either mutant protein with a single amino acid change.

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“…The former is as a zinc-dependent enzyme [7] with strong similarity to other bacterial alcohol dehydrogenases [8,91 and therefore to the zinc-dependent enzymes of yeast, mammals and plants [lo]. In contrast, ZADH I1 is a novel type of alcohol dehydrogenase.…”

mentioning

confidence: 99%

“…In contrast, ZADH I1 is a novel type of alcohol dehydrogenase. It has a high specificity for ethanol [7], requires ferrous ion for activity [8], and shows no obvious sequence similarity to other dehydrogenases, except ADH IV from yeast, which also appears to require a ferrous ion for catalytic activity [ I l , 121.…”

mentioning

confidence: 99%

The stereospecificity of the ferrous‐ion‐dependent alcohol dehydrogenase from Zymomonas mobilis

Glasfeld

Benner

1989

European Journal of Biochemistry

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Alcohol dehydrogenase from Zymomonus mobilis has been found to transfer the pro-R hydrogen of NADH to acetaldehyde. This is the first report of the stereospecificity of a dehydrogenase in the mechanistic and structural class of Fez +-dependent alcohol dehydrogenases and offers an opportunity to expand mechanistic hypotheses relating stereospecificity, reaction mechanism and reaction thermodynamics in dehydrogenases.

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Characterization of the two alcohol dehydrogenases of Zymomonas mobilis

Cited by 75 publications

References 16 publications

Thermotolerant Zymomonas mobilis: Comparison of Ethanol Fermentation Capability with that of an Efficient Type Strain

Thermotolerant Zymomonas mobilis: Comparison of Ethanol Fermentation Capability with that of an Efficient Type Strain

Evolution of an Escherichia coli Protein with Increased Resistance to Oxidative Stress

The stereospecificity of the ferrous‐ion‐dependent alcohol dehydrogenase from Zymomonas mobilis

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