ArticleJournal of industrial microbiology & biotechnology2017
Determining the roles of the three alcohol dehydrogenases (AdhA, AdhB and AdhE) in Thermoanaerobacter ethanolicus during ethanol formation.
Article in Journal of industrial microbiology & biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- A thermostable Cas9-based genome editing system for thermophilic acetogenic bacteriumApplied and environmental microbiology · 2025Article
- Expression and characterization of monofunctional alcohol dehydrogenase enzymes inMetabolic engineering communications · 2024Article
- Biofuel production from lignocellulose via thermophile-based consolidated bioprocessing.Engineering microbiology · 2024Review
- Alcohol dehydrogenases AdhE and AdhB with broad substrate ranges are important enzymes for organic acid reduction in Thermoanaerobacter sp. strain X514.Biotechnology for biofuels · 2021Article
- Influence of Culture Conditions on the Bioreduction of Organic Acids to Alcohols byMicroorganisms · 2021Article
- Genome Editing of the Anaerobic Thermophile Thermoanaerobacter ethanolicus Using Thermostable Cas9.Applied and environmental microbiology · 2020Article
- Branched-chain amino acid catabolism of Thermoanaerobacter pseudoethanolicus reveals potential route to branched-chain alcohol formation.Extremophiles : life under extreme conditions · 2020Article
- Ethanol Dehydrogenase I Contributes to Growth and Sporulation Under Low Oxygen Condition via Detoxification of Acetaldehyde inFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermoanaerobacter ethanolicus is a promising candidate for biofuel production due to the broad range of substrates it can utilize and its high ethanol yield compared to other thermophilic bacteria, such as Clostridium thermocellum. Three alcohol dehydrogenases, AdhA, AdhB and AdhE, play key roles in ethanol formation. To study their physiological roles during ethanol formation, we deleted them separately and in combination. Previously, it has been thought that both AdhB and AdhE were bifunctional alcohol dehydrogenases. Here we show that AdhE has primarily acetyl-CoA reduction activity (ALDH) and almost no acetaldehyde reduction (ADH) activity, whereas AdhB has no ALDH activity and but high ADH activity. We found that AdhA and AdhB have similar patterns of activity. Interestingly, although deletion of both adhA and adhB reduced ethanol production, a single deletion of either one actually increased ethanol yields by 60-70%.
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