ArticleThe Journal of biological chemistry2024
The role of AdhE on ethanol tolerance and production in Clostridium thermocellum.
Article in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Impact of alcohol on gut microbial metabolism and the gut-liver-brain axis.Alcohol (Fayetteville, N.Y.) · 2026Review
- Effects of heterologous expression of glycolysis enzymes on product formation inMetabolic engineering communications · 2026Article
- Visual exoproteomics ofbioRxiv : the preprint server for biology · 2026Article
- Genetic and metabolic drivers of membrane remodeling inmSystems · 2026Article
- Article
- Endogenous Ethanol Metabolism and Development of MASLD-MASH.International journal of molecular sciences · 2025Review
- Toxicity reduction in continuous, high productivity ethanol fermentation by Parageobacillus thermoglucosidasius using in situ microbubble gas stripping.Microbial cell factories · 2025Article
- The role of AdhE mutations inJournal of bacteriology · 2025Article
- Pyrophosphate-free glycolysis in Clostridium thermocellum increases both thermodynamic driving force and ethanol titers.Biotechnology for biofuels and bioproducts · 2024Article
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Authors and funding
9 authors.
Funding
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Abstract
Many anaerobic microorganisms use the bifunctional aldehyde and alcohol dehydrogenase enzyme, AdhE, to produce ethanol. One such organism is Clostridium thermocellum, which is of interest for cellulosic biofuel production. In the course of engineering this organism for improved ethanol tolerance and production, we observed that AdhE was a frequent target of mutations. Here, we characterized those mutations to understand their effects on enzymatic activity, as well ethanol tolerance and product formation in the organism. We found that there is a strong correlation between NADH-linked alcohol dehydrogenase (ADH) activity and ethanol tolerance. Mutations that decrease NADH-linked ADH activity increase ethanol tolerance; correspondingly, mutations that increase NADH-linked ADH activity decrease ethanol tolerance. We also found that the magnitude of ADH activity did not play a significant role in determining ethanol titer. Increasing ADH activity had no effect on ethanol titer. Reducing ADH activity had indeterminate effects on ethanol titer, sometimes increasing and sometimes decreasing it. Finally, this study shows that the cofactor specificity of ADH activity was found to be the primary factor affecting ethanol yield. We expect that these results will inform efforts to use AdhE enzymes in metabolic engineering approaches.
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