ArticleNature communications2019
Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 72 citations in OpenAlex.
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- Membrane vesicle production via cell-to-cell communication-induced autolysis inMicrobiology spectrum · 2025Article
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- The role of AdhE mutations inJournal of bacteriology · 2025Article
- LAP-Hsp60 complex modulates epithelial tight junction barrier.Research square · 2025Article
- Multidimensional Engineering of Escherichia coli for Efficient Adipic Acid Synthesis From Cyclohexane.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Identifying microbial functional guilds performing cryptic organotrophic and lithotrophic redox cycles in anaerobic granular biofilms.PloS one · 2025Article
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- The role of AdhE on ethanol tolerance and production in Clostridium thermocellum.The Journal of biological chemistry · 2024Article
- Evolutionary paths toward multi-level convergence of lactic acid bacteria in fructose-rich environments.Communications biology · 2024Article
- A Versatile Aldehyde: Ferredoxin Oxidoreductase from the Organic Acid ReducingInternational journal of molecular sciences · 2024Article
- Structural Insight into the Catalytic Mechanisms of an L-Sorbosone Dehydrogenase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aldehyde-alcohol dehydrogenase (AdhE) is a key enzyme in bacterial fermentation, converting acetyl-CoA to ethanol, via two consecutive catalytic reactions. Here, we present a 3.5 Å resolution cryo-EM structure of full-length AdhE revealing a high-order spirosome architecture. The structure shows that the aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase (ADH) active sites reside at the outer surface and the inner surface of the spirosome respectively, thus topologically separating these two activities. Furthermore, mutations disrupting the helical structure abrogate enzymatic activity, implying that formation of the spirosome structure is critical for AdhE activity. In addition, we show that this spirosome structure undergoes conformational change in the presence of cofactors. This work presents the atomic resolution structure of AdhE and suggests that the high-order helical structure regulates its enzymatic activity.
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