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Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation

Author

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  • Pauline Pony

    (University of Bordeaux
    University of Bordeaux)

  • Chiara Rapisarda

    (University of Bordeaux
    University of Bordeaux
    UCB Celltech)

  • Laurent Terradot

    (Institut de Biologie et Chimie des Protéines, CNRS-Université de Lyon)

  • Esther Marza

    (University of Bordeaux
    University of Bordeaux)

  • Rémi Fronzes

    (University of Bordeaux
    University of Bordeaux)

Abstract

Acetaldehyde–alcohol dehydrogenase (AdhE) enzymes are a key metabolic enzyme in bacterial physiology and pathogenicity. They convert acetyl-CoA to ethanol via an acetaldehyde intermediate during ethanol fermentation in an anaerobic environment. This two-step reaction is associated to NAD+ regeneration, essential for glycolysis. The bifunctional AdhE enzyme is conserved in all bacterial kingdoms but also in more phylogenetically distant microorganisms such as green microalgae. It is found as an oligomeric form called spirosomes, for which the function remains elusive. Here, we use cryo-electron microscopy to obtain structures of Escherichia coli spirosomes in different conformational states. We show that spirosomes contain active AdhE monomers, and that AdhE filamentation is essential for its activity in vitro and function in vivo. The detailed analysis of these structures provides insight showing that AdhE filamentation is essential for substrate channeling within the filament and for the regulation of enzyme activity.

Suggested Citation

  • Pauline Pony & Chiara Rapisarda & Laurent Terradot & Esther Marza & Rémi Fronzes, 2020. "Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15214-y
    DOI: 10.1038/s41467-020-15214-y
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    Cited by:

    1. Eric M. Lynch & Heather Hansen & Lauren Salay & Madison Cooper & Stepan Timr & Justin M. Kollman & Bradley A. Webb, 2024. "Structural basis for allosteric regulation of human phosphofructokinase-1," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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