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

Acetaldehyde–alcohol dehydrogenase (AdhE) converts acetyl-CoA to ethanol and is a key enzyme in bacterial alcoholic fermentation. AdhE forms spirosomes and, here, the authors present the cryoEM structures of compact and extended E.coli AdhE spirosomes and show that the extended conformation is the c...

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Autores principales: Pauline Pony, Chiara Rapisarda, Laurent Terradot, Esther Marza, Rémi Fronzes
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/07fa1f5397a148c884f80a53704a93fe
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spelling oai:doaj.org-article:07fa1f5397a148c884f80a53704a93fe2021-12-02T17:31:09ZFilamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation10.1038/s41467-020-15214-y2041-1723https://doaj.org/article/07fa1f5397a148c884f80a53704a93fe2020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15214-yhttps://doaj.org/toc/2041-1723Acetaldehyde–alcohol dehydrogenase (AdhE) converts acetyl-CoA to ethanol and is a key enzyme in bacterial alcoholic fermentation. AdhE forms spirosomes and, here, the authors present the cryoEM structures of compact and extended E.coli AdhE spirosomes and show that the extended conformation is the catalytically active form of the enzyme and discuss mechanistic implications.Pauline PonyChiara RapisardaLaurent TerradotEsther MarzaRémi FronzesNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Pauline Pony
Chiara Rapisarda
Laurent Terradot
Esther Marza
Rémi Fronzes
Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation
description Acetaldehyde–alcohol dehydrogenase (AdhE) converts acetyl-CoA to ethanol and is a key enzyme in bacterial alcoholic fermentation. AdhE forms spirosomes and, here, the authors present the cryoEM structures of compact and extended E.coli AdhE spirosomes and show that the extended conformation is the catalytically active form of the enzyme and discuss mechanistic implications.
format article
author Pauline Pony
Chiara Rapisarda
Laurent Terradot
Esther Marza
Rémi Fronzes
author_facet Pauline Pony
Chiara Rapisarda
Laurent Terradot
Esther Marza
Rémi Fronzes
author_sort Pauline Pony
title Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation
title_short Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation
title_full Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation
title_fullStr Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation
title_full_unstemmed Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation
title_sort filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase adhe is essential for substrate channeling and enzymatic regulation
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/07fa1f5397a148c884f80a53704a93fe
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AT chiararapisarda filamentationofthebacterialbifunctionalalcoholaldehydedehydrogenaseadheisessentialforsubstratechannelingandenzymaticregulation
AT laurentterradot filamentationofthebacterialbifunctionalalcoholaldehydedehydrogenaseadheisessentialforsubstratechannelingandenzymaticregulation
AT esthermarza filamentationofthebacterialbifunctionalalcoholaldehydedehydrogenaseadheisessentialforsubstratechannelingandenzymaticregulation
AT remifronzes filamentationofthebacterialbifunctionalalcoholaldehydedehydrogenaseadheisessentialforsubstratechannelingandenzymaticregulation
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