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Literature summary for 1.1.1.1 extracted from

  • Pony, P.; Rapisarda, C.; Terradot, L.; Marza, E.; Fronzes, R.
    Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation (2020), Nat. Commun., 11, 1426 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene adhe, eecombinant expression of N-terminally His6-tagged AdhE in Escherichia coli strain Bl21 Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information the enzyme occurs in an oligomeric form called spirosomes Escherichia coli
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetaldehyde + NADH + H+ Escherichia coli
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ethanol + NAD+
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r
additional information Escherichia coli the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate ?
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Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9Q7
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged AdhE from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + NADH + H+
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Escherichia coli ethanol + NAD+
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r
additional information the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate Escherichia coli ?
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-

Subunits

Subunits Comment Organism
oligomer the enzyme occurs in an oligomeric form called spirosomes. Incubation with NAD+ and Fe2+ is sufficient to extend the filaments. The addition of coenzyme A does not impair the conformational change triggered by NAD+ and Fe2+. In the same conditions, NADH and Fe2+ are not able to trigger a conformational change from the compact to the extended form. CryoEM analysis of the AdhE spirosomes in their compact and extended forms, enzyme filaments and quarternary structure analysis, overview Escherichia coli

Synonyms

Synonyms Comment Organism
acetaldehyde-alcohol dehydrogenase
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Escherichia coli
AdhE
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Escherichia coli
bi-functional alcohol/aldehyde dehydrogenase
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Escherichia coli
More see also EC 1.2.1.10 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
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Escherichia coli
NADH
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Escherichia coli

General Information

General Information Comment Organism
evolution the bifunctional AdhE enzyme is conserved in all bacterial kingdoms but also in more phylogenetically distant microorganisms such as green microalgae Escherichia coli
additional information filamentation of the bacterial bifunctional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation. Incubation with NAD+ and Fe2+ is sufficient to extend the filaments. The addition of coenzyme A does not impair the conformational change triggered by NAD+ and Fe2+. In the same conditions, NADH and Fe2+ are not able to trigger a conformational change from the compact to the extended form. Comparison of the structure of AdhE in its extended conformation with monofunctional ADH and AlDH enzymes, overview. The substrate/product channels of both the AlDH and ADH domains lead to the two cavities located at the AlDH-ADH interfaces within the AdhE dimer. The loops 2 and 3 seal this cavity by mediating the interactions between the AlDH and ADH domains. This allows a direct channeling between the AlDH and ADH domain active sites Escherichia coli
physiological function 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 biological role of AdhE seems to go beyond alcoholic fermentation. This protein could also be directly or indirectly involved in bacterial pathogenicity Escherichia coli