Cloned (Comment) | Organism |
---|---|
gene adhe, eecombinant expression of N-terminally His6-tagged AdhE in Escherichia coli strain Bl21 | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | the enzyme occurs in an oligomeric form called spirosomes | Escherichia coli | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetaldehyde + NADH + H+ | Escherichia coli | - |
ethanol + NAD+ | - |
r | |
additional information | Escherichia coli | the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate | ? | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A9Q7 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant N-terminally His6-tagged AdhE from Escherichia coli strain BL21 by nickel affinity chromatography and gel filtration | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetaldehyde + NADH + H+ | - |
Escherichia coli | ethanol + NAD+ | - |
r | |
additional information | the bifunctional enzymes commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate | Escherichia coli | ? | - |
- |
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 | Comment | Organism |
---|---|---|
acetaldehyde-alcohol dehydrogenase | - |
Escherichia coli |
AdhE | - |
Escherichia coli |
bi-functional alcohol/aldehyde dehydrogenase | - |
Escherichia coli |
More | see also EC 1.2.1.10 | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Escherichia coli | |
NADH | - |
Escherichia coli |
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 |