1.2.1.10: acetaldehyde dehydrogenase (acetylating)
This is an abbreviated version!
For detailed information about acetaldehyde dehydrogenase (acetylating), go to the full flat file.
Word Map on EC 1.2.1.10
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1.2.1.10
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synthesis
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propionaldehyde
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nad-dependent
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meta-cleavage
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biofuel production
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transthioesterification
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histolytica
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benzaldehyde
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pre-steady-state
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ammonia-lyase
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propionyl-coa
- 1.2.1.10
- synthesis
- propionaldehyde
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nad-dependent
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meta-cleavage
- biofuel production
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transthioesterification
- histolytica
- benzaldehyde
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pre-steady-state
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ammonia-lyase
- propionyl-coa
Reaction
Synonyms
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase, ACDH, acetaldehyde dehydrogenase, Acetaldehyde dehydrogenase [acetylating], acetaldehyde-alcohol dehydrogenase, acetyl-CoA reductase, acylating acetaldehyde dehydrogenase, AdhE, ADHES77, aldehyde dehydrogenase, aldehyde dehydrogenase (acylating), aldehyde/alcohol dehydrogenase, ALDH, BAD, bi-functional alcohol/aldehyde dehydrogenase, bifunctional acetaldehyde-alcohol dehydrogenase, BphJ, CoA-acylating aldehyde dehydrogenase, CoA-dependent aldehyde dehydrogenase, coenzyme A linked aldehyde dehydrogenase, coenzyme A-acylating aldehyde dehydrogenase, DmpF, DmpFG, MhpF, More, NAD+/CoA-dependent aldehyde dehydrogenase, nonphosphorylating acylating aldehyde dehydrogenase, PduP, Teth514_0627, Teth514_1942, Tsac_0416, TTHB247
ECTree
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General Information on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
cells with increased ADHE abundance exhibit better survival under dark anoxia
metabolism
physiological function
additional information
evolution
distribution of ADHE among the five eukaryotic supergroups, overview
evolution
the bifunctional AdhE enzyme is conserved in all bacterial kingdoms but also in more phylogenetically distant microorganisms such as green microalgae
metabolism
DmpFG catalyzes the final two steps of the meta-cleavage pathway of catechol and its methylated substituents. This pathway breaks down toxic waste products such as naphthalenes, salicylates, and benzoates to harmless metabolites
metabolism
ADHE can be involved either in ethanol production or assimilation, or both, depending upon environmental conditions. Presence of ADHE in an oxygen-respiring algal mitochondrion and co-expression at ambient oxygen levels with respiratory chain components is unexpected with respect to the view that eukaryotes acquire ADHE genes specifically as an adaptation to an anaerobic lifestyle
metabolism
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the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
metabolism
anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
metabolism
analysis of the anerobic metabolic routes involving the enzyme in Chlamydomonas reinhardtii, overview
metabolism
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DmpFG catalyzes the final two steps of the meta-cleavage pathway of catechol and its methylated substituents. This pathway breaks down toxic waste products such as naphthalenes, salicylates, and benzoates to harmless metabolites
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physiological function
deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strain, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. It loses more than 85% of alcohol dehydrogenase activity. Aldehyde dehydrogenase activity does not appear to be affected, although its activity is low in cell extracts. Adding ubiquinone-0 to the aldehyde dehydrogenase assay increases activity in the parent strain but does not increase activity in the adhE deletion strain
physiological function
deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strains, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. The deletion strain additionally contains a point mutation in the lactate dehydrogenase gene, which appears to deregulate its activation by fructose 1,6-bisphosphate, leading to constitutive activation of lactate dehydrogenase
physiological function
deletion of adhE reduces ethanol production by more than 95%. Fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. The adhE deletion strain loses more than 85% of alcohol dehydrogenase activity. Aldehyde dehydrogenase activity does not appear to be affected
physiological function
deletion of adhE reduces ethanol production by more than 95%. Fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. The adhE deletion strain loses more than 90% of ALDH and ADH activity in cell extracts
physiological function
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acetaldehyde-alcohol dehydrogenase (ADHE) is a bifunctional enzyme consisting of two domains of an N-terminal acetaldehyde dehydrogenase (ALDH) and a C-terminal alcohol dehydrogenase (ADH). The N-terminal domain is responsible for the conversion of acetyl-CoA to acetaldehyde and the C-terminal domain is subsequently responsible for the conversion of acetaldehyde to ethanol. The enzyme is important in the cellular alcohol metabolism. The coenzyme A-acylating ADHE from Citrobacter sp. S-77 may play a pivotal role in modulating intracellular acetaldehyde concentration
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
physiological function
aldehyde/alcohol dehydrogenases (ADHEs) are bifunctional enzymes that commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate and play a key role in anaerobic redox balance in many fermenting bacteria. ADHEs are also present in photosynthetic unicellular eukaryotes
physiological function
Acetivibrio thermocellus DSM 1237
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deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strains, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. The deletion strain additionally contains a point mutation in the lactate dehydrogenase gene, which appears to deregulate its activation by fructose 1,6-bisphosphate, leading to constitutive activation of lactate dehydrogenase
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physiological function
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deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strain, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. It loses more than 85% of alcohol dehydrogenase activity. Aldehyde dehydrogenase activity does not appear to be affected, although its activity is low in cell extracts. Adding ubiquinone-0 to the aldehyde dehydrogenase assay increases activity in the parent strain but does not increase activity in the adhE deletion strain
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physiological function
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aldehyde/alcohol dehydrogenases (ADHEs) are bifunctional enzymes that commonly produce ethanol from acetyl-CoA with acetaldehyde as intermediate and play a key role in anaerobic redox balance in many fermenting bacteria. ADHEs are also present in photosynthetic unicellular eukaryotes
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additional information
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the enzyme's two functional domains are fused into a single polypeptide by a linker amino acid region
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
