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Information on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)

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EC Tree
IUBMB Comments
Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower .
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UNIPROT: A0A1D3TRQ6
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
dmpfg, coa-dependent aldehyde dehydrogenase, acetyl-coa reductase, tthb247, aldehyde dehydrogenase (acylating), 4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase, nonphosphorylating acylating aldehyde dehydrogenase, coenzyme a linked aldehyde dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACDH
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Acetaldehyde dehydrogenase [acetylating]
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acetyl-CoA reductase
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aldehyde dehydrogenase (acylating)
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CoA-dependent aldehyde dehydrogenase
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coenzyme A linked aldehyde dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
acetaldehyde:NAD+ oxidoreductase (CoA-acetylating)
Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9028-91-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
show the reaction diagram
activity of the enzyme is confirmed by proteome analysis and enzyme assays with cell extract glycerol-grown cells
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A1D3TRQ6_9FIRM
871
0
95229
TrEMBL
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biofuel production
proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates 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. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Patil, Y.; Junghare, M.; Mller, N.
Fermentation of glycerol by Anaerobium acetethylicum and its potential use in biofuel production
Microb. Biotechnol.
10
203-217
2017
Anaerobium acetethylicum (A0A1D3TRQ6)
Manually annotated by BRENDA team