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Information on EC 1.1.1.1 - alcohol dehydrogenase

for references in articles please use BRENDA:EC1.1.1.1
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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.1 alcohol dehydrogenase
IUBMB Comments
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
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This record set is specific for:
UNIPROT: B0K4A2
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
adh, alcohol dehydrogenase, aldehyde dehydrogenase, adh1b, short-chain dehydrogenase/reductase, ssadh, adh1c, yeast alcohol dehydrogenase, retinol dehydrogenase, faldh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AdhE
bifunctional enzyme, catalyzes reactions of EC 1.1.1.1 and EC 1.2.1.10
40 kDa allergen
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ADH
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ADH-A2
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ADH-B2
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ADH-C2
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ADH-HT
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ADH3
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alcohol dehydrogenase (NAD)
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Alcohol dehydrogenase-B2
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aldehyde reductase
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aliphatic alcohol dehydrogenase
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dehydrogenase, alcohol
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ethanol dehydrogenase
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FALDH
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FDH
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Gastric alcohol dehydrogenase
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Glutathione-dependent formaldehyde dehydrogenase
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GSH-FDH
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NAD-dependent alcohol dehydrogenase
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NAD-specific aromatic alcohol dehydrogenase
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NADH-alcohol dehydrogenase
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NADH-aldehyde dehydrogenase
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Octanol dehydrogenase
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primary alcohol dehydrogenase
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Retinol dehydrogenase
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yeast alcohol 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
alcohol:NAD+ oxidoreductase
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-72-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B0K4A2_THEPX
Thermoanaerobacter sp. (strain X514)
872
0
96853
TrEMBL
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
synthetic pathway for n-butanol production from acetyl coenzyme at 70°C, using beta-ketothiolase Thl, 3-hydroxybutyryl-CoA dehydrogenase Hbd, and 3-hydroxybutyryl-CoA dehydratase Crt from Caldanaerobacter subterraneus subsp. tengcongensis, trans-2-enoyl-CoA reductase Ter from Spirochaeta thermophila and bifunctional aldehyde dehydrogenase AdhE and and butanol dehydrogenase in vitro. n-Butanol is produced at 70°C, but with different amounts of ethanol as a coproduct, because of the broad substrate specificities of AdhE, Bad, and Bdh. A reaction kinetics model, validated via comparison to in vitro experiments, is used to determine relative enzyme ratios needed to maximize n-butanol production. By using large relative amounts of Thl and Hbd and small amounts of Bad and Bdh, >70% conversion to n-butanol is observed in vitro, but with a 60% decrease in the predicted pathway flux
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Loder, A.J.; Zeldes, B.M.; Garrison, G.D.; Lipscomb, G.L.; Adams, M.W.; Kelly, R.M.
Alcohol selectivity in a synthetic thermophilic n-butanol pathway is driven by biocatalytic and thermostability characteristics of constituent enzymes
Appl. Environ. Microbiol.
81
7187-7200
2015
Thermoanaerobacter sp. (B0K4A2), Thermoanaerobacter sp.
Manually annotated by BRENDA team