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Information on EC 1.1.1.2 - alcohol dehydrogenase (NADP+) and Organism(s) Escherichia coli and UniProt Accession Q46856

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IUBMB Comments
A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH.
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Escherichia coli
UNIPROT: Q46856
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nadph-cytochrome c reductase, aldo-keto reductase, liver alcohol dehydrogenase, adh-1, adh-2, short-chain alcohol dehydrogenase, lbadh, nadph-dependent aldehyde reductase, cbadh, tsadh319, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-DG-reducing enzyme
-
-
-
-
ADH
-
-
-
-
Alcohol dehydrogenase [NADP+]
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-
-
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aldehyde reductase
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-
-
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aldehyde reductase (NADPH2)
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-
-
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Aldo-keto reductase family 1 member A1
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-
-
-
ALR
-
-
-
-
ALR 1
-
-
-
-
high-Km aldehyde reductase
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-
-
-
low-Km aldehyde reductase
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-
-
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NADP-alcohol dehydrogenase
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-
-
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NADP-aldehyde reductase
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-
-
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NADP-dependent aldehyde reductase
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-
-
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NADPH-aldehyde reductase
-
-
-
-
NADPH-dependent aldehyde reductase
nonspecific succinic semialdehyde reductase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
alcohol:NADP+ oxidoreductase
A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-12-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + NADPH + H+
ethanol + NADP+
show the reaction diagram
-
-
-
-
r
acrolein + NADPH
propenol + NADP+
show the reaction diagram
-
-
-
-
r
butanaldehyde + NADPH
butanol + NADP+
show the reaction diagram
-
-
-
-
r
ethanol + NADP+
acetaldehyde + NADPH + H+
show the reaction diagram
-
-
-
-
r
malondialdehyde + NADPH
?
show the reaction diagram
-
-
-
-
r
propanaldehyde + NADPH
propanol + NADP+
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
YqhD mediates resistance to potassium tellurite and other reactive oxygen species elicitors in Escherichia coli, and protects from protein oxidation, YqhD lowers toxic acrolein concentrations, overview
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
one atom per active site
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
28.47
acetaldehyde
-
pH 7.0, 37°C
4.81
acrolein
-
pH 7.0, 37°C
0.67
butanaldehyde
-
pH 7.0, 37°C
1.78
malondialdehyde
-
pH 7.0, 37°C
3.31
propionaldehyde
-
pH 7.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
53.5
acetaldehyde
-
pH 7.0, 37°C
62.5
acrolein
-
pH 7.0, 37°C
59.5
butanaldehyde
-
pH 7.0, 37°C
60.1
malondialdehyde
-
pH 7.0, 37°C
45.1
propionaldehyde
-
pH 7.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
crystallization data, each monomer is composed of two domains
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
a yqhD knockout mutant does not confer resistance to potassium tellurite and other ROS elicitors
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
1° Adh cloned and characterized
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expression of wild-type and mutant enzymes
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
overexpression of the endogenous zwf gene, which encodes glucose-6-phosphate dehydrogenase of the pentose phosphate pathway, in Synechocystis sp. PCC 6803 results in increased NADPH production, and promoted biomass production. Ethanol production by alcohol dehydrogenase YqhD is increased in autotrophic conditions by zwf overexpression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bryant, F.O.; Wiegel, J.; Ljungdahl, L.G.
Purification and properties of primary and secondary alcohol dehydrogenases from Thermoanaerobacter ethanolicus
Appl. Environ. Microbiol.
2
460-465
1988
Acinetobacter sp., Geobacillus stearothermophilus, Saccharomyces cerevisiae, Clostridium beijerinckii, Thermoanaerobacter brockii, Thermoanaerobacter thermohydrosulfuricus, Escherichia coli, Thermoanaerobacter ethanolicus, Zymomonas mobilis
-
Manually annotated by BRENDA team
Burdette, D.; Zeikus, J.G.
Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenase (2 degrees Adh) as a bifunctional alcohol dehydrogenase-acetyl-CoA reductive thioesterase
Biochem. J.
302
163-170
1994
Leuconostoc mesenteroides, Saccharomyces cerevisiae, Clostridium acetobutylicum, Clostridium beijerinckii, Thermoanaerobacter brockii, Clostridium kluyveri, Acetivibrio thermocellus, Thermoanaerobacter thermohydrosulfuricus, Escherichia coli, Propionibacterium freudenreichii, Thermoanaerobacter ethanolicus, Vibrio harveyi, Zymomonas mobilis, Clostridium acetobutylicum NRRL B643, Clostridium beijerinckii NRRL B592, Thermoanaerobacter ethanolicus JW 200
Manually annotated by BRENDA team
Li, D.; Stevenson, K.J.
Purification and sequence analysis of a novel NADP(H)-dependent type III alcohol dehydrogenase from Thermococcus strain AN1
J. Bacteriol.
179
4433-4437
1997
Bacillus methanolicus, Saccharomyces cerevisiae, Clostridium acetobutylicum, Drosophila melanogaster, Escherichia coli, Thermococcus sp., Zymomonas mobilis, Thermococcus sp. AN1
Manually annotated by BRENDA team
Galamba, A.; Soetaert, K.; Buyssens, P.; Monnaie, D.; Jacobs, P.; Content, J.
Molecular and biochemical characterization of Mycobacterium smegmatis alcohol dehydrogenase C
FEMS Microbiol. Lett.
196
51-56
2001
Bacillus subtilis, Escherichia coli, Equus sp., Helicobacter pylori, Mycobacterium tuberculosis, Mycobacterium avium, Mycobacterium tuberculosis variant bovis, Mycobacterium leprae, Mycobacterium avium subsp. paratuberculosis, Mycolicibacterium smegmatis
Manually annotated by BRENDA team
Sulzenbacher, G.; Alvarez, K.; Van Den Heuvel, R.H.; Versluis, C.; Spinelli, S.; Campanacci, V.; Valencia, C.; Cambillau, C.; Eklund, H.; Tegoni, M.
Crystal structure of E. coli alcohol dehydrogenase YqhD: evidence of a covalently modified NADP coenzyme
J. Mol. Biol.
342
489-502
2004
Escherichia coli
Manually annotated by BRENDA team
Perez, J.M.; Arenas, F.A.; Pradenas, G.A.; Sandoval, J.M.; Vasquez, C.C.
Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes
J. Biol. Chem.
283
7346-7353
2008
Escherichia coli
Manually annotated by BRENDA team
Choi, Y.N.; Park, J.M.
Enhancing biomass and ethanol production by increasing NADPH production in Synechocystis sp. PCC 6803
Biores. Technol.
213
54-57
2016
Escherichia coli (Q46856)
Manually annotated by BRENDA team