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1,2-butanediol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
1,2-cyclopentandiol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
1,3-butanediol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
1-butanol + phenazine methosulfate
butanal + reduced phenazine methosulfate
-
-
-
?
1-cyclohexylethanol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
1-hexanol + phenazine methosulfate
hexanal + reduced phenazine methosulfate
-
-
-
?
1-octanol + phenazine methosulfate
octanal + reduced phenazine methosulfate
-
-
-
?
2,3-butanediol + phenazine methosulfate
? + reduced phenazine methosulfate
2,4-pentanediol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
2-butanol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
2-butanol + phenazine methosulfate
butan-2-one + reduced phenazine methosulfate
-
-
-
?
2-hexanol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
2-phenylethanol + phenazine methosulfate
phenylacetaldehyde + reduced phenazine methosulfate
acetaldehyde + phenazine methosulfate
? + reduced phenazine methosulfate
butanol + 2 cytochrome c
butyraldehyde + 2 reduced cytochrome c
butyraldehyde + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
?
cinnamyl alcohol + phenazine methosulfate
cinnamyl aldehyde + reduced phenazine methosulfate
-
-
-
?
cis-1,2-cyclohexanediol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
cyclohexanol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
D-arabinose + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
D-arabitol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
D-galactose + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
D-gluconate + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
D-lyxose + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
D-mannitol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
D-ribose + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
D-sorbitol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
D-xylose + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
ethanol + 2 cytochrome c
ethanal + 2 reduced cytochrome c
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
ethanol + N,N,N',N'-tetramethyl-p-phenylenediamine
ethanal + ?
-
i.e. Wurster's Blue
-
-
?
ethanol + oxidized 2,6-dichlorophenolindophenol
ethanal + reduced 2,6-dichlorophenolindophenol
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
-
-
?
ethanolamine + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
?
farnesol + phenazine methosulfate
farnesal + reduced phenazine methosulfate
-
-
-
?
glyceraldehyde + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
glycerol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
hexanal + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
?
isopropanol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
L-arabinose + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
L-ribose + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
meso-erythritol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
?
octanal + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
?
propanol + 2 cytochrome c
propanal + 2 reduced cytochrome c
ribitol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
threitol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
trans-1,2-cyclohexanediol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
additional information
?
-
2,3-butanediol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
-
?
2,3-butanediol + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
?
2-phenylethanol + phenazine methosulfate
phenylacetaldehyde + reduced phenazine methosulfate
-
-
-
?
2-phenylethanol + phenazine methosulfate
phenylacetaldehyde + reduced phenazine methosulfate
converted with 76% of the activity determined with ethanol
-
-
?
acetaldehyde + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
?
acetaldehyde + phenazine methosulfate
? + reduced phenazine methosulfate
converted with 71% of the activity determined with ethanol
-
-
?
butanol + 2 cytochrome c
butyraldehyde + 2 reduced cytochrome c
-
-
-
r
butanol + 2 cytochrome c
butyraldehyde + 2 reduced cytochrome c
-
-
-
r
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
r
ethanol + 2 cytochrome c
ethanal + 2 reduced cytochrome c
-
EPR-study to elucidate reaction mechanism. In an addition/elimination mechanism, the negatively charged substrate oxygen then performs a nucleophilic addition to the PQQ(C5) to form a covalent substrate-PQQ complex. This is followed by elimination of ethanal, leaving the fully reduced PQQH2. In a hydride transfer mechanism, a nucleophilic addition to the PQQ(C5) again occurs, but this time it is the hydride from C1 of the substrate that is transferred, completing the oxidization of the ethanol to ethanal. Subsequently, the PQQ enolizes to form PQQH2. The results are consistent with either proposed mechanism
-
-
?
ethanol + 2 cytochrome c
ethanal + 2 reduced cytochrome c
-
-
-
-
?
ethanol + 2 cytochrome c
ethanal + 2 reduced cytochrome c
-
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + oxidized 2,6-dichlorophenolindophenol
ethanal + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
ethanol + oxidized 2,6-dichlorophenolindophenol
ethanal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
-
-
-
-
r
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
-
the maximal reaction velocity of ExaF-La for formaldehyde is 23% greater than for methanol as the substrate
-
-
r
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
-
-
-
-
r
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
-
the maximal reaction velocity of ExaF-La for formaldehyde is 23% greater than for methanol as the substrate
-
-
r
propanol + 2 cytochrome c
propanal + 2 reduced cytochrome c
-
-
-
-
?
propanol + 2 cytochrome c
propanal + 2 reduced cytochrome c
-
-
-
-
?
additional information
?
-
-
the enzyme oxidizes a wide variety of secondary alcohols but has higher KM-values than PQQ-dependent glycerol dehydrogenase with regard to linear substrates such as glycerol. Cyclic substrates such as cis-1,2-cyclohexanediol are readily oxidized
-
-
-
additional information
?
-
-
ExaF is functionally an ethanol dehydrogenase, with secondary activities with formaldehyde, methanol, and acetaldehyde. Enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol. Methanol-independent reduction of the latter is not observed with purified enzyme
-
-
?
additional information
?
-
-
ExaF is functionally an ethanol dehydrogenase, with secondary activities with formaldehyde, methanol, and acetaldehyde. Enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol. Methanol-independent reduction of the latter is not observed with purified enzyme
-
-
?
additional information
?
-
-
enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol
-
-
?
additional information
?
-
-
enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol
-
-
?
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butanol + 2 cytochrome c
butyraldehyde + 2 reduced cytochrome c
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
additional information
?
-
butanol + 2 cytochrome c
butyraldehyde + 2 reduced cytochrome c
-
-
-
r
butanol + 2 cytochrome c
butyraldehyde + 2 reduced cytochrome c
-
-
-
r
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
r
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
-
-
-
-
r
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
-
-
-
-
r
additional information
?
-
-
ExaF is functionally an ethanol dehydrogenase, with secondary activities with formaldehyde, methanol, and acetaldehyde. Enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol. Methanol-independent reduction of the latter is not observed with purified enzyme
-
-
?
additional information
?
-
-
ExaF is functionally an ethanol dehydrogenase, with secondary activities with formaldehyde, methanol, and acetaldehyde. Enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol. Methanol-independent reduction of the latter is not observed with purified enzyme
-
-
?
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0.0031
-
substrate: threitol, pH 5.0, 25°C
0.0052
-
substrate: D-arabinose, pH 5.0, 25°C
0.01
-
substrate: trans-1,2-cyclohexanediol, pH 5.0, 25°C
0.018
-
substrate: glycerol, pH 5.0, 25°C
0.022
-
substrate: 1-cyclohexylethanol, pH 5.0, 25°C
0.027
-
substrate: D-mannitol, pH 5.0, 25°C
0.028
-
substrate: ribitol, pH 5.0, 25°C
0.03
-
substrate: 2-hexanol, pH 5.0, 25°C
0.035
-
substrate: isopropanol, pH 5.0, 25°C
0.055
-
substrate: D-sorbitol, pH 5.0, 25°C
0.065
-
substrate: 1,3-butanediol, pH 5.0, 25°C
0.08
-
substrate: 1,2-butanediol, pH 5.0, 25°C
0.084
-
substrate: cyclohexanol, pH 5.0, 25°C
0.085
-
substrate: 2,4-pentanediol, pH 5.0, 25°C
0.09
-
substrate: D-ribose, pH 5.0, 25°C
0.1
-
substrate: D-lyxose, pH 5.0, 25°C
0.17
-
substrate: D-arabitol, pH 5.0, 25°C
0.19
-
substrate: meso-erythritol, pH 5.0, 25°C
0.2
-
substrate: L-ribose, pH 5.0, 25°C
0.35
-
substrate: 1,2-cyclopentandiol, pH 5.0, 25°C
0.4
-
substrate: 2,3-butanediol, pH 5.0, 25°C
0.55
-
substrate: cis-1,2-cyclohexanediol, pH 5.0, 25°C
0.12
-
substrate: D-xylose, pH 5.0, 25°C
0.12
-
substrate: L-arabinose, pH 5.0, 25°C
0.13
-
substrate: D-galactose, pH 5.0, 25°C
0.13
-
substrate: D-gluconate, pH 5.0, 25°C
0.14
-
substrate: 2-butanol, pH 5.0, 25°C
0.14
-
substrate: glyceraldehyde, pH 5.0, 25°C
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additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
brenda
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
brenda
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
brenda
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
brenda
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
brenda
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
brenda
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
brenda
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
brenda
additional information
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
-
brenda
additional information
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
-
brenda
additional information
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
-
brenda
additional information
-
ADH is largely expressed in its active form
brenda
additional information
-
ADH is largely expressed in its active form
-
brenda
additional information
-
growth rate constants of Methylobacterium extorquens wild-type and mutant strains grown with ethanol as the carbon source
brenda
additional information
-
growth rate constants of Methylobacterium extorquens wild-type and mutant strains grown with ethanol as the carbon source
-
brenda
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evolution
-
ADHs are categorized into three groups (type I, II, and III ADHs) according to their domain structure and localization. Type I ADHs have molecular and enzymatic properties that are very similar to those of methanol dehydrogenases, MDHs, but they have a low affinity for methanol. Type I ADHs, on the other hand, generally use ethylamine or methylamine as essential activators instead of ammonia
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
-
evolution
-
ADHs are categorized into three groups (type I, II, and III ADHs) according to their domain structure and localization. Type I ADHs have molecular and enzymatic properties that are very similar to those of methanol dehydrogenases, MDHs, but they have a low affinity for methanol. Type I ADHs, on the other hand, generally use ethylamine or methylamine as essential activators instead of ammonia
-
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
-
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
-
malfunction
-
an exaF mutant is not affected for growth with ethanol
malfunction
single deletions of genes coding for PQQ-dependent alcohol dehydrogenases PedE and PedH have only minor effects on growth rates, indicating that Pseudomonas putida strain KT2440 can use both enzymes in a redundant fashion for the metabolization of butanol. Growth of mutants lacking PedE and PedH on n-butanol is significantly impaired, but not completely inhibited, suggesting that additional alcohol dehydrogenases can at least partially complement their function in strain KT2440
malfunction
-
inactivation of exaA adversely affects the growth of Azospirillum brasilense on glycerol
malfunction
-
an exaF mutant is not affected for growth with ethanol
-
malfunction
-
inactivation of exaA adversely affects the growth of Azospirillum brasilense on glycerol
-
malfunction
-
single deletions of genes coding for PQQ-dependent alcohol dehydrogenases PedE and PedH have only minor effects on growth rates, indicating that Pseudomonas putida strain KT2440 can use both enzymes in a redundant fashion for the metabolization of butanol. Growth of mutants lacking PedE and PedH on n-butanol is significantly impaired, but not completely inhibited, suggesting that additional alcohol dehydrogenases can at least partially complement their function in strain KT2440
-
metabolism
butanol is oxidized to butyraldehyde by PedE and PedH and then further oxidized to butyric acid by the aldehyde dehydrogenase PedI. Both enzymes, PedE and PedH, are directly involved in butanol oxidation in Pseudomonas putida KT2440
metabolism
KY643658; KY584296
key enzyme in the ethanol oxidase respiratory chain of acetic acid bacteria
metabolism
-
the enzyme plays an important role in the catabolism of alcohols in bacteria
metabolism
-
the enzyme plays an important role in the catabolism of alcohols in bacteria
-
metabolism
-
butanol is oxidized to butyraldehyde by PedE and PedH and then further oxidized to butyric acid by the aldehyde dehydrogenase PedI. Both enzymes, PedE and PedH, are directly involved in butanol oxidation in Pseudomonas putida KT2440
-
metabolism
-
key enzyme in the ethanol oxidase respiratory chain of acetic acid bacteria
-
physiological function
the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
physiological function
-
ExaF contributes to ethanol metabolism when La3 is present, expanding the role of lanthanides to multicarbon metabolism. ExaA quinoprotein ethanol dehydrogenase, and not the type I ADH,EC 1.1.2.4, is responsible for methanol oxidation in the MDH-3 mutant strain
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
physiological function
functional redundancy and inverse regulation of PedE (Ca2+-dependent PQQ-ADH) and PedH (lanthanide-dependent PQQ-ADH) represent an adaptive strategy of Pseudomonas putida KT2440 to optimize growth with volatile alcohols in response to the availability of different lanthanides
physiological function
-
the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
-
physiological function
-
ExaF contributes to ethanol metabolism when La3 is present, expanding the role of lanthanides to multicarbon metabolism. ExaA quinoprotein ethanol dehydrogenase, and not the type I ADH,EC 1.1.2.4, is responsible for methanol oxidation in the MDH-3 mutant strain
-
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
-
physiological function
-
the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
-
physiological function
-
the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
-
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
-
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
-
additional information
-
the enzyme occurs in active and inactive forms, overview. Active ADHa is brought back by ethanol to its full reduction state, but in inactive ADHi, only one-quarter of the total heme c is reduced, pH dependencies and redox potentials of cofactors, overview
additional information
-
Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity
additional information
-
ExaF homology modeling using the crystal structure of the quinoprotein ethanol dehydrogenase QEDH from Pseudomonas aeruginosa, PDB 1FLG, overview. Residues E198, D317, D319, and N275 form the active site. Residue D319 might be necessary for lanthanide coordination next to catalytic aspartate D317
additional information
-
ExaF homology modeling using the crystal structure of the quinoprotein ethanol dehydrogenase QEDH from Pseudomonas aeruginosa, PDB 1FLG, overview. Residues E198, D317, D319, and N275 form the active site. Residue D319 might be necessary for lanthanide coordination next to catalytic aspartate D317
-
additional information
-
the enzyme occurs in active and inactive forms, overview. Active ADHa is brought back by ethanol to its full reduction state, but in inactive ADHi, only one-quarter of the total heme c is reduced, pH dependencies and redox potentials of cofactors, overview
-
additional information
-
Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity
-
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A26V
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
G55D
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
L18Q
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
T104K
-
site-directed mutagenesis, the mutation leads to a complete loss of ethanol oxidizing ability
V107A
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
V36I
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
V54I
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
V70A
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
C105A/C106A
-
mutation of residues forming a characteristic disulfide ring in the binding pocket of pyrroloquinoline quinone. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone
E408P
mutant shows a 2.3fold increased stability upon incubation at 45°C for 1 h compared with the wild-type allele
N410K
44% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
N410S
about 30% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
N410T
about 35% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
R91D
41% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
R91D/E408P
mutant shows a 3.2fold stability upon incubation at 45°C for 1 h compared with the wild-type allele
R91E
about 35% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
R91Q
about 30% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
R91D/E408P/N410K
mutant shows a 4.0fold increased stability upon incubation at 45°C for 1 h compared with the wild-type allele
R91D/E408P/N410K
the mutant exhibits a 7°C increase in thermal stability but also a twofold increase in residual activity upon incubation with up to 50% dimethyl sulfoxide, while showing no significant difference in enzymatic efficiency (kcat/KM)
additional information
-
construction of adhS gene disruptant and mutants. The adhS gene disruptant completely loses its PQQ-ADH activity and acetate-producing ability but retains acetic acid toleration. In contrast, this disruptant grows well, even better than the wild-type, in the ethanol containing medium even though its PQQ-ADH activity and ethanol oxidizing ability is completely lost, while NAD+-dependent ADH is induced. Random mutagenesis of adhS gene reveal that complete loss of PQQ-ADH activity and ethanol oxidizing ability are observed in the mutants lacking the 140 and 73 amino acid residues at the C-terminal, whereas the lack of 22 amino acid residues at the C-terminal affects neither the PQQ-ADH activity nor ethanol oxidizing ability, overview
additional information
-
a triple mutant strain (mxaF xoxF1 xoxF2, named MDH-3), deficient in the three methanol dehydrogenases of the model methylotroph Methylobacterium extorquens AM1, is able to grow poorly with methanol if exogenous lanthanides are added to the growth medium. When the gene encoding a putative quinoprotein ethanol dehydrogenase, exaF, is mutated in the MDH-3 background, the quadruple mutant strain can no longer grow on methanol in minimal medium with added lanthanum (La3+)
additional information
-
a triple mutant strain (mxaF xoxF1 xoxF2, named MDH-3), deficient in the three methanol dehydrogenases of the model methylotroph Methylobacterium extorquens AM1, is able to grow poorly with methanol if exogenous lanthanides are added to the growth medium. When the gene encoding a putative quinoprotein ethanol dehydrogenase, exaF, is mutated in the MDH-3 background, the quadruple mutant strain can no longer grow on methanol in minimal medium with added lanthanum (La3+)
-
additional information
In the presence of the prosthetic group, expression of the Pseudomonas gene encoding the 60-kDa subunit of quinoprotein ethanol dehydrogenase in Escherichia coli results in formation of active enzyme
additional information
generation of a single deletion mutant strain of the gene coding for PedE resulting in strain GN104, and of a double mutant with deletion of both genes PedE and PedH, strain GN127
additional information
generation of a single deletion mutant strain of the gene coding for PedE resulting in strain GN104, and of a double mutant with deletion of both genes PedE and PedH, strain GN127
additional information
generation of a single deletion mutant strain of the gene coding for PedH resulting in strain GN116, and of a double mutant with deletion of both genes PedE and PedH, strain GN127
additional information
generation of a single deletion mutant strain of the gene coding for PedH resulting in strain GN116, and of a double mutant with deletion of both genes PedE and PedH, strain GN127
additional information
-
generation of a single deletion mutant strain of the gene coding for PedE resulting in strain GN104, and of a double mutant with deletion of both genes PedE and PedH, strain GN127
-
additional information
-
generation of a single deletion mutant strain of the gene coding for PedH resulting in strain GN116, and of a double mutant with deletion of both genes PedE and PedH, strain GN127
-
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Keitel, T.; Diehl, A.; Knaute, T.; Stezowski, J.J.; Hhne, W.; Grisch, H.
X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity
J. Mol. Biol.
297
961-974
2000
Pseudomonas aeruginosa
brenda
Diehl, A.; v.Wintzingerode, F.; Grisch, H.
Quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa is a homodimer. Sequence of the gene and deduced structural properties of the enzyme
Eur. J. Biochem.
257
409-419
1998
Pseudomonas aeruginosa (Q9Z4J7)
brenda
Kay, C.W.; Mennenga, B.; Goerisch, H.; Bittl, R.
Structure of the pyrroloquinoline quinone radical in quinoprotein ethanol dehydrogenase
J. Biol. Chem.
281
1470-1476
2006
Pseudomonas aeruginosa
brenda
Kay, C.W.; Mennenga, B.; Goerisch, H.; Bittl, R.
Substrate binding in quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa studied by electron-nuclear double resonance
Proc. Natl. Acad. Sci. USA
103
5267-5272
2006
Pseudomonas aeruginosa
brenda
Mutzel, A.; Goerisch, H.
Quinoprotein ethanol dehydrogenase: preparation of the apo-form and reconstitution with pyrroloquinoline quinone and calcium or strontium(2+) ions
Agric. Biol. Chem.
55
1721-1726
1991
Pseudomonas aeruginosa
-
brenda
Schrover, J.M.; Frank, J.; van Wielink, J.E.; Duine, J.A.
Quaternary structure of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa and its reoxidation with a novel cytochrome c from this organism
Biochem. J.
290 (Pt 1)
123-127
1993
Pseudomonas aeruginosa
brenda
Stezowski, J.J.; Gorisch, H.; Dauter, Z.; Rupp, M.; Hoh, A.; Englmaier, R.; Wilson, K.
Preliminary X-ray crystallographic study of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa
J. Mol. Biol.
205
617-618
1989
Pseudomonas aeruginosa
brenda
Kanchanarach, W.; Theeragool, G.; Yakushi, T.; Toyama, H.; Adachi, O.; Matsushita, K.
Characterization of thermotolerant Acetobacter pasteurianus strains and their quinoprotein alcohol dehydrogenases
Appl. Microbiol. Biotechnol.
85
741-751
2010
Acetobacter pasteurianus (C7G3B7), Acetobacter pasteurianus (C7G3B8), Acetobacter pasteurianus (C9K501), Acetobacter pasteurianus (C9K502), Acetobacter pasteurianus (C9K504), Acetobacter pasteurianus (C9W9E3), Acetobacter pasteurianus (D2SZY4), Acetobacter pasteurianus (D2SZY5), Acetobacter pasteurianus MSU10 (C7G3B7), Acetobacter pasteurianus MSU10 (C7G3B8), Acetobacter pasteurianus IFO3191 (C9K501), Acetobacter pasteurianus IFO3191 (C9K502), Acetobacter pasteurianus IFO3191 (C9K504), Acetobacter pasteurianus SKU1108 (C9W9E3), Acetobacter pasteurianus SKU1108 (D2SZY4), Acetobacter pasteurianus SKU1108 (D2SZY5)
brenda
Gomez-Manzo, S.; Gonzalez-Valdez, A.A.; Oria-Hernandez, J.; Reyes-Vivas, H.; Arreguin-Espinosa, R.; Kroneck, P.M.; Sosa-Torres, M.E.; Escamilla, J.E.
The active (ADHa) and inactive (ADHi) forms of the PQQ-alcohol dehydrogenase from Gluconacetobacter diazotrophicus differ in their respective oligomeric structures and redox state of their corresponding prosthetic groups
FEMS Microbiol. Lett.
328
106-113
2012
Gluconacetobacter diazotrophicus, Gluconacetobacter diazotrophicus PAL5
brenda
Masud, U.; Matsushita, K.; Theeragool, G.
Cloning and functional analysis of adhS gene encoding quinoprotein alcohol dehydrogenase subunit III from Acetobacter pasteurianus SKU1108
Int. J. Food Microbiol.
138
39-49
2010
Acetobacter pasteurianus, Acetobacter pasteurianus SKU1108
brenda
Zhang, W.; Niu, Z.; Liao, C.; Chen, L.
Isolation and characterization of Pseudomonas sp. strain capable of degrading diethylstilbestrol
Appl. Microbiol. Biotechnol.
97
4095-4104
2013
Pseudomonas sp., Pseudomonas mendocina, Pseudomonas stutzeri, Pseudomonas sp. J51, Pseudomonas stutzeri ATCC 14405, Pseudomonas mendocina YMP
brenda
Takeda, K.; Ishida, T.; Igarashi, K.; Samejima, M.; Nakamura, N.; Ohno, H.
Effect of amines as activators on the alcohol-oxidizing activity of pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase
Biosci. Biotechnol. Biochem.
78
1195-1198
2014
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Good, N.M.; Vu, H.N.; Suriano, C.J.; Subuyuj, G.A.; Skovran, E.; Martinez-Gomez, N.C.
Pyrroloquinoline quinone ethanol dehydrogenase in Methylobacterium extorquens AM1 extends lanthanide-dependent metabolism to multicarbon substrates
J. Bacteriol.
198
3109-3118
2016
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
brenda
Simon, O.; Klebensberger, J.; Muekschel, B.; Klaiber, I.; Graf, N.; Altenbuchner, J.; Huber, A.; Hauer, B.; Pfannstiel, J.
Analysis of the molecular response of Pseudomonas putida KT2440 to the next-generation biofuel n-butanol
J. Proteomics
122
11-25
2015
Pseudomonas putida (B1N7J0), Pseudomonas putida (B1N7J5), Pseudomonas putida KT 2240 (B1N7J0), Pseudomonas putida KT 2240 (B1N7J5)
brenda
Nguyen, T.; Naoki, K.; Kataoka, N.; Matsutani, M.; Ano, Y.; Adachi, O.; Matsushita, K.; Yakushi, T.
Characterization of a cryptic, pyrroloquinoline quinone-dependent dehydrogenase of Gluconobacter sp. strain CHM43
Biosci. Biotechnol. Biochem.
85
998-1004
2021
Gluconobacter sp. CHM43
brenda
Wu, X.; Yao, H.; Cao, L.; Zheng, Z.; Chen, X.; Zhang, M.; Wei, Z.; Cheng, J.; Jiang, S.; Pan, L.; Li, X.
Improving Acetic Acid Production by Over-Expressing PQQ-ADH in Acetobacter pasteurianus
Front. Microbiol.
8
1713
2017
Acetobacter pasteurianus (KY643658 AND KY584296), Acetobacter pasteurianus JST-S (KY643658 AND KY584296)
brenda
Singh, V.S.; Dubey, A.P.; Gupta, A.; Singh, S.; Singh, B.N.; Tripathi, A.K.
Regulation of a glycerol-induced quinoprotein alcohol dehydrogenase by ?54 and a LuxR-type regulator in Azospirillum brasilense Sp7
J. Bacteriol.
199
e00035-17
2017
Azospirillum brasilense, Azospirillum brasilense Sp7
brenda
Wehrmann, M.; Billard, P.; Martin-Meriadec, A.; Zegeye, A.; Klebensberger, J.
Functional role of lanthanides in enzymatic activity and transcriptional regulation of pyrroloquinoline quinone-dependent alcohol dehydrogenases in Pseudomonas putida KT2440
mBio
8
e00570-17
2017
Pseudomonas putida (Q88JH5)
brenda
Wehrmann, M.; Klebensberger, J.
Engineering thermal stability and solvent tolerance of the soluble quinoprotein PedE from Pseudomonas putida KT2440 with a heterologous whole-cell screening approach
Microb. Biotechnol.
11
399-408
2018
Pseudomonas putida (Q88JH5)
brenda