Information on EC 1.1.5.5 - alcohol dehydrogenase (quinone)

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The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY
1.1.5.5
-
RECOMMENDED NAME
GeneOntology No.
alcohol dehydrogenase (quinone)
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ethanol + ubiquinone = acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
Acidomonas methanolica JCM
-
-
-
redox reaction
-
-
redox reaction
Acidomonas methanolica JCM
-
-
-
reduction
Acidomonas methanolica JCM
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
long chain fatty acid ester synthesis for microdiesel production
-
SYSTEMATIC NAME
IUBMB Comments
alcohol:quinone oxidoreductase
Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed ‘propeller’ structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ADH
Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
-
-
-
ADH
Gluconacetobacter xylinus
-
-
ADH
Gluconacetobacter xylinus IFO 13693
-
-
-
ADHI
Gluconacetobacter europaeus
Q44002
-
ExaA2
-
-
ExaA2
-
-
-
ExaA3
-
-
ExaA3
-
-
-
formaldehyde-oxidizing enzyme
-
-
PQQ dependent alcohol dehydrogenase
Gluconobacter sp.
-
-
PQQ dependent alcohol dehydrogenase
Gluconobacter sp. 33
-
-
-
PQQ-ADH
Acetobacter lovaniensis IFO3284
-
-
-
PQQ-ADH
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452
-
-
-
PQQ-ADH
Acetobacter pasteurianus SKU1108
-
;
-
PQQ-ADH
Acidomonas methanolica JCM6891
-
-
-
PQQ-ADH
CCU55317
-
PQQ-ADH
Frateuria aurantia LMG 1558
CCU55317
-
-
PQQ-ADH
Gluconacetobacter diazotrophicus PAL5
-
-
-
PQQ-ADH
Gluconacetobacter europaeus
-
-
PQQ-ADH
Gluconacetobacter europaeus V3
-
-
-
PQQ-ADH
Gluconacetobacter intermedius
-
-
PQQ-ADH
Gluconacetobacter intermedius JK3
-
-
-
PQQ-ADH
Gluconacetobacter polyoxogenes NBI1028
-
-
-
PQQ-ADH
Gluconacetobacter xylinus, Gluconobacter oxydans
-
-
PQQ-ADH
Gluconobacter oxydans IFO12528
-
-
-
PQQ-alcohol dehydrogenase
-
-
PQQ-dependent ADH
Q335W4
-
PQQ-dependent ADH
Gluconacetobacter europaeus
Q44002
-
PQQ-dependent ADH
Gluconacetobacter intermedius
Q335V9
-
PQQ-dependent ADH
Gluconacetobacter intermedius JK3
Q335V9
-
-
PQQ-dependent ADH
Gluconobacter sp.
-
-
PQQ-dependent ADH
Gluconobacter sp. 33
-
-
-
PQQ-dependent alcohol dehydrogenase
CCU55317
-
PQQ-dependent alcohol dehydrogenase
Frateuria aurantia LMG 1558
CCU55317
-
-
PQQ-dependent alcohol dehydrogenase
Gluconacetobacter europaeus
-
-
PQQ-dependent alcohol dehydrogenase
Gluconacetobacter europaeus V3
-
-
-
PQQ-dependent alcohol dehydrogenase
Gluconobacter sp.
-
-
PQQ-dependent alcohol dehydrogenase
Gluconobacter sp. 33
-
-
-
PQQ-dependent alcohol dehydrogenase
-
-
PQQ-dependent ethanol dehydrogenase
-
-
PQQ-dependent ethanol dehydrogenase
-
-
PQQ–alcohol dehydrogenase
P18278
-
PQQ–alcohol dehydrogenase
-
-
pyrrolo-quinoline quinone-dependent alcohol dehydrogenase
-
-
pyrrolo-quinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroloquinoline quinone dependent ADH
Gluconobacter sp.
-
-
pyrroloquinoline quinone dependent ADH
Gluconobacter sp. 33
-
-
-
pyrroloquinoline quinone dependent alcohol dehydrogenase
Gluconobacter sp.
-
-
pyrroloquinoline quinone dependent alcohol dehydrogenase
Gluconobacter sp. 33
-
-
-
pyrroloquinoline quinone-dependent alcohol dehydrogenase
CCU55317
-
pyrroloquinoline quinone-dependent alcohol dehydrogenase
Frateuria aurantia LMG 1558
CCU55317
-
-
pyrroloquinoline quinone-dependent alcohol dehydrogenase
Gluconobacter sp.
-
-
pyrroloquinoline quinone-dependent alcohol dehydrogenase
Gluconobacter sp. 33
-
-
-
pyrroloquinoline quinone–alcohol dehydrogenase
P18278
-
pyrroloquinoline quinone–alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Acetobacter lovaniensis IFO3284
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452, Acetobacter pasteurianus SKU1108
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Acidomonas methanolica JCM6891
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Gluconacetobacter diazotrophicus PAL5
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Gluconacetobacter europaeus
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Gluconacetobacter europaeus V3
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Gluconacetobacter intermedius
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Gluconacetobacter intermedius JK3
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Gluconacetobacter polyoxogenes NBI1028
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Gluconacetobacter xylinus, Gluconobacter oxydans
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Gluconobacter oxydans IFO12528
-
-
-
QH-ADH
Gluconobacter sp.
-
-
QH-ADH
Gluconobacter sp. 33
-
-
-
quinocytochrome alcohol dehydrogenase GS
-
-
quinohaemoprotein alcohol dehydrogenase
P18278
-
quinohemoprotein alcohol dehydrogenase
P18278
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
Acetobacter pasteurianus SKU1108
-
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
-
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
Gluconacetobacter xylinus
-
-
quinohemoprotein alcohol dehydrogenase
Gluconacetobacter xylinus IFO 13693
-
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
Gluconobacter sp.
-
-
quinohemoprotein alcohol dehydrogenase
Gluconobacter sp. 33
-
-
-
quinone-dependent alcohol dehydrogenase
-
-
quinoprotein alcohol dehydrogenase
-
-
quinoprotein alcohol dehydrogenase
Acetobacter pasteurianus SKU1108
-
-
-
quinoprotein alcohol dehydrogenase
-
-
quinoprotein alcohol dehydrogenase
Gluconobacter oxydans IFO 12528
-
-
-
quinoprotein alcohol dehydrogenases
-
-
quinoprotein alcohol dehydrogenases
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus IFO3284, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus SKU1108
-
-
-
formaldehyde-oxidizing enzyme
Acetobacter sp. SKU 14
-
-
-
additional information
-
the enzyme is a type III ADH
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
genes adhA, adhB, and adhS encoding the three subunits
-
-
Manually annotated by BRENDA team
Acetobacter lovaniensis IFO3284
genes adhA, adhB, and adhS encoding the three subunits
-
-
Manually annotated by BRENDA team
; subsp lovaniensis
-
-
Manually annotated by BRENDA team
AdhA fragment; strains KKP/584 and DSM 3509, gene adhA
UniProt
Manually annotated by BRENDA team
genes adhA, adhB, and adhS encoding the three subunis; genes adhA, adhB, and adhS encoding the three subunits
-
-
Manually annotated by BRENDA team
genes adhA, adhB, and adhS, encding subunits I , II, and III, respectively
-
-
Manually annotated by BRENDA team
strain SKU1108
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus IFO3191
-
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus IFO3191
genes adhA, adhB, and adhS encoding the three subunits
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus IFO3284
subsp lovaniensis
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus KKP584
genes adhA, adhB, and adhS encoding the three subunis
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus MSU10
-
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus MSU10
genes adhA, adhB, and adhS encoding the three subunits
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus NCI1452
genes adhA, adhB, and adhS encoding the three subunits
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus SKU1108
-
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus SKU1108
genes adhA, adhB, and adhS encoding the three subunits
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus SKU1108
genes adhA, adhB, and adhS, encding subunits I , II, and III, respectively
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus SKU1108
strain SKU1108
-
-
Manually annotated by BRENDA team
strain SKU 14, isolated in Thailand
-
-
Manually annotated by BRENDA team
Acetobacter sp. SKU 14
strain SKU 14, isolated in Thailand
-
-
Manually annotated by BRENDA team
genes adhA, adhB, and adhS, encoding the three subunits
-
-
Manually annotated by BRENDA team
strain JCM 6891
-
-
Manually annotated by BRENDA team
Acidomonas methanolica JCM
strain JCM 6891
-
-
Manually annotated by BRENDA team
Acidomonas methanolica JCM6891
genes adhA, adhB, and adhS, encoding the three subunits
-
-
Manually annotated by BRENDA team
genes exaA2 and exaA3
-
-
Manually annotated by BRENDA team
genes exaA2 and exaA3
-
-
Manually annotated by BRENDA team
genes adhA and adhB encoding subunits I and II
CCU55317
GenBank
Manually annotated by BRENDA team
Frateuria aurantia LMG 1558
genes adhA and adhB encoding subunits I and II
CCU55317
GenBank
Manually annotated by BRENDA team
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
Gluconacetobacter diazotrophicus PAL5
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
-
-
-
Manually annotated by BRENDA team
Gluconacetobacter europaeus
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
Gluconacetobacter europaeus
strain V3, LMG 18494
-
-
Manually annotated by BRENDA team
Gluconacetobacter europaeus
strains VA and DSM 6160, gene adh
UniProt
Manually annotated by BRENDA team
Gluconacetobacter europaeus V3
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
Gluconacetobacter europaeus V3
strain V3, LMG 18494
-
-
Manually annotated by BRENDA team
Gluconacetobacter intermedius
adh, fragment; strain JK3, gene adh
UniProt
Manually annotated by BRENDA team
Gluconacetobacter intermedius
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
Gluconacetobacter intermedius JK3
adh, fragment; strain JK3, gene adh
UniProt
Manually annotated by BRENDA team
Gluconacetobacter intermedius JK3
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
Gluconacetobacter polyoxogenes NBI1028
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
Gluconacetobacter xylinus
-
-
-
Manually annotated by BRENDA team
Gluconacetobacter xylinus
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
Gluconacetobacter xylinus IFO 13693
-
-
-
Manually annotated by BRENDA team
genes adhA, adhB, and adhS, encoding the three subunits; genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
strain IFO 12528, constitutive enzyme
-
-
Manually annotated by BRENDA team
Gluconobacter oxydans IFO 12528
strain IFO 12528, constitutive enzyme
-
-
Manually annotated by BRENDA team
Gluconobacter oxydans IFO12528
genes adhA, adhB, and adhS, encoding the three subunits
-
-
Manually annotated by BRENDA team
Gluconobacter sp.
strain 33
-
-
Manually annotated by BRENDA team
Gluconobacter sp. 33
strain 33
-
-
Manually annotated by BRENDA team
gene PA1982 or exaA
-
-
Manually annotated by BRENDA team
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,6-dichloro-4-dicyanovinylphenol
-
i.e. PC-16, competitive quinone reduction inhibition mode, the inhibitor binds to the low affinity quinone binding site(S) QN and/or QL ofquinone-bound ADH, overview
antimycin A
-
inhibits Q2H2 oxidation and Q reduction
antimycin A
Gluconacetobacter xylinus
-
powerful inhibitor of the purified ADH complex, most likely acting at the ubiquinone acceptor site in subunit II
Myxothiazol
Gluconacetobacter xylinus
-
powerful inhibitor of the purified ADH complex, most likely acting at the ubiquinone acceptor site in subunit II
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ethanol
-
ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
additional information
Gluconacetobacter europaeus
-
acetic acid induces the enzyme
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
30.8
-
acetaldehyde
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
67.5
-
allylic alcohol
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
-
71
-
ethanol
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
52.3
-
n-butanol
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
76.3
-
ubiquinone-1
Gluconacetobacter xylinus
-
using ethanol as cosubstrate, pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
446
-
acetaldehyde
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
6104
157
-
allylic alcohol
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
0
108
-
ethanol
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
10367
145
-
n-butanol
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
13792
162
-
ubiquinone-1
Gluconacetobacter xylinus
-
using ethanol as cosubstrate, pH and temperature not specified in the publication
17611
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
inhibition kinetics
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
6
CCU55317, -
strong decrease of activity at pH levels below pH 4 and above pH 5.5, and no activity at pH 2.0 and pH 7.0, activity range, profile overview
5
7.5
-
pH 5.0: about 50% of maximal activity, pH 7.5: about 55% of maximal activity, substrate: ethanol
additional information
-
-
PQQ-ADH has ubiquinone reductase activity at acidic pH 4.0-5.0
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
50
CCU55317, -
activity range, profile overview. No activity above 50°C, maximum activity at 20°C
25
50
-
25°C: about 75% of maximal activity, 50°C: about 60% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.7
-
Gluconacetobacter xylinus
-
isoelectric focusing
6.1
-
-
gradient electrophoresis, determined in pH range 3.4-9.0
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Gluconacetobacter europaeus
Q44002
the cells show high enzyme activity
Manually annotated by BRENDA team
Gluconacetobacter europaeus
-
the cells are able to grow on up to 10% acetic acid, expression analysis, overview
Manually annotated by BRENDA team
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while the 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 strains IFO3191 and IFO3284 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
Manually annotated by BRENDA team
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus IFO3284, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus SKU1108
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while the 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 strains IFO3191 and IFO3284 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
-
Manually annotated by BRENDA team
Gluconacetobacter europaeus V3
-
the cells are able to grow on up to 10% acetic acid, expression analysis, overview
-
Manually annotated by BRENDA team
Acetobacter sp. SKU 14
-
-
-
Manually annotated by BRENDA team
additional information
-
growth and tolerance to acetic acid and ethanol of thermotolerant strains at several conditions, overview
Manually annotated by BRENDA team
additional information
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus IFO3284, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus SKU1108
-
growth and tolerance to acetic acid and ethanol of thermotolerant strains at several conditions, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
115000
-
-
non-denaturing PAGE
119000
-
Gluconacetobacter xylinus
-
gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ADH-GS, 10 mg/ml protein in 100 mM sodium acetate buffer, pH 4.5, 0.34 mM n-dodecyl-beta-D-maltoside or 0.16 mM C12E8 and either 150 mM ammonium sulfate/6% PEG 3350 or 1.3 M ammonium sulfate only, with or without 2 mM Ca2+, X-ray diffraction structure determination and analysis at 3.0-5.0 A resolution, heavy atom labeling
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
9
-
stable at 6°C, overnight
10
-
-
at 6°C, overnight, about 75% inactivation
11
-
-
at 6°C, overnight, complete inactivation
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
10 min, stable
40
-
-
15 min, 80% loss of activity
45
-
-
10 min, about 50% loss of activity
45
-
-
30 min, stable up to
50
-
-
10 min, 95% loss of activity
additional information
-
-
ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0.1% Triton X-100 stabilizes the enzyme
Gluconobacter sp.
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ethanol
-
ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature; ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature, the ADH from strain IFO3191 loses all the activity at 40°C at 22% ethanol; ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature, the ADH from strain MSU10 shows 43% remaining activity at 40°C at 22% ethanol; ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature, the ADH from strain SKU1108 shows 29% reamining activity at 40°C at 22% ethanol
Ethanol
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus IFO3284, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus SKU1108
-
ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature; ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature, the ADH from strain IFO3191 loses all the activity at 40°C at 22% ethanol; ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature, the ADH from strain MSU10 shows 43% remaining activity at 40°C at 22% ethanol; ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature, the ADH from strain SKU1108 shows 29% reamining activity at 40°C at 22% ethanol
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4°C, purified enzyme in 10 mM potassium phosphate buffer containing 0.1% (v/v) Triton X-100, 30 days, no appreciable loss of activity
Gluconacetobacter xylinus
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
-
ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
Acetobacter pasteurianus SKU1108
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A26V
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
G55D
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random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
T104K
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random mutagenesis, the mutation leads to complpete loss of ethanol oxidizing ability
V107A
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random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
V36I
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random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
V54I
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random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
V70A
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random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
A26V
Acetobacter pasteurianus SKU1108
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random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
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V54I
Acetobacter pasteurianus SKU1108
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random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
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L18Q
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random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
additional information
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random mutagenesis of adhS gene, complete loss of PQQ-ADH activity and ethanol oxidizing ability are observed in the mutants lacking of the 140 and 73 amino acid residues at the C-terminal, whereas the lack of 22 amino acid residues at the C-terminal affected neither the PQQ-ADH activity nor ethanol oxidizing ability
G55D
Acetobacter pasteurianus SKU1108
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random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
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additional information
Acetobacter pasteurianus SKU1108
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random mutagenesis of adhS gene, complete loss of PQQ-ADH activity and ethanol oxidizing ability are observed in the mutants lacking of the 140 and 73 amino acid residues at the C-terminal, whereas the lack of 22 amino acid residues at the C-terminal affected neither the PQQ-ADH activity nor ethanol oxidizing ability
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V70A
Acetobacter pasteurianus SKU1108
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random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
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additional information
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disruption of genes exaA2 and exaA3
additional information
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disruption of genes exaA2 and exaA3
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additional information
Gluconobacter sp.
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construction of enzyme electrodes containing pyrroloquinoline quinone-dependent alcohol dehydrogenase as a biological component in combination with 4-ferrocenylphenol as an electron transfer mediator between PQQ and a carbon electrode for measurements of ethanol, overview. The biosensor shows the highest response at pH 5.5 and the working potential of 0.3 V, versus AgNAgCl, for ADH
additional information
Gluconobacter sp. 33
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construction of enzyme electrodes containing pyrroloquinoline quinone-dependent alcohol dehydrogenase as a biological component in combination with 4-ferrocenylphenol as an electron transfer mediator between PQQ and a carbon electrode for measurements of ethanol, overview. The biosensor shows the highest response at pH 5.5 and the working potential of 0.3 V, versus AgNAgCl, for ADH
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
Gluconobacter sp.
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construction and evaluation of an ethanol sensor based on the enzyme using direct electron-transfer processes between the polypyrrole entrapped quinohemoprotein alcohol dehydrogenase and a platinum electrode, overview
analysis
Gluconobacter sp.
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the enzyme can be used in biosensors, method development, overview
analysis
Gluconobacter sp. 33
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construction and evaluation of an ethanol sensor based on the enzyme using direct electron-transfer processes between the polypyrrole entrapped quinohemoprotein alcohol dehydrogenase and a platinum electrode, overview; the enzyme can be used in biosensors, method development, overview
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analysis
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adhA expression is related to the ability to oxidize and grow on ethanol. Differential expression of pyrroloquinoline quinone–alcohol dehydrogenase could be a marker to analyse both growth and oxidation ability in some acetic acid bacteria, especially those of the genus Acetobacter
additional information
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
additional information
Acetobacter lovaniensis IFO3284
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
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analysis
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adhA expression is related to the ability to oxidize and grow on ethanol. Differential expression of pyrroloquinoline quinone–alcohol dehydrogenase could be a marker to analyse both growth and oxidation ability in some acetic acid bacteria, especially those of the genus Acetobacter
additional information
-
applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
additional information
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452, Acetobacter pasteurianus SKU1108
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
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additional information
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
additional information
Acidomonas methanolica JCM6891
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
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additional information
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
additional information
Gluconacetobacter diazotrophicus PAL5
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
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additional information
Gluconacetobacter europaeus
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
additional information
Gluconacetobacter europaeus V3
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
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additional information
Gluconacetobacter intermedius
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
additional information
Gluconacetobacter intermedius JK3
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
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additional information
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
additional information
Gluconacetobacter polyoxogenes NBI1028
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
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additional information
Gluconacetobacter xylinus
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview
additional information
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview; applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview. Development of a DET-based biofuel system by combination of electrodes coated with FAD-dependent fructose dehydrogenase of Gluconobacter sp. as an anode and laccase of mushroom as a cathode
additional information
Gluconobacter oxydans IFO12528
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applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview; applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview. Development of a DET-based biofuel system by combination of electrodes coated with FAD-dependent fructose dehydrogenase of Gluconobacter sp. as an anode and laccase of mushroom as a cathode
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