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
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
CCU55317, -
high similarity between genes encoding subunits I and II of PQQ-ADH
evolution
Frateuria aurantia LMG 1558
-
high similarity between genes encoding subunits I and II of PQQ-ADH
-
malfunction
-
mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
malfunction
-
inactivation of PA1982 by insertion mutagenesis results in inability of the mutant to utilise ethanol and in reduced growth on geraniol. Growth on ethanol is restored by transferring an intact copy of the PA1982 gene into the mutant
malfunction
-
exaA2 and exaA3 mutants are less competitive than the wild type during colonization of rice roots
malfunction
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452, Acetobacter pasteurianus SKU1108
-
mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
-
malfunction
-
exaA2 and exaA3 mutants are less competitive than the wild type during colonization of rice roots
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview; ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview; ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing Q in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
metabolism
Gluconacetobacter diazotrophicus, Gluconacetobacter europaeus, Gluconacetobacter intermedius, Gluconacetobacter polyoxogenes, Gluconacetobacter xylinus, Gluconobacter oxydans
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
Acetobacter lovaniensis IFO3284
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452, Acetobacter pasteurianus SKU1108
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview; ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview; ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
-
metabolism
Acidomonas methanolica JCM6891
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing Q in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
physiological function
Acidomonas methanolica, Gluconacetobacter diazotrophicus, Gluconacetobacter europaeus, Gluconacetobacter intermedius, Gluconacetobacter polyoxogenes, Gluconacetobacter xylinus
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain; PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
-
the PQQ-dependent alcohol dehydrogenase of Pseudomonas aeruginosa functions in ethanol metabolism and is involved in catabolism of acyclic terpenes, overview
physiological function
-
ethanol is an important carbon source for the endophytic life of Azoarcus sp. in Oryza sativa roots
physiological function
Acetobacter lovaniensis IFO3284, Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452, Acetobacter pasteurianus SKU1108
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
-
physiological function
Acidomonas methanolica JCM6891
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
-
physiological function
-
ethanol is an important carbon source for the endophytic life of Azoarcus sp. in Oryza sativa roots
-
physiological function
Gluconacetobacter diazotrophicus PAL5, Gluconacetobacter europaeus V3, Gluconacetobacter intermedius JK3, Gluconacetobacter polyoxogenes NBI1028
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
-
physiological function
Gluconobacter oxydans IFO12528
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain; PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
-
metabolism
Gluconacetobacter diazotrophicus PAL5, Gluconacetobacter europaeus V3, Gluconacetobacter intermedius JK3, Gluconacetobacter polyoxogenes NBI1028, Gluconobacter oxydans IFO12528
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, 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
Acetobacter pasteurianus SKU1108
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-butandiol + ubiquinone
? + ubiquinol
show the reaction diagram
-
very low activity, 0.94% of the activity with ethanol
-
-
?
1,3-propandiol + ubiquinone
? + ubiquinol
show the reaction diagram
-
15% of the activity with ethanol
-
-
?
1-butanol + ubiquinone
butanal + ubiquinol
show the reaction diagram
-
88% of the activity with ethanol
-
-
?
1-hexanol + ubiquinone
hexanal + ubiquinol
show the reaction diagram
-
93% of the activity with ethanol
-
-
?
1-octanol + ubiquinone
octanal + ubiquinol
show the reaction diagram
-
66% of the activity with ethanol
-
-
?
1-pentanol + ubiquinone
pentanal + ubiquinol
show the reaction diagram
-
97% of the activity with ethanol
-
-
?
1-propanol + ubiquinone
propanal + ubiquinol
show the reaction diagram
-
90% of the activity with ethanol
-
-
?
2-butanol + ubiquinone
2-butanone + ubiquinol
show the reaction diagram
-
64% of the activity with ethanol
-
-
?
2-propanol + ubiquinone
acetone + ubiquinol
show the reaction diagram
-
51% of the activity with ethanol
-
-
?
3-methyl-1-butanol + ubiquinone
3-methyl-1-butanal + ubiquinol
show the reaction diagram
-
48% of the activity with ethanol
-
-
?
acetaldehyde + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Gluconacetobacter xylinus
-
42% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
acetaldehyde + ferricyanide
?
show the reaction diagram
Gluconacetobacter xylinus
-
13% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
allyl alcohol + ferricyanide
acrolein + ferricyanide
show the reaction diagram
-
the best substrate
-
-
?
allylic alcohol + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Gluconacetobacter xylinus
-
91% activity compared to n-butanol
-
-
?
allylic alcohol + ferricyanide
?
show the reaction diagram
Gluconacetobacter xylinus
-
96% activity compared to n-butanol
-
-
?
citral + ubiquinol
? + ubiquinone
show the reaction diagram
-
39% of the activity with ethanol
-
-
?
citronellal + ubiquinol
citronellol + ubiquinone
show the reaction diagram
-
45% of the activity with ethanol
-
-
?
citronellol + ubiquinone
citronellal + ubiquinol
show the reaction diagram
-
74% of the activity with ethanol
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
Gluconacetobacter europaeus
Q44002
with phenazine methosulfonate
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
Gluconacetobacter intermedius
Q335V9
with phenazine methosulfonate
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
Q335W4
with phenazine methosulfonate
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
Gluconacetobacter intermedius JK3
Q335V9
with phenazine methosulfonate
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Gluconacetobacter xylinus, Gluconacetobacter xylinus IFO 13693
-
88% activity compared to n-butanol
-
-
?
ethanol + acceptor
acetaldehyde + reduced acceptor
show the reaction diagram
Gluconobacter sp., Gluconobacter sp. 33
-
direct electron-transfer processes between the polypyrrole entrapped quinohemoprotein alcohol dehydrogenase and a platinum electrode take place via the conducting-polymer network, mechanism modelling, overview
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
show the reaction diagram
-
-
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
show the reaction diagram
-
95% of the activity with allyl alcohol
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
show the reaction diagram
-
about 40% of the activity with n-butanol
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
show the reaction diagram
-
electrons extracted from ethanol at PQQ site are transferred to ubiquinone via heme c in subunit I and two of the three hemes c in subunit II
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
show the reaction diagram
Gluconacetobacter xylinus, Gluconacetobacter xylinus IFO 13693
-
91% activity compared to n-butanol
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
show the reaction diagram
Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
-
-
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
show the reaction diagram
Acidomonas methanolica JCM
-
electrons extracted from ethanol at PQQ site are transferred to ubiquinone via heme c in subunit I and two of the three hemes c in subunit II
-
-
?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Gluconacetobacter xylinus
-
-
-
-
?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
-
-
-
?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Gluconacetobacter xylinus IFO 13693
-
-
-
-
?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Gluconacetobacter xylinus, Gluconobacter oxydans
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acidomonas methanolica, Gluconacetobacter europaeus, Gluconacetobacter diazotrophicus, Gluconacetobacter polyoxogenes, Gluconacetobacter intermedius
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
CCU55317, -
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
best substrate
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity, electron transfer mechanism, intramolecular transfer of electrons from pyrroloquinoline quinone to ubiquinone and the quinone binding sites, overview
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus MSU10
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus NCI1452
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Gluconacetobacter diazotrophicus PAL5, Gluconobacter oxydans IFO12528
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Gluconobacter oxydans IFO 12528
-
the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity, electron transfer mechanism, intramolecular transfer of electrons from pyrroloquinoline quinone to ubiquinone and the quinone binding sites, overview
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus KKP584, Gluconacetobacter europaeus V3, Gluconacetobacter intermedius JK3
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus IFO3191
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus IFO3284, Acetobacter pasteurianus SKU1108
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus SKU1108
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter lovaniensis IFO3284, Gluconacetobacter polyoxogenes NBI1028
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Frateuria aurantia LMG 1558
CCU55317
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acidomonas methanolica JCM6891
-
-
-
-
?
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
show the reaction diagram
-
-, electrons extracted from ethanol at PQQ site are transferred to ubiquinone via heme c in subunit I and two of the three hemes c in subunit II
-
-
?
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
show the reaction diagram
Gluconacetobacter xylinus
-
the ADH complex shows a high affinity for ubiquinone-1 with ethanol as cosubstrate
-
-
?
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
show the reaction diagram
Acidomonas methanolica JCM
-
-, electrons extracted from ethanol at PQQ site are transferred to ubiquinone via heme c in subunit I and two of the three hemes c in subunit II
-
-
?
formaldehyde + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Gluconacetobacter xylinus
-
38% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
formaldehyde + ferricyanide
?
show the reaction diagram
Gluconacetobacter xylinus
-
34% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
geraniol + ubiquinone
geranial + ubiquinol
show the reaction diagram
-
37% of the activity with ethanol
-
-
?
glutaraldehyde + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Gluconacetobacter xylinus
-
18% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
glutaraldehyde + ferricyanide
?
show the reaction diagram
Gluconacetobacter xylinus, Gluconacetobacter xylinus IFO 13693
-
8% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
iso-propanol + ferricyanide
propan-2-one + ferrocyanide
show the reaction diagram
-
about 10% of the activity with n-butanol
-
-
?
isopropanol + ferricyanide
propan-2-one + ferrocyanide
show the reaction diagram
-
18% of the activity with allyl alcohol
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
n-butanal + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Gluconacetobacter xylinus
-
100% activity
-
-
?
n-butanol + ferricyanide
n-butanal + ferrocyanide
show the reaction diagram
-
-
-
-
?
n-butanol + ferricyanide
butyraldehyde + ferrocyanide
show the reaction diagram
-
98% of the activity with allyl alcohol
-
-
?
n-pentanol + ferricyanide
n-pentanal + ferrocyanide
show the reaction diagram
-
about 45% of the activity with n-butanol
-
-
?
n-propanol + + 2,6-dichlorophenolindophenol
n-propanal + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Gluconacetobacter xylinus
-
96% activity compared to n-butanol
-
-
?
n-propanol + ferricyanide
n-propanal + ferrocyanide
show the reaction diagram
-
about 95% of the activity with n-butanol
-
-
?
n-propanol + ferricyanide
n-propanal + ferrocyanide
show the reaction diagram
Gluconacetobacter xylinus
-
98% activity compared to n-butanol
-
-
?
n-propanol + ferricyanide
propionaldehyde + ferrocyanide
show the reaction diagram
-
90% of the activity with allyl alcohol
-
-
?
propionaldehyde + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Gluconacetobacter xylinus
-
33% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
propionaldehyde + ferricyanide
?
show the reaction diagram
Gluconacetobacter xylinus
-
24% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
methanol + ferricyanide
formaldehyde + ferrocyanide
show the reaction diagram
-
9% of the activity with allyl alcohol
-
-
?
additional information
?
-
CCU55317, -
substrate specificity, overview
-
-
-
additional information
?
-
Q335W4
the enzyme activity is correlated with resistance to acetic acid, due to lower enzyme activity in the organism, the growth of Acetobacter pasteurianus on high acetic acid concentrations is limited, overview
-
-
-
additional information
?
-
Gluconacetobacter intermedius
Q335V9
the enzyme activity is correlated with resistance to acetic acid, due to lower enzyme activity in the organism, the growth of Gluconacetobacter intermedius on high acetic acid concentrations is limited, overview
-
-
-
additional information
?
-
Gluconacetobacter europaeus
-
the enzyme is involved in the cellular adaptation mechanism to high acetic acid concentrations, overview
-
-
-
additional information
?
-
-
the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview
-
-
-
additional information
?
-
P18278
the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview
-
-
-
additional information
?
-
-
by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles
-
-
-
additional information
?
-
Gluconacetobacter europaeus
Q44002
high alcohol dehydrogenase activity in the Gluconacetobacter europaeus cells and high acetic acid stability of the purified enzyme represent two of the unique features that enable this species to grow and stay metabolically active at extremely high concentrations of acetic acid
-
-
-
additional information
?
-
-
in ADH, electrons pass from PQQH2 to a heme c on the same quinohemoprotein subunit, and then to ubiquinone in the membrane by way of a separate cytochrome c subunit in the three-component membrane complex, ovreview
-
-
-
additional information
?
-
-
no activity with glucose, benzaldehyde, formaldehyde, acetone, sorbitol or glycerol
-
-
-
additional information
?
-
Gluconacetobacter xylinus
-
purified ADH oxidizes primary alcohols (C2-C6) but not methanol
-
-
-
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
-
broad substrate specificity of PQQ-ADH. The organism shows enantiospecific oxidation of alcoholic compounds, e.g. oxidation of prochiral compound 2-methylpropane-1,3-diol to (R)-beta-hydroxyisobutyric acid with 83% enantiomeric excess
-
-
-
additional information
?
-
-
PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
-
additional information
?
-
-
substrate specificity, assayed with dichlorophenolindophenol and phenazinemethosulfate as electron acceptors, overview
-
-
-
additional information
?
-
Acetobacter pasteurianus MSU10
-
broad substrate specificity of PQQ-ADH, PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
-
additional information
?
-
Gluconacetobacter xylinus IFO 13693
-
purified ADH oxidizes primary alcohols (C2-C6) but not methanol
-
-
-
additional information
?
-
Acetobacter pasteurianus NCI1452
-
broad substrate specificity of PQQ-ADH, PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
-
additional information
?
-
Gluconacetobacter diazotrophicus PAL5, Gluconobacter oxydans IFO12528
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
Gluconobacter oxydans IFO12528
-
broad substrate specificity of PQQ-ADH. The organism shows enantiospecific oxidation of alcoholic compounds, e.g. oxidation of prochiral compound 2-methylpropane-1,3-diol to (R)-beta-hydroxyisobutyric acid with 83% enantiomeric excess
-
-
-
additional information
?
-
Acetobacter pasteurianus KKP584
-
broad substrate specificity of PQQ-ADH, PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
-
additional information
?
-
Gluconacetobacter europaeus V3
-
the enzyme is involved in the cellular adaptation mechanism to high acetic acid concentrations, overview
-
-
-
additional information
?
-
Gluconacetobacter europaeus V3, Gluconacetobacter intermedius JK3
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
Gluconacetobacter intermedius JK3
Q335V9
the enzyme activity is correlated with resistance to acetic acid, due to lower enzyme activity in the organism, the growth of Gluconacetobacter intermedius on high acetic acid concentrations is limited, overview
-
-
-
additional information
?
-
Acetobacter pasteurianus IFO3191
-
broad substrate specificity of PQQ-ADH, PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
-
additional information
?
-
Acetobacter pasteurianus SKU1108
-
the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview, by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles
-
-
-
additional information
?
-
Acetobacter pasteurianus SKU1108
-
broad substrate specificity of PQQ-ADH, PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
-
additional information
?
-
Acetobacter lovaniensis IFO3284, Gluconacetobacter polyoxogenes NBI1028
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
Frateuria aurantia LMG 1558
CCU55317
substrate specificity, overview
-
-
-
additional information
?
-
Acidomonas methanolica JCM6891
-
broad substrate specificity of PQQ-ADH, PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Gluconacetobacter xylinus, Gluconobacter oxydans
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acidomonas methanolica, Gluconacetobacter europaeus, Gluconacetobacter diazotrophicus, Gluconacetobacter polyoxogenes, Gluconacetobacter intermedius
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
CCU55317, -
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus MSU10
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus NCI1452
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Gluconacetobacter diazotrophicus PAL5, Gluconobacter oxydans IFO12528
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Gluconobacter oxydans IFO 12528
-
the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus KKP584, Gluconacetobacter europaeus V3, Gluconacetobacter intermedius JK3
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus IFO3191
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus IFO3284, Acetobacter pasteurianus SKU1108
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus SKU1108
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter lovaniensis IFO3284, Gluconacetobacter polyoxogenes NBI1028
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Frateuria aurantia LMG 1558
CCU55317
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acidomonas methanolica JCM6891
-
-
-
-
?
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
show the reaction diagram
Acidomonas methanolica, Acidomonas methanolica JCM
-
-
-
-
?
additional information
?
-
Q335W4
the enzyme activity is correlated with resistance to acetic acid, due to lower enzyme activity in the organism, the growth of Acetobacter pasteurianus on high acetic acid concentrations is limited, overview
-
-
-
additional information
?
-
Gluconacetobacter intermedius
Q335V9
the enzyme activity is correlated with resistance to acetic acid, due to lower enzyme activity in the organism, the growth of Gluconacetobacter intermedius on high acetic acid concentrations is limited, overview
-
-
-
additional information
?
-
Gluconacetobacter europaeus
-
the enzyme is involved in the cellular adaptation mechanism to high acetic acid concentrations, overview
-
-
-
additional information
?
-
-
by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles
-
-
-
additional information
?
-
Gluconacetobacter europaeus
Q44002
high alcohol dehydrogenase activity in the Gluconacetobacter europaeus cells and high acetic acid stability of the purified enzyme represent two of the unique features that enable this species to grow and stay metabolically active at extremely high concentrations of acetic acid
-
-
-
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
-
broad substrate specificity of PQQ-ADH. The organism shows enantiospecific oxidation of alcoholic compounds, e.g. oxidation of prochiral compound 2-methylpropane-1,3-diol to (R)-beta-hydroxyisobutyric acid with 83% enantiomeric excess
-
-
-
additional information
?
-
Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452, Gluconacetobacter diazotrophicus PAL5, Gluconobacter oxydans IFO12528
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
Gluconobacter oxydans IFO12528
-
broad substrate specificity of PQQ-ADH. The organism shows enantiospecific oxidation of alcoholic compounds, e.g. oxidation of prochiral compound 2-methylpropane-1,3-diol to (R)-beta-hydroxyisobutyric acid with 83% enantiomeric excess
-
-
-
additional information
?
-
Acetobacter pasteurianus KKP584
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
Gluconacetobacter europaeus V3
-
the enzyme is involved in the cellular adaptation mechanism to high acetic acid concentrations, overview
-
-
-
additional information
?
-
Gluconacetobacter europaeus V3, Gluconacetobacter intermedius JK3
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
Gluconacetobacter intermedius JK3
Q335V9
the enzyme activity is correlated with resistance to acetic acid, due to lower enzyme activity in the organism, the growth of Gluconacetobacter intermedius on high acetic acid concentrations is limited, overview
-
-
-
additional information
?
-
Acetobacter pasteurianus IFO3191
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
Acetobacter pasteurianus SKU1108
-
by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles
-
-
-
additional information
?
-
Acetobacter pasteurianus SKU1108, Acetobacter lovaniensis IFO3284, Gluconacetobacter polyoxogenes NBI1028, Acidomonas methanolica JCM6891
-
broad substrate specificity of PQQ-ADH
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cytochrome
-
-
-
cytochrome c
-
presence of cytochrome c in both subunits
cytochrome c
Gluconacetobacter xylinus
-
the enzyme contains 4 cytochromes c per enzyme
cytochrome c
-
ADH contains 4 c-type cytochromes
heme
-
4 molecules per enzyme molecule
heme
Gluconobacter sp.
-
eight molecules per enzyme molecule
heme
-
the two subunits of 78000 Da and 55000 Da contain cytochrome c
heme
Gluconacetobacter xylinus
-
the quinohaemoprotein alcohol dehydrogenase contains heme C in both subunits, the ADH complex of contains 18 nmol of heme C per mg of protein (ratio of 3.6 mol of heme C per mol of enzyme)
heme
-
ADH is a typical quinohemoprotein
Heme c
-
electrons extracted from ethanol at PQQ site are transferred to ubiquinone via heme c in subunit I and two of the three hemes c in subunit II; subunit I contains pyrroloquinoline quinone and heme c, and subunit II contains three heme c components, determination of redox potentials at pH 4.5-7.0
Heme c
-
four heme c per enzyme involved in electron transfer for ubiquinone reduction and ubiquinol oxidation
pyrroloquinoline quinone
-
dependent on, 1 molecule per enzyme molecule
pyrroloquinoline quinone
Gluconobacter sp.
-
PQQ, two molecules per enzyme molecule
pyrroloquinoline quinone
Gluconacetobacter intermedius
Q335V9
dependent on
pyrroloquinoline quinone
-
PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview
pyrroloquinoline quinone
-
PQQ, subunit I contains pyrroloquinoline quinone and heme c, and subunit II contains three heme c components
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
PQQ, active in electron transfer, a tightly bound ubiquinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase. The enzyme possesses distinct quinone oxidation, reduction and high affinity binding sites, analysis, overview
pyrroloquinoline quinone
Gluconobacter sp.
-
-
pyrroloquinoline quinone
Gluconacetobacter europaeus
-
dependent on
pyrroloquinoline quinone
-
electrons removed from substrate by alcohol dehydrogenase complex are initially transferred to the pyrroloquinoline quinone centre and further tunnelled across four cytochromes c
pyrroloquinoline quinone
-
PQQ, the PQQ ring is sandwiched between the indole ring of Trp245 and the two sulfur atoms of the disulfide ring structure
pyrroloquinoline quinone
Gluconacetobacter xylinus
-
one pyrroloquinoline quinone is associated with one molecule of the purified ADH complex; the ADH complex contains one mol of pyrroloquinoline quinone
pyrroloquinoline quinone
-
ADH is a typical quinohemoprotein with one pyrroloquinoline quinone
pyrroloquinoline quinone
-
dependent on
pyrroloquinoline quinone
Acetobacter lovaniensis, Acidomonas methanolica, Gluconacetobacter diazotrophicus, Gluconacetobacter europaeus, Gluconacetobacter intermedius, Gluconacetobacter polyoxogenes, Gluconacetobacter xylinus, Gluconobacter oxydans
-
-
pyrroloquinoline quinone
CCU55317, -
dependent on
pyrroloquinoline quinone
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
dependent on, enzyme bound
pyrroloquinoline quinone
-
dependent on
ubiquinone
-
the enzyme has a high affinity ubiquinone binding site besides low-affinity ubiquinone reduction and ubiquinol oxidation sites. The bound ubiquinone in the ubiquinol site is involved in the electron transfer between heme c moieties and bulk ubiquinone or ubiquinol in the low affinity sites
ubiquinone-1
-
electrons extracted from ethanol at PQQ site are transferred to ubiquinone via heme c in subunit I and two of the three hemes c in subunit II
[2Fe-2S]-center
-
ADH contains 5.9 Fe2+ and 2.06 acid-labile sulfurs per heterodimer
additional information
-
an NAD(P)-independent enzyme
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
Gluconobacter sp.
-
required, stabilizes the pyrroloquinoline quinone in the active site
Ca2+
Gluconobacter sp.
-
-
Ca2+
-
the enzyme contains one calcium ion which is required for cofactor binding and stabilization of the pyrroloquinoline quinone semiquinone radical
Ca2+
-
required, two ions, one bound in the active site, and one away from the active site near the N-terminus of the molecule. Dimensions of the active site cavity are provided by the stabilization of the spatial enzyme structure by the second Ca2+ ion
Ca2+
-
required
Fe2+
-
a heme protein
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.9
-
acetaldehyde
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
0.43
-
allylic alcohol
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
-
1.3
-
citral
-
pH 9.0, 30°C
2.4
-
citronellal
-
pH 9.0, 30°C
0.0073
-
citronellol
-
pH 9.0, 30°C
0.0038
-
ethanol
-
pH 9.0, 30°C
0.66
-
ethanol
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
0.025
-
ferricyanide
-
isolated subunit I
0.36
-
n-butanol
Gluconacetobacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
0.0035
-
pyrroloquinoline quinone
-
pH 5.0, 25°C, quinone-bound enzyme, in presence of N-dodecyl-beta-D-maltoside
0.0064
-
pyrroloquinoline quinone
-
pH 5.0, 25°C, quinone-free enzyme, in presence of N-dodecyl-beta-D-maltoside
0.011
-
pyrroloquinoline quinone
-
pH 5.0, 25°C, quinone-free enzyme, in presence of Triton X-100
0.047
-
ubiquinone-1
Gluconacetobacter xylinus
-
using ethanol as cosubstrate, pH and temperature not specified in the publication
0.11
-
geraniol
-
pH 9.0, 30°C
additional information
-
additional information
-
quinone reduction kinetics, overview
-
additional information
-
additional information
Gluconobacter sp.
-
kinetic parameters of the enzymatic behavior in solution (photometric data) and electrochemical characteristics of the immobilized enzymes on different electro-active surfaces are compared
-
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.1
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 1,3-butanediol
1.3
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 1,3-propandiol
3
-
CCU55317, -
enzyme in cell membranes, pH 4.5, 20°C
3.1
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate geraniol
3.3
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate citronellal
3.8
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate citral
4
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 3-methyl-1--butanol
4.4
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 1-octanol in DMSO; purified recombinant enzyme, pH 9.0, 30°C, substrate 2-propanol
4.5
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 1-hexanol in DMSO
5.4
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 2-butanol
5.6
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 1-octanol in H2O
6.3
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate citronellol
7.5
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 1-butanol
7.7
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 1-propanol
7.9
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 1-hexanol in H2O
8.2
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate 1-pentanol
8.5
-
-
purified recombinant enzyme, pH 9.0, 30°C, substrate ethanol
25
40
Gluconobacter sp.
-
purified enzyme
32.2
-
Gluconobacter sp.
-
purified native enzyme
179
-
Gluconacetobacter europaeus
Q44002
purified enzyme
192
-
Gluconacetobacter intermedius
Q335V9
purified enzyme
205
-
Q335W4
purified enzyme
293
-
-
purified native enzyme
additional information
-
Gluconobacter sp.
-
171 U/ml
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
CCU55317, -
-
5
-
-
assay at
5.5
-
Gluconacetobacter xylinus
-
activity responses to pH are sharp, showing two distinct optimal pH values (pH 5.5 and 6.5) depending on the electron acceptor used (optimum pH 5.5 with ferricyanide as electron acceptor)
6
-
Gluconobacter sp.
-
assay at
6
-
-
substrate: ethanol
6.5
-
Gluconacetobacter xylinus
-
activity responses to pH are sharp, showing two distinct optimal pH values (pH 5.5 and 6.5) depending on the electron acceptor used (optimum pH 6.5 when phenazine methosulfate plus 2,6-dichlorophenolindophenol are used as electron acceptors)
7
-
Q335W4
assay at
7
-
Gluconacetobacter europaeus
Q44002
assay at
7
-
Gluconacetobacter intermedius
Q335V9
assay at
7
-
Gluconobacter sp.
-
assay at
7
-
Gluconacetobacter europaeus
-
assay at
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 OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
Gluconobacter sp.
-
assay at
20
-
CCU55317, -
-
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
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
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Acidomonas methanolica JCM
-
-
-
-
Manually annotated by BRENDA team
Gluconacetobacter intermedius
Q335V9
-
Manually annotated by BRENDA team
Gluconacetobacter europaeus
-
-
Manually annotated by BRENDA team
Gluconacetobacter xylinus
-
-
Manually annotated by BRENDA team
-
ubiquinone-reacting subunit, i.e., the subunit II, is responsible for binding to the membrane
Manually annotated by BRENDA team
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452, Acetobacter pasteurianus SKU1108
-
ubiquinone-reacting subunit, i.e., the subunit II, is responsible for binding to the membrane
-
Manually annotated by BRENDA team
Acetobacter sp. SKU 14
-
-
-
Manually annotated by BRENDA team
Frateuria aurantia LMG 1558
-
bound
-
Manually annotated by BRENDA team
Gluconacetobacter diazotrophicus PAL5 (ATCC 49037), Gluconacetobacter europaeus V3, Gluconacetobacter intermedius JK3, Gluconacetobacter xylinus IFO 13693
-
-
-
Manually annotated by BRENDA team
-
at the side of the cytoplasmic membrane
-
Manually annotated by BRENDA team
Acidomonas methanolica JCM
-
at the side of the cytoplasmic membrane
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus SKU1108
-
-
-
-
Manually annotated by BRENDA team
Gluconobacter oxydans IFO 12528
-
bound
-
Manually annotated by BRENDA team
additional information
-
the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane
-
Manually annotated by BRENDA team
additional information
-
the nucleotide sequence of adhS indicates that the 22 kDa protein is synthesized as a preprotein with NH2-terminal 28 amino acids probably acting as a signal sequence for secretion from cytoplasm to periplasm
-
Manually annotated by BRENDA team
additional information
Acetobacter lovaniensis IFO3284, Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452
-
the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane
-
-
Manually annotated by BRENDA team
additional information
Acetobacter pasteurianus SKU1108
-
the nucleotide sequence of adhS indicates that the 22 kDa protein is synthesized as a preprotein with NH2-terminal 28 amino acids probably acting as a signal sequence for secretion from cytoplasm to periplasm; the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane
-
-
Manually annotated by BRENDA team
additional information
Acidomonas methanolica JCM6891, Gluconobacter oxydans IFO12528
-
the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane
-
-
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
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 78000 + x * 55000 + x * 18000, SDS-PAGE
?
Acetobacter sp. SKU 14
-
x * 78000 + x * 55000 + x * 18000, SDS-PAGE
-
dimer
Gluconobacter sp.
-
-
dimer
Gluconacetobacter europaeus
Q44002
1 * 72000 + 1 * 45000, SDS-PAGE
dimer
Gluconacetobacter intermedius
Q335V9
1 * 72000 + 1 * 45000, SDS-PAGE
dimer
-
1 * 71400 + 1 * 43500, SDS-PAGE
dimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
dimer
Gluconacetobacter xylinus
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
dimer
Gluconacetobacter intermedius JK3
-
1 * 72000 + 1 * 45000, SDS-PAGE
-
dimer
Gluconacetobacter polyoxogenes NBI1028
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
-
dimer
Gluconobacter sp. 33
-
-
-
heterodimer
Gluconacetobacter xylinus
-
1 * 68000 + 1 * 41000, SDS-PAGE
heterodimer
-
1 * 71000 + 1 * 44000, SDS-PAGE
heterodimer
CCU55317, -
1 * 72000 + 1 * 45000, SDS-PAGE
heterodimer
Frateuria aurantia LMG 1558
-
1 * 72000 + 1 * 45000, SDS-PAGE
-
heterodimer
Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
-
1 * 71000 + 1 * 44000, SDS-PAGE
-
heterodimer
Gluconacetobacter xylinus IFO 13693
-
1 * 68000 + 1 * 41000, SDS-PAGE
-
trimer
-
heterotrimer with unequal numers of heme groups, overview
trimer
Q335W4
1 * 74000 + 1 * 44000 + 1 * 16000, SDS-PAGE
trimer
Gluconobacter sp.
-
subunit I contains one PQQ and one heme moiety, subunit II contains three heme moieties, and subunit III is a small protein subunit essential for the enzymatic activity providing electron exchange between PQQ and hemes, overview
trimer
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE
trimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE; 1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE; 1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
trimer
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE
trimer
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
trimer
Gluconacetobacter europaeus, Gluconacetobacter intermedius
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
trimer
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE; 1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE
trimer
Acetobacter lovaniensis IFO3284
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE
-
trimer
Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452, Acetobacter pasteurianus SKU1108
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE; 1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE; 1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
Acidomonas methanolica JCM6891
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE
-
trimer
Gluconacetobacter diazotrophicus PAL5
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
-
trimer
Gluconacetobacter europaeus V3, Gluconacetobacter intermedius JK3
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
-
trimer
Gluconobacter oxydans IFO12528
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE; 1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE
-
trimer
Gluconobacter sp. 33
-
subunit I contains one PQQ and one heme moiety, subunit II contains three heme moieties, and subunit III is a small protein subunit essential for the enzymatic activity providing electron exchange between PQQ and hemes, overview
-
homodimer
-
two alpha-subunits
additional information
-
the enzyme shows a propeller structure, QEDH contains a disulfide structure that is similar to the analogous structure in QMDH, EC 1.1.2.8
additional information
Acetobacter pasteurianus SKU1108
-
structure-function relationship, overview
-
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.
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ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ethanol
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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
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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
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme from strain KKP/584, by anion exchange and hydroxylapatite chromatography
Q335W4
native enzyme 130fold from membranes of glycerol-grown cells by two different steps of anion exchange chromatography, solubilization with 0.1% Triton X-100 or Tween 20, copurification with a cytochrome c
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purification of subunit I and of subunit II
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native enzyme from membranes by anion exchange and cation exchange chromatography, followed by hydroxyapatite chromatography, to near homogeneity
CCU55317, -
native enzyme from strain V3, by anion exchange and hydroxylapatite chromatography
Gluconacetobacter europaeus
Q44002
native enzyme from strain JK3, by anion exchange and hydroxylapatite chromatography
Gluconacetobacter intermedius
Q335V9
QAE-Toyopearl 550C column chromatography, DEAE-Toyopearl 650 M column chromatography, HA-Ultrogel column chromatography, and Sephacryl-S200 gel filtration
Gluconacetobacter xylinus
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quinone-bound and quinone-free native enzyme from membranes, purification of an active enzyme is successful with N-dodecyl beta-D-maltoside, but not with Triton X-100
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native enzyme by anion exchange and hydrophobic interaction chromatography, and dialysis against high-viscosity carboxymethyl cellulose as the absorber
Gluconobacter sp.
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recombinant C-terminally His6-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) pLysS RARE by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sequence comparisons, phylogenetic tree
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gene adhA, DNA and amino acid sequence determination and analysis, sequence comparisons
Q335W4
gene adhS, sequence determination and analysis, encoding quinoprotein alcohol dehydrogenase subunit III
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sequence comparisons, phylogenetic tree
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genes exaA2 and exaA3, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
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genes adhA and adhB, encoding subunits I and II, DNA and amino acid sequence determination and analysis,phylogenetic tree
CCU55317, -
gene adh, DNA and amino acid sequence determination and analysis, sequence comparisons
Gluconacetobacter europaeus
Q44002
gene adh, DNA and amino acid sequence determination and analysis, sequence comparisons
Gluconacetobacter intermedius
Q335V9
sequence comparisons, phylogenetic tree
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gene exaA, expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3) pLysS RARE
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EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
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ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
Acetobacter pasteurianus SKU1108
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A26V
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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
-
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
-
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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