Information on EC 1.1.5.5 - alcohol dehydrogenase (quinone)

New: Word Map on EC 1.1.5.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
LITERATURE
ethanol + ubiquinone = acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
Acidomonas methanolica JCM
-
-
-
redox reaction
-
-
redox reaction
Acidomonas methanolica JCM
-
-
-
reduction
Acidomonas methanolica JCM
-
-
-
PATHWAY
BRENDA Link
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
COMMENTARY
LITERATURE
ADH
Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
-
-
-
ADH
Komagataeibacter xylinus IFO 13693
-
-
-
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 polyoxogenes NBI1028
-
-
-
PQQ-ADH
Gluconobacter oxydans IFO12528
-
-
-
PQQ-ADH
Komagataeibacter europaeus V3
-
-
-
PQQ-ADH
Komagataeibacter intermedius JK3
-
-
-
PQQ-alcohol dehydrogenase
-
-
PQQ-dependent ADH
Q335W4
-
PQQ-dependent ADH
Gluconobacter sp.
-
-
PQQ-dependent ADH
Gluconobacter sp. 33
-
-
-
PQQ-dependent ADH
Q44002
-
PQQ-dependent ADH
Q335V9
-
PQQ-dependent ADH
Komagataeibacter intermedius JK3
Q335V9
-
-
PQQ-dependent alcohol dehydrogenase
CCU55317
-
PQQ-dependent alcohol dehydrogenase
Frateuria aurantia LMG 1558
CCU55317
-
-
PQQ-dependent alcohol dehydrogenase
Gluconobacter sp.
-
-
PQQ-dependent alcohol dehydrogenase
Gluconobacter sp. 33
-
-
-
PQQ-dependent alcohol dehydrogenase
-
-
PQQ-dependent alcohol dehydrogenase
Komagataeibacter europaeus V3
-
-
-
PQQ-dependent alcohol dehydrogenase
-
-
PQQ-dependent ethanol dehydrogenase
-
-
PQQ-dependent ethanol dehydrogenase
-
-
PQQalcohol dehydrogenase
P18278
-
PQQalcohol 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 quinonealcohol dehydrogenase
P18278
-
pyrroloquinoline quinonealcohol 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
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Gluconacetobacter polyoxogenes NBI1028
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Gluconobacter oxydans IFO12528
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Komagataeibacter europaeus V3
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
Komagataeibacter intermedius JK3
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
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
Gluconobacter sp.
-
-
quinohemoprotein alcohol dehydrogenase
Gluconobacter sp. 33
-
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
Komagataeibacter xylinus IFO 13693
-
-
-
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
UNIPROT
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
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
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
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
strain V3, LMG 18494
-
-
Manually annotated by BRENDA team
strains VA and DSM 6160, gene adh
UniProt
Manually annotated by BRENDA team
Komagataeibacter europaeus V3
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
Komagataeibacter europaeus V3
strain V3, LMG 18494
-
-
Manually annotated by BRENDA team
adh, fragment; strain JK3, gene adh
UniProt
Manually annotated by BRENDA team
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
Komagataeibacter intermedius JK3
adh, fragment; strain JK3, gene adh
UniProt
Manually annotated by BRENDA team
Komagataeibacter 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
Komagataeibacter xylinus IFO 13693
-
-
-
Manually annotated by BRENDA team
gene PA1982 or exaA
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
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
-
exaA2 and exaA3 mutants are less competitive than the wild type during colonization of rice roots
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
-
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
Acetobacter pasteurianus MSU10, Acetobacter pasteurianus NCI1452
-
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
-
malfunction
Acetobacter pasteurianus KKP584, Acetobacter pasteurianus IFO3191, 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
-
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
-
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
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
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 ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
metabolism
Acetobacter pasteurianus MSU10
-
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
Komagataeibacter intermedius JK3
-
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 pasteurianus NCI1452
-
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
Gluconacetobacter diazotrophicus PAL5, 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
-
metabolism
Acetobacter pasteurianus KKP584
-
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
Acetobacter pasteurianus IFO3191
-
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
Komagataeibacter europaeus V3
-
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 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
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
Gluconacetobacter polyoxogenes NBI1028
-
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
-
physiological function
-
ethanol is an important carbon source for the endophytic life of Azoarcus sp. in Oryza sativa roots
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain
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
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
-
the PQQ-dependent alcohol dehydrogenase of Pseudomonas aeruginosa functions in ethanol metabolism and is involved in catabolism of acyclic terpenes, overview
physiological function
Acetobacter pasteurianus MSU10
-
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
Komagataeibacter intermedius JK3
-
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
Acetobacter pasteurianus NCI1452
-
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
-
ethanol is an important carbon source for the endophytic life of Azoarcus sp. in Oryza sativa roots
-
physiological function
Gluconacetobacter diazotrophicus PAL5
-
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
-
physiological function
Acetobacter pasteurianus KKP584, Acetobacter pasteurianus IFO3191
-
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
Komagataeibacter europaeus V3
-
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
Acetobacter pasteurianus SKU1108, Acetobacter lovaniensis IFO3284
-
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
Gluconacetobacter polyoxogenes NBI1028, 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
-
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
-
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
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
-
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
-
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
-
91% activity compared to n-butanol
-
-
?
allylic alcohol + ferricyanide
?
show the reaction diagram
-
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
Q44002
with phenazine methosulfonate
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
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
Komagataeibacter intermedius JK3
Q335V9
with phenazine methosulfonate
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Komagataeibacter xylinus, Komagataeibacter 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
-
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 + ferricyanide
acetaldehyde + ferrocyanide
show the reaction diagram
Komagataeibacter xylinus IFO 13693
-
91% activity compared to n-butanol
-
-
?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
-
-
-
?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Gluconacetobacter diazotrophicus, Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
-
-
-
-
?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
Komagataeibacter xylinus IFO 13693
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
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
Komagataeibacter intermedius JK3, 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
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus IFO3191
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus IFO3284
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Komagataeibacter europaeus V3
-
-
-
-
?
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
-
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
-
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
-
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
-
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
Komagataeibacter xylinus, Komagataeibacter 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
-
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 + 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
-
98% activity compared to n-butanol
-
-
?
n-propanol + ferricyanide
propionaldehyde + ferrocyanide
show the reaction diagram
-
90% of the activity with allyl alcohol
-
-
?
n-propanol + oxidized 2,6-dichlorophenolindophenol
n-propanal + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
96% activity compared to n-butanol
-
-
?
propionaldehyde + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
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
-
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
?
-
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
?
-
-
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
?
-
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
?
-
-
purified ADH oxidizes primary alcohols (C2-C6) but not methanol
-
-
-
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
?
-
Komagataeibacter intermedius JK3
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
Komagataeibacter 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 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
?
-
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
?
-
Komagataeibacter europaeus V3
-
the enzyme is involved in the cellular adaptation mechanism to high acetic acid concentrations, overview
-
-
-
additional information
?
-
Komagataeibacter europaeus V3
-
broad substrate specificity of PQQ-ADH
-
-
-
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
?
-
Komagataeibacter xylinus IFO 13693
-
purified ADH oxidizes primary alcohols (C2-C6) but not methanol
-
-
-
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
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
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
?
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
Komagataeibacter intermedius JK3, 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
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus IFO3191
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Acetobacter pasteurianus IFO3284
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
Komagataeibacter europaeus V3
-
-
-
-
?
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
?
-
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
?
-
-
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
?
-
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. 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, Komagataeibacter intermedius JK3
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
Komagataeibacter 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 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, Acetobacter pasteurianus IFO3191
-
broad substrate specificity of PQQ-ADH
-
-
-
additional information
?
-
Komagataeibacter europaeus V3
-
the enzyme is involved in the cellular adaptation mechanism to high acetic acid concentrations, overview
-
-
-
additional information
?
-
Komagataeibacter europaeus V3
-
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
COMMENTARY
LITERATURE
IMAGE
cytochrome
-
-
-
cytochrome c
-
presence of cytochrome c in both subunits
cytochrome c
-
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
-
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
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
-
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
-
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
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
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
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
-
powerful inhibitor of the purified ADH complex, most likely acting at the ubiquinone acceptor site in subunit II
Myxothiazol
-
powerful inhibitor of the purified ADH complex, most likely acting at the ubiquinone acceptor site in subunit II
Triton X-100
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethanol
-
ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
additional information
-
acetic acid induces the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.9
acetaldehyde
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
0.43
allylic alcohol
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
1.3
citral
-
pH 9.0, 30C
2.4
citronellal
-
pH 9.0, 30C
0.0073
citronellol
-
pH 9.0, 30C
0.0038
ethanol
-
pH 9.0, 30C
0.66
ethanol
-
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
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
0.0035
pyrroloquinoline quinone
-
pH 5.0, 25C, quinone-bound enzyme, in presence of N-dodecyl-beta-D-maltoside
0.0064
pyrroloquinoline quinone
-
pH 5.0, 25C, quinone-free enzyme, in presence of N-dodecyl-beta-D-maltoside
0.011
pyrroloquinoline quinone
-
pH 5.0, 25C, quinone-free enzyme, in presence of Triton X-100
0.047
ubiquinone-1
-
using ethanol as cosubstrate, pH and temperature not specified in the publication
0.11
geraniol
-
pH 9.0, 30C
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
30.8
acetaldehyde
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
67.5
allylic alcohol
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
71
ethanol
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
52.3
n-butanol
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
76.3
ubiquinone-1
-
using ethanol as cosubstrate, pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
446
acetaldehyde
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
90
157
allylic alcohol
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
28106
108
ethanol
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
69
145
n-butanol
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
629
162
ubiquinone-1
-
using ethanol as cosubstrate, pH and temperature not specified in the publication
1150
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1,3-butanediol
1.3
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1,3-propandiol
3
CCU55317
enzyme in cell membranes, pH 4.5, 20C
3.1
-
purified recombinant enzyme, pH 9.0, 30C, substrate geraniol
3.3
-
purified recombinant enzyme, pH 9.0, 30C, substrate citronellal
3.8
-
purified recombinant enzyme, pH 9.0, 30C, substrate citral
4
-
purified recombinant enzyme, pH 9.0, 30C, substrate 3-methyl-1--butanol
4.4
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-octanol in DMSO; purified recombinant enzyme, pH 9.0, 30C, substrate 2-propanol
4.5
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-hexanol in DMSO
5.4
-
purified recombinant enzyme, pH 9.0, 30C, substrate 2-butanol
5.6
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-octanol in H2O
6.3
-
purified recombinant enzyme, pH 9.0, 30C, substrate citronellol
7.5
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-butanol
7.7
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-propanol
7.9
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-hexanol in H2O
8.2
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-pentanol
8.5
-
purified recombinant enzyme, pH 9.0, 30C, substrate ethanol
25 - 40
Gluconobacter sp.
-
purified enzyme
32.2
Gluconobacter sp.
-
purified native enzyme
179
Q44002
purified enzyme
192
Q335V9
purified enzyme
205
Q335W4
purified enzyme
293
-
purified native enzyme
additional information
Gluconobacter sp.
-
171 U/ml
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
CCU55317
-
5.5
-
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
-
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
Gluconobacter sp.
-
assay at
pH RANGE
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
Gluconobacter sp.
-
assay at
20
CCU55317
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
CCU55317
activity range, profile overview. No activity above 50C, maximum activity at 20C
25 - 50
-
25C: about 75% of maximal activity, 50C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7
-
isoelectric focusing
6.1
-
gradient electrophoresis, determined in pH range 3.4-9.0
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the cells are able to grow on up to 10% acetic acid, expression analysis, overview
Manually annotated by BRENDA team
Q44002
the cells show high enzyme activity
Manually annotated by BRENDA team
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37C 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 37C of these thermotolerant strains is superior to that of mesophilic strains IFO3191 and IFO3284 having weak growth and very delayed acetic acid production at 37C even at 4% ethanol
Manually annotated by BRENDA team
Acetobacter pasteurianus MSU10, Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus IFO3284
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37C 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 37C of these thermotolerant strains is superior to that of mesophilic strains IFO3191 and IFO3284 having weak growth and very delayed acetic acid production at 37C even at 4% ethanol
-
Manually annotated by BRENDA team
Komagataeibacter europaeus V3
-
the cells are able to grow on up to 10% acetic acid, expression analysis, overview
-
Manually annotated by BRENDA team
Acetobacter pasteurianus SKU1108
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37C 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 37C of these thermotolerant strains is superior to that of mesophilic strains IFO3191 and IFO3284 having weak growth and very delayed acetic acid production at 37C even at 4% ethanol
-
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 MSU10, Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus IFO3284, 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
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Acidomonas methanolica JCM
-
-
-
-
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 MSU10
-
ubiquinone-reacting subunit, i.e., the subunit II, is responsible for binding to the membrane
-
Manually annotated by BRENDA team
Komagataeibacter intermedius JK3
-
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus NCI1452
-
ubiquinone-reacting subunit, i.e., the subunit II, is responsible for binding to the membrane
-
Manually annotated by BRENDA team
Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
-
-
-
Manually annotated by BRENDA team
Gluconobacter oxydans IFO 12528
-
bound
-
Manually annotated by BRENDA team
Acetobacter sp. SKU 14
-
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus KKP584, Acetobacter pasteurianus IFO3191
-
ubiquinone-reacting subunit, i.e., the subunit II, is responsible for binding to the membrane
-
Manually annotated by BRENDA team
Komagataeibacter europaeus V3
-
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus SKU1108
-
ubiquinone-reacting subunit, i.e., the subunit II, is responsible for binding to the membrane
-
Manually annotated by BRENDA team
Frateuria aurantia LMG 1558
-
bound
-
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
Komagataeibacter xylinus IFO 13693
-
-
-
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
-
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 MSU10, Acetobacter pasteurianus NCI1452, Gluconobacter oxydans IFO12528, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus SKU1108
-
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
-
-
Manually annotated by BRENDA team
additional information
Acetobacter lovaniensis IFO3284, Acidomonas methanolica JCM6891
-
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115000
-
non-denaturing PAGE
687166
119000
-
gel filtration
711032
SUBUNITS
ORGANISM
UNIPROT
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
Q44002
1 * 72000 + 1 * 45000, SDS-PAGE
dimer
Q335V9
1 * 72000 + 1 * 45000, SDS-PAGE
dimer
-
1 * 71400 + 1 * 43500, SDS-PAGE
dimer
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
dimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
dimer
Komagataeibacter intermedius JK3
-
1 * 72000 + 1 * 45000, SDS-PAGE
-
dimer
Gluconobacter sp. 33
-
-
-
dimer
Gluconacetobacter polyoxogenes NBI1028
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
-
heterodimer
CCU55317
1 * 72000 + 1 * 45000, SDS-PAGE
heterodimer
-
1 * 68000 + 1 * 41000, SDS-PAGE
heterodimer
-
1 * 71000 + 1 * 44000, SDS-PAGE
heterodimer
Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
-
1 * 71000 + 1 * 44000, SDS-PAGE
-
heterodimer
Frateuria aurantia LMG 1558
-
1 * 72000 + 1 * 45000, SDS-PAGE
-
heterodimer
Komagataeibacter xylinus IFO 13693
-
1 * 68000 + 1 * 41000, SDS-PAGE
-
trimer
Q335W4
1 * 74000 + 1 * 44000 + 1 * 16000, SDS-PAGE
trimer
-
heterotrimer with unequal numers of heme groups, overview
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 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
trimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE
trimer
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
trimer
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE
trimer
-
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 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE
trimer
Acetobacter pasteurianus MSU10
-
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
Komagataeibacter intermedius JK3
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
-
trimer
Acetobacter pasteurianus NCI1452
-
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
Gluconacetobacter diazotrophicus PAL5, Gluconobacter oxydans IFO12528
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
-
trimer
Gluconobacter oxydans IFO12528
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE
-
trimer
Acetobacter pasteurianus KKP584
-
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
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
-
trimer
Acetobacter pasteurianus IFO3191
-
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
Komagataeibacter europaeus V3
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
-
trimer
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
Acetobacter lovaniensis IFO3284
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE
-
trimer
Acidomonas methanolica JCM6891
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE
-
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
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
-
stable at 6C, overnight
685650
10
-
at 6C, overnight, about 75% inactivation
685650
11
-
at 6C, overnight, complete inactivation
685650
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
10 min, stable
685650
40
-
15 min, 80% loss of activity
687166
45
-
10 min, about 50% loss of activity
685650
45
-
30 min, stable up to
724042
50
-
10 min, 95% loss of activity
685650
additional information
-
ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature
724042
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1% Triton X-100 stabilizes the enzyme
Gluconobacter sp.
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
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 40C 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 40C 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 40C at 22% ethanol
Ethanol
Acetobacter pasteurianus MSU10
-
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 40C 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 40C 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 40C at 22% ethanol
-
Ethanol
Acetobacter pasteurianus IFO3191
-
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 40C 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 40C 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 40C at 22% ethanol
-
Ethanol
Acetobacter pasteurianus IFO3284
-
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 40C 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 40C 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 40C at 22% ethanol
-
Ethanol
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 40C 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 40C 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 40C at 22% ethanol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, purified enzyme in 10 mM potassium phosphate buffer containing 0.1% (v/v) Triton X-100, 30 days, no appreciable loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
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
-
purification of subunit I and of subunit II
-
native enzyme from membranes by anion exchange and cation exchange chromatography, followed by hydroxyapatite chromatography, to near homogeneity
CCU55317
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
-
native enzyme by anion exchange and hydrophobic interaction chromatography, and dialysis against high-viscosity carboxymethyl cellulose as the absorber
Gluconobacter sp.
-
native enzyme from strain V3, by anion exchange and hydroxylapatite chromatography
Q44002
native enzyme from strain JK3, by anion exchange and hydroxylapatite chromatography
Q335V9
QAE-Toyopearl 550C column chromatography, DEAE-Toyopearl 650 M column chromatography, HA-Ultrogel column chromatography, and Sephacryl-S200 gel filtration
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) pLysS RARE by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sequence comparisons, phylogenetic tree
-
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
-
sequence comparisons, phylogenetic tree
-
genes exaA2 and exaA3, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
genes adhA and adhB, encoding subunits I and II, DNA and amino acid sequence determination and analysis,phylogenetic tree
CCU55317
sequence comparisons, phylogenetic tree
-
gene adh, DNA and amino acid sequence determination and analysis, sequence comparisons
Q44002
gene adh, DNA and amino acid sequence determination and analysis, sequence comparisons
Q335V9
gene exaA, expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3) pLysS RARE
-
EXPRESSION
ORGANISM
UNIPROT
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
COMMENTARY
LITERATURE
A26V
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
G55D
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
T104K
-
random mutagenesis, the mutation leads to complpete loss of ethanol oxidizing ability
V107A
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
V36I
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
V54I
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
V70A
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
A26V
Acetobacter pasteurianus SKU1108
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
-
V54I
Acetobacter pasteurianus SKU1108
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
-
L18Q
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
additional information
-
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
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
-
additional information
Acetobacter pasteurianus SKU1108
-
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
-
V70A
Acetobacter pasteurianus SKU1108
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
-
additional information
-
disruption of genes exaA2 and exaA3
additional information
-
disruption of genes exaA2 and exaA3
-
additional information
Gluconobacter sp.
-
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
Gluconobacter sp.
-
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.
-
the enzyme can be used in biosensors, method development, overview
analysis
-
adhA expression is related to the ability to oxidize and grow on ethanol. Differential expression of pyrroloquinoline quinonealcohol 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 lovaniensis IFO3284
-
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
-
analysis
-
adhA expression is related to the ability to oxidize and grow on ethanol. Differential expression of pyrroloquinoline quinonealcohol 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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
analysis
Gluconobacter sp. 33
-
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
-
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
Komagataeibacter europaeus V3
-
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
-
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
Komagataeibacter intermedius JK3
-
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
-
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