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Literature summary for 1.1.5.5 extracted from

  • Yakushi, T.; Matsushita, K.
    Alcohol dehydrogenase of acetic acid bacteria: structure, mode of action, and applications in biotechnology (2010), Appl. Microbiol. Biotechnol., 86, 1257-1265.
    View publication on PubMed

Application

Application Comment Organism
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 Komagataeibacter xylinus
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 Gluconobacter oxydans
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 Acetobacter pasteurianus
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 Acidomonas methanolica
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 Komagataeibacter europaeus
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 Gluconacetobacter diazotrophicus
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 Gluconacetobacter polyoxogenes
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 Komagataeibacter intermedius
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 Acetobacter lovaniensis
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. 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 Gluconobacter oxydans

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane ubiquinone-reacting subunit, i.e., the subunit II, is responsible for binding to the membrane Acetobacter pasteurianus 16020
-
additional information the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane Gluconobacter oxydans
-
-
additional information the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane Acetobacter pasteurianus
-
-
additional information the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane Acidomonas methanolica
-
-
additional information the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane Acetobacter lovaniensis
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
8000
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE Acidomonas methanolica
14000
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE Gluconobacter oxydans
15000
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE Acetobacter lovaniensis
16000
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
16000
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
20000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE Acetobacter pasteurianus
44000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Komagataeibacter xylinus
44000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconobacter oxydans
44000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconacetobacter diazotrophicus
44000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE Acetobacter pasteurianus
44000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconacetobacter polyoxogenes
44000
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
45000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE Komagataeibacter europaeus
45000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE Komagataeibacter intermedius
49000
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE Gluconobacter oxydans
50000
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE Acetobacter lovaniensis
54000
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE Acidomonas methanolica
55000
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
71000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Komagataeibacter xylinus
71000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconobacter oxydans
71000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconacetobacter diazotrophicus
72000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE Acetobacter pasteurianus
72000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconacetobacter polyoxogenes
72000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE Komagataeibacter europaeus
72000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE Komagataeibacter intermedius
72000
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE Acetobacter lovaniensis
74000
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
76000
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
80000
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE Acidomonas methanolica
85000
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE Gluconobacter oxydans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ethanol + ubiquinone Komagataeibacter xylinus
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Gluconobacter oxydans
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Acetobacter pasteurianus
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Acidomonas methanolica
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Komagataeibacter europaeus
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Gluconacetobacter diazotrophicus
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Gluconacetobacter polyoxogenes
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Komagataeibacter intermedius
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Acetobacter lovaniensis
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Acetobacter pasteurianus MSU10
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Komagataeibacter intermedius JK3
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Gluconacetobacter diazotrophicus PAL5
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Acetobacter pasteurianus NCI1452
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Komagataeibacter europaeus V3 / LMG 18494
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Acidomonas methanolica JCM 6891
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Gluconobacter oxydans IFO12528
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Acetobacter pasteurianus KKP584
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Acetobacter pasteurianus IFO3191
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Acetobacter pasteurianus SKU1108
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Acetobacter lovaniensis IFO3284
-
acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone Gluconacetobacter polyoxogenes NBI1028
-
acetaldehyde + ubiquinol
-
?
additional information Komagataeibacter xylinus broad substrate specificity of PQQ-ADH ?
-
?
additional information Gluconobacter oxydans broad substrate specificity of PQQ-ADH ?
-
?
additional information Acetobacter pasteurianus broad substrate specificity of PQQ-ADH ?
-
?
additional information Acidomonas methanolica broad substrate specificity of PQQ-ADH ?
-
?
additional information Komagataeibacter europaeus broad substrate specificity of PQQ-ADH ?
-
?
additional information Gluconacetobacter diazotrophicus broad substrate specificity of PQQ-ADH ?
-
?
additional information Gluconacetobacter polyoxogenes broad substrate specificity of PQQ-ADH ?
-
?
additional information Komagataeibacter intermedius broad substrate specificity of PQQ-ADH ?
-
?
additional information Acetobacter lovaniensis broad substrate specificity of PQQ-ADH ?
-
?
additional information Gluconobacter oxydans 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 broad substrate specificity of PQQ-ADH ?
-
?
additional information Komagataeibacter intermedius JK3 broad substrate specificity of PQQ-ADH ?
-
?
additional information Gluconacetobacter diazotrophicus PAL5 broad substrate specificity of PQQ-ADH ?
-
?
additional information Acetobacter pasteurianus NCI1452 broad substrate specificity of PQQ-ADH ?
-
?
additional information Komagataeibacter europaeus V3 / LMG 18494 broad substrate specificity of PQQ-ADH ?
-
?
additional information Acidomonas methanolica JCM 6891 broad substrate specificity of PQQ-ADH ?
-
?
additional information 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 Acetobacter pasteurianus IFO3191 broad substrate specificity of PQQ-ADH ?
-
?
additional information Acetobacter pasteurianus SKU1108 broad substrate specificity of PQQ-ADH ?
-
?
additional information Acetobacter lovaniensis IFO3284 broad substrate specificity of PQQ-ADH ?
-
?
additional information Gluconacetobacter polyoxogenes NBI1028 broad substrate specificity of PQQ-ADH ?
-
?

Organism

Organism UniProt Comment Textmining
Acetobacter lovaniensis
-
genes adhA, adhB, and adhS encoding the three subunits
-
Acetobacter lovaniensis IFO3284
-
genes adhA, adhB, and adhS encoding the three subunits
-
Acetobacter pasteurianus
-
genes adhA, adhB, and adhS encoding the three subunis
-
Acetobacter pasteurianus
-
genes adhA, adhB, and adhS encoding the three subunits
-
Acetobacter pasteurianus IFO3191
-
genes adhA, adhB, and adhS encoding the three subunits
-
Acetobacter pasteurianus KKP584
-
genes adhA, adhB, and adhS encoding the three subunis
-
Acetobacter pasteurianus MSU10
-
genes adhA, adhB, and adhS encoding the three subunits
-
Acetobacter pasteurianus NCI1452
-
genes adhA, adhB, and adhS encoding the three subunits
-
Acetobacter pasteurianus SKU1108
-
genes adhA, adhB, and adhS encoding the three subunits
-
Acidomonas methanolica
-
genes adhA, adhB, and adhS, encoding the three subunits
-
Acidomonas methanolica JCM 6891
-
genes adhA, adhB, and adhS, encoding the three subunits
-
Gluconacetobacter diazotrophicus
-
genes adhA and adhB, encoding the two subunits
-
Gluconacetobacter diazotrophicus PAL5
-
genes adhA and adhB, encoding the two subunits
-
Gluconacetobacter polyoxogenes
-
genes adhA and adhB, encoding the two subunits
-
Gluconacetobacter polyoxogenes NBI1028
-
genes adhA and adhB, encoding the two subunits
-
Gluconobacter oxydans
-
genes adhA and adhB, encoding the two subunits
-
Gluconobacter oxydans
-
genes adhA, adhB, and adhS, encoding the three subunits
-
Gluconobacter oxydans IFO12528
-
genes adhA, adhB, and adhS, encoding the three subunits
-
Komagataeibacter europaeus
-
-
-
Komagataeibacter europaeus V3 / LMG 18494
-
-
-
Komagataeibacter intermedius
-
genes adhA and adhB, encoding the two subunits
-
Komagataeibacter intermedius JK3
-
genes adhA and adhB, encoding the two subunits
-
Komagataeibacter xylinus
-
genes adhA and adhB, encoding the two subunits
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ethanol + ubiquinone
-
Komagataeibacter xylinus acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Gluconobacter oxydans acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acetobacter pasteurianus acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acidomonas methanolica acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Komagataeibacter europaeus acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Gluconacetobacter diazotrophicus acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Gluconacetobacter polyoxogenes acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Komagataeibacter intermedius acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acetobacter lovaniensis acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acetobacter pasteurianus MSU10 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Komagataeibacter intermedius JK3 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Gluconacetobacter diazotrophicus PAL5 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acetobacter pasteurianus NCI1452 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Komagataeibacter europaeus V3 / LMG 18494 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acidomonas methanolica JCM 6891 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Gluconobacter oxydans IFO12528 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acetobacter pasteurianus KKP584 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acetobacter pasteurianus IFO3191 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acetobacter pasteurianus SKU1108 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acetobacter lovaniensis IFO3284 acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Gluconacetobacter polyoxogenes NBI1028 acetaldehyde + ubiquinol
-
?
additional information broad substrate specificity of PQQ-ADH Komagataeibacter xylinus ?
-
?
additional information broad substrate specificity of PQQ-ADH Gluconobacter oxydans ?
-
?
additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus ?
-
?
additional information broad substrate specificity of PQQ-ADH Acidomonas methanolica ?
-
?
additional information broad substrate specificity of PQQ-ADH Komagataeibacter europaeus ?
-
?
additional information broad substrate specificity of PQQ-ADH Gluconacetobacter diazotrophicus ?
-
?
additional information broad substrate specificity of PQQ-ADH Gluconacetobacter polyoxogenes ?
-
?
additional information broad substrate specificity of PQQ-ADH Komagataeibacter intermedius ?
-
?
additional information broad substrate specificity of PQQ-ADH Acetobacter lovaniensis ?
-
?
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 Gluconobacter oxydans ?
-
?
additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus ?
-
?
additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acidomonas methanolica ?
-
?
additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus MSU10 ?
-
?
additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus MSU10 ?
-
?
additional information broad substrate specificity of PQQ-ADH Komagataeibacter intermedius JK3 ?
-
?
additional information broad substrate specificity of PQQ-ADH Gluconacetobacter diazotrophicus PAL5 ?
-
?
additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus NCI1452 ?
-
?
additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus NCI1452 ?
-
?
additional information broad substrate specificity of PQQ-ADH Komagataeibacter europaeus V3 / LMG 18494 ?
-
?
additional information broad substrate specificity of PQQ-ADH Acidomonas methanolica JCM 6891 ?
-
?
additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acidomonas methanolica JCM 6891 ?
-
?
additional information broad substrate specificity of PQQ-ADH Gluconobacter oxydans IFO12528 ?
-
?
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 Gluconobacter oxydans IFO12528 ?
-
?
additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus KKP584 ?
-
?
additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus KKP584 ?
-
?
additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus IFO3191 ?
-
?
additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus IFO3191 ?
-
?
additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus SKU1108 ?
-
?
additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus SKU1108 ?
-
?
additional information broad substrate specificity of PQQ-ADH Acetobacter lovaniensis IFO3284 ?
-
?
additional information broad substrate specificity of PQQ-ADH Gluconacetobacter polyoxogenes NBI1028 ?
-
?

Subunits

Subunits Comment Organism
dimer 1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Komagataeibacter xylinus
dimer 1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconacetobacter polyoxogenes
trimer 1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconobacter oxydans
trimer 1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconacetobacter diazotrophicus
trimer 1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE Acetobacter pasteurianus
trimer 1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE Komagataeibacter europaeus
trimer 1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE Komagataeibacter intermedius
trimer 1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE Acetobacter lovaniensis
trimer 1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
trimer 1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
trimer 1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE Acidomonas methanolica
trimer 1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE Gluconobacter oxydans

Synonyms

Synonyms Comment Organism
PQQ-ADH
-
Komagataeibacter xylinus
PQQ-ADH
-
Gluconobacter oxydans
PQQ-ADH
-
Acetobacter pasteurianus
PQQ-ADH
-
Acidomonas methanolica
PQQ-ADH
-
Komagataeibacter europaeus
PQQ-ADH
-
Gluconacetobacter diazotrophicus
PQQ-ADH
-
Gluconacetobacter polyoxogenes
PQQ-ADH
-
Komagataeibacter intermedius
PQQ-ADH
-
Acetobacter lovaniensis
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
Komagataeibacter xylinus
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
Gluconobacter oxydans
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
Acetobacter pasteurianus
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
Acidomonas methanolica
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
Komagataeibacter europaeus
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
Gluconacetobacter diazotrophicus
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
Gluconacetobacter polyoxogenes
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
Komagataeibacter intermedius
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
Acetobacter lovaniensis

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
PQQ-ADH has ubiquinone reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus
additional information
-
PQQ-ADH has ubiquinone reductase activity at acidic pH 4.0-5.0 Acetobacter lovaniensis

Cofactor

Cofactor Comment Organism Structure
heme c
-
Acetobacter pasteurianus
heme c
-
Acidomonas methanolica
heme c
-
Acetobacter lovaniensis
pyrroloquinoline quinone
-
Komagataeibacter xylinus
pyrroloquinoline quinone
-
Gluconobacter oxydans
pyrroloquinoline quinone
-
Acetobacter pasteurianus
pyrroloquinoline quinone
-
Acidomonas methanolica
pyrroloquinoline quinone
-
Komagataeibacter europaeus
pyrroloquinoline quinone
-
Gluconacetobacter diazotrophicus
pyrroloquinoline quinone
-
Gluconacetobacter polyoxogenes
pyrroloquinoline quinone
-
Komagataeibacter intermedius
pyrroloquinoline quinone
-
Acetobacter lovaniensis

General Information

General Information Comment Organism
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 Acetobacter pasteurianus
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 Acidomonas methanolica
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 Acetobacter pasteurianus
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 Komagataeibacter xylinus
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 Gluconobacter oxydans
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 Komagataeibacter europaeus
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 Gluconacetobacter diazotrophicus
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 Gluconacetobacter polyoxogenes
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 Komagataeibacter intermedius
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 Acetobacter pasteurianus
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 Acetobacter lovaniensis
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 Acetobacter pasteurianus
physiological function PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain Gluconobacter oxydans
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 Komagataeibacter xylinus
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 Gluconobacter oxydans
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 Acidomonas methanolica
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 Komagataeibacter europaeus
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 Gluconacetobacter diazotrophicus
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 Gluconacetobacter polyoxogenes
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 Komagataeibacter intermedius
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 Acetobacter pasteurianus
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 Acetobacter lovaniensis