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Literature summary 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

EC Number Application Comment Organism
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.5 membrane ubiquinone-reacting subunit, i.e., the subunit II, is responsible for binding to the membrane Acetobacter pasteurianus 16020
-
1.1.5.5 additional information the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane Gluconobacter oxydans
-
-
1.1.5.5 additional information the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane Acetobacter pasteurianus
-
-
1.1.5.5 additional information the subunit III exists freely in the periplasmic space besides in the PQQ-ADH complex on the cytoplasmic membrane Acidomonas methanolica
-
-
1.1.5.5 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.5.5 8000
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE Acidomonas methanolica
1.1.5.5 14000
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE Gluconobacter oxydans
1.1.5.5 15000
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE Acetobacter lovaniensis
1.1.5.5 16000
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
1.1.5.5 16000
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
1.1.5.5 20000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE Acetobacter pasteurianus
1.1.5.5 44000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Komagataeibacter xylinus
1.1.5.5 44000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconobacter oxydans
1.1.5.5 44000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconacetobacter diazotrophicus
1.1.5.5 44000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE Acetobacter pasteurianus
1.1.5.5 44000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconacetobacter polyoxogenes
1.1.5.5 44000
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
1.1.5.5 45000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE Komagataeibacter europaeus
1.1.5.5 45000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE Komagataeibacter intermedius
1.1.5.5 49000
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE Gluconobacter oxydans
1.1.5.5 50000
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE Acetobacter lovaniensis
1.1.5.5 54000
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE Acidomonas methanolica
1.1.5.5 55000
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
1.1.5.5 71000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Komagataeibacter xylinus
1.1.5.5 71000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconobacter oxydans
1.1.5.5 71000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconacetobacter diazotrophicus
1.1.5.5 72000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE Acetobacter pasteurianus
1.1.5.5 72000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE Gluconacetobacter polyoxogenes
1.1.5.5 72000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE Komagataeibacter europaeus
1.1.5.5 72000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE Komagataeibacter intermedius
1.1.5.5 72000
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE Acetobacter lovaniensis
1.1.5.5 74000
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
1.1.5.5 76000
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE Acetobacter pasteurianus
1.1.5.5 80000
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE Acidomonas methanolica
1.1.5.5 85000
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE Gluconobacter oxydans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.5.5 ethanol + ubiquinone Komagataeibacter xylinus
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Gluconobacter oxydans
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Acetobacter pasteurianus
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Acidomonas methanolica
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Komagataeibacter europaeus
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Gluconacetobacter diazotrophicus
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Gluconacetobacter polyoxogenes
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Komagataeibacter intermedius
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Acetobacter lovaniensis
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Acetobacter pasteurianus MSU10
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Komagataeibacter intermedius JK3
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Gluconacetobacter diazotrophicus PAL5
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Acetobacter pasteurianus NCI1452
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Komagataeibacter europaeus V3 / LMG 18494
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Acidomonas methanolica JCM 6891
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Gluconobacter oxydans IFO12528
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Acetobacter pasteurianus KKP584
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Acetobacter pasteurianus IFO3191
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Acetobacter pasteurianus SKU1108
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Acetobacter lovaniensis IFO3284
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Gluconacetobacter polyoxogenes NBI1028
-
acetaldehyde + ubiquinol
-
?
1.1.5.5 additional information Komagataeibacter xylinus broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Gluconobacter oxydans broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Acetobacter pasteurianus broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Acidomonas methanolica broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Komagataeibacter europaeus broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Gluconacetobacter diazotrophicus broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Gluconacetobacter polyoxogenes broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Komagataeibacter intermedius broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Acetobacter lovaniensis broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 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 ?
-
?
1.1.5.5 additional information Acetobacter pasteurianus MSU10 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Komagataeibacter intermedius JK3 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Gluconacetobacter diazotrophicus PAL5 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Acetobacter pasteurianus NCI1452 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Komagataeibacter europaeus V3 / LMG 18494 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Acidomonas methanolica JCM 6891 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Gluconobacter oxydans IFO12528 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 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 ?
-
?
1.1.5.5 additional information Acetobacter pasteurianus KKP584 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Acetobacter pasteurianus IFO3191 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Acetobacter pasteurianus SKU1108 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Acetobacter lovaniensis IFO3284 broad substrate specificity of PQQ-ADH ?
-
?
1.1.5.5 additional information Gluconacetobacter polyoxogenes NBI1028 broad substrate specificity of PQQ-ADH ?
-
?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.5 ethanol + ubiquinone
-
Komagataeibacter xylinus acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Gluconobacter oxydans acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Acetobacter pasteurianus acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Acidomonas methanolica acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Komagataeibacter europaeus acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Gluconacetobacter diazotrophicus acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Gluconacetobacter polyoxogenes acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Komagataeibacter intermedius acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Acetobacter lovaniensis acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Acetobacter pasteurianus MSU10 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Komagataeibacter intermedius JK3 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Gluconacetobacter diazotrophicus PAL5 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Acetobacter pasteurianus NCI1452 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Komagataeibacter europaeus V3 / LMG 18494 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Acidomonas methanolica JCM 6891 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Gluconobacter oxydans IFO12528 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Acetobacter pasteurianus KKP584 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Acetobacter pasteurianus IFO3191 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Acetobacter pasteurianus SKU1108 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Acetobacter lovaniensis IFO3284 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone
-
Gluconacetobacter polyoxogenes NBI1028 acetaldehyde + ubiquinol
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Komagataeibacter xylinus ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Gluconobacter oxydans ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Acidomonas methanolica ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Komagataeibacter europaeus ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Gluconacetobacter diazotrophicus ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Gluconacetobacter polyoxogenes ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Komagataeibacter intermedius ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Acetobacter lovaniensis ?
-
?
1.1.5.5 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 ?
-
?
1.1.5.5 additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus ?
-
?
1.1.5.5 additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acidomonas methanolica ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus MSU10 ?
-
?
1.1.5.5 additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus MSU10 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Komagataeibacter intermedius JK3 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Gluconacetobacter diazotrophicus PAL5 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus NCI1452 ?
-
?
1.1.5.5 additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus NCI1452 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Komagataeibacter europaeus V3 / LMG 18494 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Acidomonas methanolica JCM 6891 ?
-
?
1.1.5.5 additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acidomonas methanolica JCM 6891 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Gluconobacter oxydans IFO12528 ?
-
?
1.1.5.5 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 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus KKP584 ?
-
?
1.1.5.5 additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus KKP584 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus IFO3191 ?
-
?
1.1.5.5 additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus IFO3191 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Acetobacter pasteurianus SKU1108 ?
-
?
1.1.5.5 additional information PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0 Acetobacter pasteurianus SKU1108 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Acetobacter lovaniensis IFO3284 ?
-
?
1.1.5.5 additional information broad substrate specificity of PQQ-ADH Gluconacetobacter polyoxogenes NBI1028 ?
-
?

Subunits

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

Synonyms

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

pH Range

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

Cofactor

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

General Information

EC Number General Information Comment Organism
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 physiological function PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain Gluconobacter oxydans
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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
1.1.5.5 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