1.1.2.8: alcohol dehydrogenase (cytochrome c)
This is an abbreviated version!
For detailed information about alcohol dehydrogenase (cytochrome c), go to the full flat file.
Reaction
+ = + 2 ferrocytochrome c + 2 H+
Synonyms
Ca2+-dependent PQQ-ADH, EC 1.1.99.8, EDH, ethanol dehydrogenase, exaA, exaF, PedE, PedH, PpADH, PP_2674, PP_2679, PQQ-ADH, PQQ-alcohol dehydrogenase, PQQ-dependent alcohol dehydrogenase, PQQ-dependent type I alcohol dehydrogenase, PQQ-DH9, pyrroloquinoline quinone ethanol dehydrogenase, pyrroloquinoline quinone-dependent alcohol dehydrogenases, pyrroloquinoline quinone-dependent dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase, pyrroquinoline quinone-dependent alcohol dehydrogenase, quinoprotein alcohol dehydrogenase
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General Information
General Information on EC 1.1.2.8 - alcohol dehydrogenase (cytochrome c)
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evolution
malfunction
metabolism
physiological function
additional information
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ADHs are categorized into three groups (type I, II, and III ADHs) according to their domain structure and localization. Type I ADHs have molecular and enzymatic properties that are very similar to those of methanol dehydrogenases, MDHs, but they have a low affinity for methanol. Type I ADHs, on the other hand, generally use ethylamine or methylamine as essential activators instead of ammonia
evolution
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quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
evolution
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quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
evolution
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quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
-
evolution
-
ADHs are categorized into three groups (type I, II, and III ADHs) according to their domain structure and localization. Type I ADHs have molecular and enzymatic properties that are very similar to those of methanol dehydrogenases, MDHs, but they have a low affinity for methanol. Type I ADHs, on the other hand, generally use ethylamine or methylamine as essential activators instead of ammonia
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evolution
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quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
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evolution
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quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
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an exaF mutant is not affected for growth with ethanol
malfunction
single deletions of genes coding for PQQ-dependent alcohol dehydrogenases PedE and PedH have only minor effects on growth rates, indicating that Pseudomonas putida strain KT2440 can use both enzymes in a redundant fashion for the metabolization of butanol. Growth of mutants lacking PedE and PedH on n-butanol is significantly impaired, but not completely inhibited, suggesting that additional alcohol dehydrogenases can at least partially complement their function in strain KT2440
malfunction
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inactivation of exaA adversely affects the growth of Azospirillum brasilense on glycerol
malfunction
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
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an exaF mutant is not affected for growth with ethanol
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malfunction
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inactivation of exaA adversely affects the growth of Azospirillum brasilense on glycerol
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malfunction
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single deletions of genes coding for PQQ-dependent alcohol dehydrogenases PedE and PedH have only minor effects on growth rates, indicating that Pseudomonas putida strain KT2440 can use both enzymes in a redundant fashion for the metabolization of butanol. Growth of mutants lacking PedE and PedH on n-butanol is significantly impaired, but not completely inhibited, suggesting that additional alcohol dehydrogenases can at least partially complement their function in strain KT2440
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butanol is oxidized to butyraldehyde by PedE and PedH and then further oxidized to butyric acid by the aldehyde dehydrogenase PedI. Both enzymes, PedE and PedH, are directly involved in butanol oxidation in Pseudomonas putida KT2440
metabolism
KY643658; KY584296
key enzyme in the ethanol oxidase respiratory chain of acetic acid bacteria
metabolism
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the enzyme plays an important role in the catabolism of alcohols in bacteria
metabolism
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the enzyme plays an important role in the catabolism of alcohols in bacteria
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metabolism
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butanol is oxidized to butyraldehyde by PedE and PedH and then further oxidized to butyric acid by the aldehyde dehydrogenase PedI. Both enzymes, PedE and PedH, are directly involved in butanol oxidation in Pseudomonas putida KT2440
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metabolism
Acetobacter pasteurianus JST-S
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key enzyme in the ethanol oxidase respiratory chain of acetic acid bacteria
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the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
physiological function
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ExaF contributes to ethanol metabolism when La3 is present, expanding the role of lanthanides to multicarbon metabolism. ExaA quinoprotein ethanol dehydrogenase, and not the type I ADH,EC 1.1.2.4, is responsible for methanol oxidation in the MDH-3 mutant strain
physiological function
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the enzyme is involved in diethylstilbestrol degradation
physiological function
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the enzyme is involved in diethylstilbestrol degradation
physiological function
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the enzyme is involved in diethylstilbestrol degradation
physiological function
functional redundancy and inverse regulation of PedE (Ca2+-dependent PQQ-ADH) and PedH (lanthanide-dependent PQQ-ADH) represent an adaptive strategy of Pseudomonas putida KT2440 to optimize growth with volatile alcohols in response to the availability of different lanthanides
physiological function
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the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
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physiological function
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
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ExaF contributes to ethanol metabolism when La3 is present, expanding the role of lanthanides to multicarbon metabolism. ExaA quinoprotein ethanol dehydrogenase, and not the type I ADH,EC 1.1.2.4, is responsible for methanol oxidation in the MDH-3 mutant strain
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physiological function
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the enzyme is involved in diethylstilbestrol degradation
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physiological function
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the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
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physiological function
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the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
-
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
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physiological function
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the enzyme is involved in diethylstilbestrol degradation
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the enzyme occurs in active and inactive forms, overview. Active ADHa is brought back by ethanol to its full reduction state, but in inactive ADHi, only one-quarter of the total heme c is reduced, pH dependencies and redox potentials of cofactors, overview
additional information
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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
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ExaF homology modeling using the crystal structure of the quinoprotein ethanol dehydrogenase QEDH from Pseudomonas aeruginosa, PDB 1FLG, overview. Residues E198, D317, D319, and N275 form the active site. Residue D319 might be necessary for lanthanide coordination next to catalytic aspartate D317
additional information
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
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ExaF homology modeling using the crystal structure of the quinoprotein ethanol dehydrogenase QEDH from Pseudomonas aeruginosa, PDB 1FLG, overview. Residues E198, D317, D319, and N275 form the active site. Residue D319 might be necessary for lanthanide coordination next to catalytic aspartate D317
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additional information
-
the enzyme occurs in active and inactive forms, overview. Active ADHa is brought back by ethanol to its full reduction state, but in inactive ADHi, only one-quarter of the total heme c is reduced, pH dependencies and redox potentials of cofactors, overview
-
additional information
-
Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity
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