1.1.2.8	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	-, 742110	
1.1.2.8	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	-, 741733	
1.1.2.8	malfunction	an exaF mutant is not affected for growth with ethanol	-, 742793	
1.1.2.8	malfunction	inactivation of exaA adversely affects the growth of Azospirillum brasilense on glycerol	-, 763204	
1.1.2.8	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	-, 743174	
1.1.2.8	metabolism	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	-, 743174	
1.1.2.8	metabolism	key enzyme in the ethanol oxidase respiratory chain of acetic acid bacteria	-, 763081	
1.1.2.8	metabolism	the enzyme plays an important role in the catabolism of alcohols in bacteria	-, 763204	
1.1.2.8	additional information	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	-, 742793	
1.1.2.8	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	-, 725041	
1.1.2.8	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	-, 725154	
1.1.2.8	physiological function	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	-, 742793	
1.1.2.8	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	763417	
1.1.2.8	physiological function	the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation	-, 724042	
1.1.2.8	physiological function	the enzyme is involved in diethylstilbestrol degradation	-, 741733