EC Number   |
General Information |
Reference  |
|---|
   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 | more |
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 | more |
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 | 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 | physiological function |
the enzyme is involved in diethylstilbestrol degradation |
-, 741733 |
| 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 | malfunction |
an exaF mutant is not affected for growth with ethanol |
-, 742793 |
| 1.1.2.8 | more |
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 | 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 | 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 |
