EC Number |
Natural Substrates |
---|
1.2.5.2 | 1-butanol + acceptor |
the NAD+-independent inducible 1-butanol dehydrogenase, a quinohemoprotein, is responsible for 1-butanol oxidation in the butane metabolism pathway |
1.2.5.2 | acetaldehyde + a quinone + H2O |
- |
1.2.5.2 | acetaldehyde + a quinone + H2O |
potassium ferricyanide, phenazine methosulfate, nitro blue tetrazolium or dichlorophenol-indophenol as artificial electron acceptors |
1.2.5.2 | acetaldehyde + ubiquinone |
electrons removed from substrate by alcohol dehydrogenase complex are initially transferred to the pyrroloquinoline quinone centre and further tunnelled across four cytochromes c to the membrane ubiquinone |
1.2.5.2 | more |
the NAD+-independent PQQ alcohol dehydrogenase BOH (a quinoprotein) is linked to butane metabolism in conjunction with BDH (a quinohemoprotein) |
1.2.5.2 | more |
three distinct quinoprotein ADHs (ADHs, ADH IIB and ADH IIG) are synthesized by the bacterium under different growth conditions. ADH I is formed most abundantly in the cells grown on ethanol |
1.2.5.2 | more |
three distinct quinoprotein ADHs (ADHs, ADH IIB and ADH IIG) are synthesized by the bacterium under different growth conditions. ADH IIB is induced by n-butanol, 1,3-butandiol, and alcohols of medium chain length |
1.2.5.2 | more |
three distinct quinoprotein ADHs (ADHs, ADH IIB and ADH IIG) are synthesized by the bacterium under different growth conditions. Induction of ADH IIG is restricted to 1,2-propanediol or glycerol |