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1.1.5.5: alcohol dehydrogenase (quinone)

This is an abbreviated version!
For detailed information about alcohol dehydrogenase (quinone), go to the full flat file.

Word Map on EC 1.1.5.5

Reaction

ethanol
+
ubiquinone
=
acetaldehyde
+
ubiquinol

Synonyms

ADD, ADH, ADH I, ADH IIB, ADH IIG, ADH-1, ADH-GS, ADH-IIB, ADH-IIG, AdhA, ADHI, ADHIIB, ADHIIG, alcohol dehydrogenase, bacterial methanol dehydrogenase, BDH, BOH, calcium-containing quinoprotein methanol dehydrogenase, EC 1.1.99.8, exaA, ExaA2, ExaA3, formaldehyde-oxidizing enzyme, GLDH, glycerol dehydrogenase, LEMA_P002680.1, lupanine hydroxylase (PQQ/heme c), MDH, MDH-PQQ, MEDH, MEDH-PD, membrane quinohaemoprotein alcohol dehydrogenase, membrane-bound alcohol dehydrogenase, methanol dehydrogenase, More, NAD+-independent, PQQ-containing alcohol dehydrogenase, PedE, PedH, PEGDH, polyethyleneglycol dehydrogenase, polypropylene glycol dehydrogenase, polypropyleneglycol dehydrogenase, polyvinylalcohol dehydrogenase, PPG-DH, PPGDH, PQQ ADH, PQQ alcohol dehydrogenase, PQQ dependent alcohol dehydrogenase, PQQ methanol dehydrogenase, PQQ-ADH, PQQ-alcohol dehydrogenase, PQQ-containing methanol dehydrogenase, PQQ-dependent ADH, PQQ-dependent alcohol dehydrogenase, PQQ-dependent alcohol oxidase, PQQ-dependent ethanol dehydrogenase, PQQ-dependent quinoprotein ethanol dehydrogenase, PQQ-linked alcohol dehydrogenase, PQQalcohol dehydrogenase, PVADH, pyrrolo-quinoline quinone-dependent alcohol dehydrogenase, pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenase, pyrroloquinoline quinone -dependent quinoprotein ethanol dehydrogenase, pyrroloquinoline quinone dependent ADH, pyrroloquinoline quinone dependent alcohol dehydrogenase, pyrroloquinoline quinone methanol dehydrogenase, pyrroloquinoline quinone-dependent alcohol dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenase, pyrroloquinoline quinonealcohol dehydrogenase, pyrroquinoline quinone-dependent alcohol dehydrogenase, Q-bound ADH, QADH, QEDH, QH-ADH, quinocytochrome alcohol dehydrogenase GS, quinocytochrome alcohol dehydrogenase IIB, quinohaemoprotein alcohol dehydrogenase, quinohemoprotein (type II) alcohol dehydrogenase, quinohemoprotein alcohol dehydrogenase, quinohemoprotein dehydrogenase, quinohemoprotein ethanol dehydrogenase, quinohemoprotein-cytochrome c complex alcohol dehydrogenase, quinone dependent alcohol dehydrogenase, quinone-dependent alcohol dehydrogenase, quinoprotein ADH, quinoprotein alcohol dehydrogenase, quinoprotein dehydrogenase, quinoprotein ethanol dehydrogenase, quinoprotein MDG, quinoprotein methanol dehydrogenase, tetrahydrofurfuryl alcohol dehydrogenase, THFA-DH, THFADH, type I ADH (PQQ), type II ADH, type II ADH (PQQ/heme c), type II quinohemoprotein alcohol dehydrogenase, type III ADH (PQQ/heme c /3 hemes c), vanillyl alcohol dehydrogenase, YogA

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.5 With a quinone or similar compound as acceptor
                1.1.5.5 alcohol dehydrogenase (quinone)

Application

Application on EC 1.1.5.5 - alcohol dehydrogenase (quinone)

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biofuel production
-
comparison of a direct electron transfer bioanode containing both PQQ-ADH (pyrroloquinoline quinone-dependent alcohol dehydrogenase) and PQQ-AldDH (PQQ-dependent aldehyde dehydrogenase) immobilized onto different modified electrode surfaces employing either a tetrabutylammonium-modified Nafion membrane polymer or polyamidoamine (PAMAM) dendrimers. The prepared bioelectrodes are able to undergo direct electron transfer onto glassy carbon surface in the presence as well as the absence of multi-walled carbon nanotubes, also, in the latter case a relevant shift in the oxidation peak of about 180 mV vs. saturated calomel electrode is observed
additional information