ID   1.1.5.5
DE   alcohol dehydrogenase (quinone).
AN   PQQ alcohol dehydrogenase.
AN   PQQ-dependent ADH.
AN   PQQ-dependent alcohol dehydrogenase.
AN   pyrroloquinoline quinone-dependent alcohol dehydrogenase.
AN   quinoprotein ADH.
AN   quinoprotein alcohol dehydrogenase.
AN   type III ADH.
CA   a ubiquinone + ethanol = a ubiquinol + acetaldehyde.
CC   -!- Only described in acetic acid bacteria where it is involved in acetic
CC       acid production.
CC   -!- Associated with membrane.
CC   -!- Electron acceptor is membrane ubiquinone.
CC   -!- A model structure suggests that, like all other quinoprotein alcohol
CC       dehydrogenases, the catalytic subunit has an 8-bladed 'propeller'
CC       structure, a calcium ion bound to the PQQ in the active site and an
CC       unusual disulfide ring structure in close proximity to the PQQ; the
CC       catalytic subunit also has a heme c in the C-terminal domain.
CC   -!- The enzyme has two additional subunits, one of which contains three
CC       molecules of heme c.
CC   -!- It does not require amines for activation.
CC   -!- It has a restricted substrate specificity, oxidizing a few primary
CC       alcohols (C2 to C6), but not methanol, secondary alcohols and some
CC       aldehydes.
CC   -!- It is assayed with phenazine methosulfate or with ferricyanide.
DR   P18278, ADHA_ACEAC ;  O05542, ADHA_GLUOX ;  P28036, ADHA_GLUPO ;
DR   Q44002, ADHA_KOMEU ;  Q47945, ADHB_GLUOX ;  P0A388, ADHB_GLUPO ;
DR   P0A389, ADHB_KOMEU ;
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