| Synonyms |
ADH, ADH-GS, AdhA, ADHI, ExaA2, ExaA3, formaldehyde-oxidizing enzyme, LEMA_P002680.1, More, PQQ dependent alcohol dehydrogenase, PQQ-ADH, PQQ-alcohol dehydrogenase, PQQ-dependent ADH, PQQ-dependent alcohol dehydrogenase, PQQ-dependent ethanol dehydrogenase, PQQ¨Calcohol dehydrogenase, pyrrolo-quinoline quinone-dependent alcohol dehydrogenase, pyrroloquinoline quinone dependent ADH, pyrroloquinoline quinone dependent alcohol dehydrogenase, pyrroloquinoline quinone-dependent alcohol dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase, pyrroloquinoline quinone¨Calcohol dehydrogenase, pyrroquinoline quinone-dependent alcohol dehydrogenase, QADH, QEDH, QH-ADH, quinocytochrome alcohol dehydrogenase GS, quinohaemoprotein alcohol dehydrogenase, quinohemoprotein alcohol dehydrogenase, quinone-dependent alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenases, YogA |
| Comments |
Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed ‘propeller’ structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidising a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide. |
