EC - Alcohol dehydrogenase (quinone)

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IntEnz Enzyme Nomenclature


Accepted name:
alcohol dehydrogenase (quinone)
Other names:
PQQ alcohol dehydrogenase
PQQ-dependent ADH
PQQ-dependent alcohol dehydrogenase
pyrroloquinoline quinone-dependent alcohol dehydrogenase
quinoprotein ADH
quinoprotein alcohol dehydrogenase
type III ADH
membrane associated quinohemoprotein alcohol dehydrogenase
Systematic name:
alcohol:quinone oxidoreductase




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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Gomez-Manzo, S., Contreras-Zentella, M., Gonzalez-Valdez, A., Sosa-Torres, M., Arreguin-Espinoza, R., Escamilla-Marvan, E.
    The PQQ-alcohol dehydrogenase of Gluconacetobacter diazotrophicus.
    Int. J. Food Microbiol. 125: 71-78 (2008). [PMID: 18321602]
  2. Shinagawa, E., Toyama, H., Matsushita, K., Tuitemwong, P., Theeragool, G., Adachi, O.
    A novel type of formaldehyde-oxidizing enzyme from the membrane of Acetobacter sp. SKU 14.
    Biosci. Biotechnol. Biochem. 70: 850-857 (2006). [PMID: 16636451]
  3. Chinnawirotpisan, P., Theeragool, G., Limtong, S., Toyama, H., Adachi, O. O., Matsushita, K.
    Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ethanol assimilation in Acetobacter pasteurianus SKU1108.
    J. Biosci. Bioeng. 96: 564-571 (2003). [PMID: 16233574]
  4. Frebortova, J., Matsushita, K., Arata, H., Adachi, O.
    Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus: a redox-titration study
    Biochim. Biophys. Acta 1363: 24-34 (1998). [PMID: 9526036]
  5. Matsushita, K., Kobayashi, Y., Mizuguchi, M., Toyama, H., Adachi, O., Sakamoto, K., Miyoshi, H.
    A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans.
    Biosci. Biotechnol. Biochem. 72: 2723-2731 (2008). [PMID: 18838797]
  6. Matsushita, K., Yakushi, T., Toyama, H., Shinagawa, E., Adachi, O.
    Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans.
    J. Biol. Chem. 271: 4850-4857 (1996). [PMID: 8617755]
  7. atsushita, K., Takaki, Y., Shinagawa, E., Ameyama, M. and Adachi, O.
    Ethanol oxidase respiratory chain of acetic acid bacteria-reactivity with ubiquinone of pyrroloquinoline quinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and Gluconobacter suboxydans.
    Biosci. Biotechnol. Biochem. 56: 304-310 (1992).
  8. Matsushita, K., Toyama, H., Adachi, O.
    Respiratory chains and bioenergetics of acetic acid bacteria.
    Adv. Microb. Physiol. 36: 247-301 (1994). [PMID: 7942316]
  9. Cozier, G. E., Giles, I. G., Anthony, C.
    The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens.
    Biochem. J. 308: 375-379 (1995). [PMID: 7772016]

[EC created 2009, modified 2010]