alcohol dehydrogenase (quinone);
type III ADH;
membrane associated quinohaemoprotein alcohol dehydrogenase

Oxidoreductases;
Acting on the CH-OH group of donors;
With a quinone or similar compound as acceptor

alcohol:quinone oxidoreductase

ethanol + ubiquinone = acetaldehyde + ubiquinol [RN:R09479]

R09479

ethanol [CPD:C00469];
ubiquinone [CPD:C00399]

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, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide.

1  [PMID:18321602]

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 (2008) 71-8.

Gluconacetobacter diazotrophicus [GN:gdi gdj]

2  [PMID:16636451]

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 (2006) 850-7.

Acetobacter sp.

3  [PMID:16233574]

Chinnawirotpisan P, Theeragool G, Limtong S, Toyama H, Adachi OO, 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 (2003) 564-71.

Acetobacter pasteurianus [GN:apt]

4  [PMID:9526036]

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 (1998) 24-34.

Acetobacter methanolicus

5  [PMID:18838797]

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 (2008) 2723-31.

Gluconobacter suboxydans

6  [PMID:8617755]

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 (1996) 4850-7.

Gluconobacter suboxydans

7

Matsushita, K., Takaki, Y., Shinagawa, E., Ameyama, M. and Adachi, O.

Ethanol oxidase respiratory chain of acetic acid bacteria. Reactivity with ubiquinone of pyrroloquinolinequinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and Gluconobacter suboxydans.

Biosci. Biotechnol. Biochem. 56 (1992) 304-310.

8  [PMID:7942316]

Matsushita K, Toyama H, Adachi O

Respiratory chains and bioenergetics of acetic acid bacteria.

Adv. Microb. Physiol. 36 (1994) 247-301.

9  [PMID:7772016]

Cozier GE, Giles IG, Anthony C

The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens.

Biochem. J. 308 ( Pt 2) (1995) 375-9.

Acetobacter aceti