Alcohol dehydrogenase (quinone)

Alcohol dehydrogenase (quinone) (EC 1.1.5.5, type III ADH, membrane associated quinohaemoprotein alcohol dehydrogenase) is an enzyme with systematic name alcohol:quinone oxidoreductase.^[1]^[2]^[3]^[4]^[5]^[6]^[7]^[8]^[9] This enzyme catalyses the following chemical reaction

ethanol + ubiquinone

\rightleftharpoons

acetaldehyde + ubiquinol

This enzyme is present in acetic acid bacteria where it is involved in acetic acid production.

References

↑ Gomez-Manzo, S.; Contreras-Zentella, M.; Gonzalez-Valdez, A.; Sosa-Torres, M.; Arreguin-Espinoza, R.; Escamilla-Marvan, E. (2008). "The PQQ-alcohol dehydrogenase of Gluconacetobacter diazotrophicus". Int. J. Food Microbiol. 125 (1): 71–78. doi:10.1016/j.ijfoodmicro.2007.10.015. PMID 18321602.
↑ Shinagawa, E.; Toyama, H.; Matsushita, K.; Tuitemwong, P.; Theeragool, G.; Adachi, O. (2006). "A novel type of formaldehyde-oxidizing enzyme from the membrane of Acetobacter sp. SKU 14". Biosci. Biotechnol. Biochem. 70 (4): 850–857. doi:10.1271/bbb.70.850. PMID 16636451.
↑ Chinnawirotpisan, P.; Theeragool, G.; Limtong, S.; Toyama, H.; Adachi, O.O.; Matsushita, K. (2003). "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 (6): 564–571. doi:10.1016/S1389-1723(04)70150-4. PMID 16233574.
↑ Frebortova, J.; Matsushita, K.; Arata, H.; Adachi, O. (1998). "Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus: a redox-titration stud". Biochim. Biophys. Acta. 1363 (1): 24–34. doi:10.1016/s0005-2728(97)00090-x. PMID 9526036.
↑ Matsushita, K.; Kobayashi, Y.; Mizuguchi, M.; Toyama, H.; Adachi, O.; Sakamoto, K.; Miyoshi, H. (2008). "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 (10): 2723–2731. doi:10.1271/bbb.80363. PMID 18838797.
↑ Matsushita, K.; Yakushi, T.; Toyama, H.; Shinagawa, E.; Adachi, O. (1996). "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 (9): 4850–4857. doi:10.1074/jbc.271.9.4850. PMID 8617755.
↑ Matsushita, K.; Takaki, Y.; Shinagawa, E.; Ameyama, M.; Adachi, O. (1992). "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. doi:10.1271/bbb.56.304.
↑ Matsushita, K.; Toyama, H.; Adachi, O. (1994). "Respiratory chains and bioenergetics of acetic acid bacteria". Adv. Microb. Physiol. 36: 247–301. doi:10.1016/s0065-2911(08)60181-2. PMID 7942316.
↑ Cozier, G.E.; Giles, I.G.; Anthony, C. (1995). "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens". Biochem. J. 308: 375–379. PMC 1136936. PMID 7772016.

External links

Alcohol dehydrogenase (quinone) at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3 Beta 3-beta-HSD NSDHL 11 Beta HSD11B1 HSD11B2 17 Beta

1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase

1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)

1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase

1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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