Alcohol dehydrogenase (quinone)

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Alcohol dehydrogenase (quinone)
Alcohol dehydrogenase (quinone)
Identifiers
EC no.	1.1.5.5
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

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

^ Gómez-Manzo S, Contreras-Zentella M, González-Valdez A, Sosa-Torres M, Arreguín-Espinoza R, Escamilla-Marván E (June 2008). "The PQQ-alcohol dehydrogenase of Gluconacetobacter diazotrophicus". International Journal of Food Microbiology. 125 (1): 71–8. doi:10.1016/j.ijfoodmicro.2007.10.015. PMID 18321602.
^ Shinagawa E, Toyama H, Matsushita K, Tuitemwong P, Theeragool G, Adachi O (April 2006). "A novel type of formaldehyde-oxidizing enzyme from the membrane of Acetobacter sp. SKU 14". Bioscience, Biotechnology, and Biochemistry. 70 (4): 850–7. doi:10.1271/bbb.70.850. PMID 16636451.
^ Chinnawirotpisan P, Theeragool G, Limtong S, Toyama H, Adachi OO, Matsushita K (2003). "Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ethanol assimilation in Acetobacter pasteurianus SKU1108". Journal of Bioscience and Bioengineering. 96 (6): 564–71. doi:10.1016/S1389-1723(04)70150-4. PMID 16233574.
^ Frébortova J, Matsushita K, Arata H, Adachi O (January 1998). "Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus: a redox-titration study". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 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 (October 2008). "A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans" (PDF). Bioscience, Biotechnology, and Biochemistry. 72 (10): 2723–31. doi:10.1271/bbb.80363. PMID 18838797. S2CID 23975228. Archived from the original (PDF) on 2019-02-28.
^ Matsushita K, Yakushi T, Toyama H, Shinagawa E, Adachi O (March 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". The Journal of Biological Chemistry. 271 (9): 4850–7. doi:10.1074/jbc.271.9.4850. PMID 8617755.
^ Matsushita, Kazunobu; Takaki, Yoshihiro; Shinagawa, Emiko; Ameyama, Minoru; Adachi, Osao (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 (2): 304–310. doi:10.1271/bbb.56.304. PMID 27823530.
^ Matsushita K, Toyama H, Adachi O (1994). "Respiratory chains and bioenergetics of acetic acid bacteria". Advances in Microbial Physiology. 36: 247–301. doi:10.1016/s0065-2911(08)60181-2. ISBN 9780120277360. PMID 7942316.
^ Cozier GE, Giles IG, Anthony C (June 1995). "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens". The Biochemical Journal. 308 ( Pt 2) (2): 375–9. doi:10.1042/bj3080375. PMC 1136936. PMID 7772016.

External links

Alcohol+dehydrogenase+(quinone) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Gómez-Manzo S, Contreras-Zentella M, González-Valdez A, Sosa-Torres M, Arreguín-Espinoza R, Escamilla-Marván E (June 2008). "The PQQ-alcohol dehydrogenase of Gluconacetobacter diazotrophicus". International Journal of Food Microbiology. 125 (1): 71–8. doi:10.1016/j.ijfoodmicro.2007.10.015. PMID 18321602.

[2] Shinagawa E, Toyama H, Matsushita K, Tuitemwong P, Theeragool G, Adachi O (April 2006). "A novel type of formaldehyde-oxidizing enzyme from the membrane of Acetobacter sp. SKU 14". Bioscience, Biotechnology, and Biochemistry. 70 (4): 850–7. doi:10.1271/bbb.70.850. PMID 16636451.

[3] Chinnawirotpisan P, Theeragool G, Limtong S, Toyama H, Adachi OO, Matsushita K (2003). "Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ethanol assimilation in Acetobacter pasteurianus SKU1108". Journal of Bioscience and Bioengineering. 96 (6): 564–71. doi:10.1016/S1389-1723(04)70150-4. PMID 16233574.

[4] Frébortova J, Matsushita K, Arata H, Adachi O (January 1998). "Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus: a redox-titration study". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1363 (1): 24–34. doi:10.1016/s0005-2728(97)00090-x. PMID 9526036.

[5] Matsushita K, Kobayashi Y, Mizuguchi M, Toyama H, Adachi O, Sakamoto K, Miyoshi H (October 2008). "A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans" (PDF). Bioscience, Biotechnology, and Biochemistry. 72 (10): 2723–31. doi:10.1271/bbb.80363. PMID 18838797. S2CID 23975228. Archived from the original (PDF) on 2019-02-28.

[6] Matsushita K, Yakushi T, Toyama H, Shinagawa E, Adachi O (March 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". The Journal of Biological Chemistry. 271 (9): 4850–7. doi:10.1074/jbc.271.9.4850. PMID 8617755.

[7] Matsushita, Kazunobu; Takaki, Yoshihiro; Shinagawa, Emiko; Ameyama, Minoru; Adachi, Osao (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 (2): 304–310. doi:10.1271/bbb.56.304. PMID 27823530.

[8] Matsushita K, Toyama H, Adachi O (1994). "Respiratory chains and bioenergetics of acetic acid bacteria". Advances in Microbial Physiology. 36: 247–301. doi:10.1016/s0065-2911(08)60181-2. ISBN 9780120277360. PMID 7942316.

[9] Cozier GE, Giles IG, Anthony C (June 1995). "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens". The Biochemical Journal. 308 ( Pt 2) (2): 375–9. doi:10.1042/bj3080375. PMC 1136936. PMID 7772016.

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v t e 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: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
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 Alcohol 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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)