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
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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  ⇌ {\displaystyle \rightleftharpoons } acetaldehyde + ubiquinol

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

## References[edit]

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.

## External links[edit]

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

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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

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Coenzyme
* 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)

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