Alcohol dehydrogenase (quinone)

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Alcohol dehydrogenase (quinone)
Identifiers
EC no. 1.1.5.5
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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 acetaldehyde + ubiquinol

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

References

  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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