Alcohol dehydrogenase (quinone)

Alcohol dehydrogenase (quinone)
Identifiers
EC number 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

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. ↑ 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.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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. PMID 27823530.
  8. ↑ 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.
  9. ↑ 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.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.