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
| 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 | ||||||||
| |||||||||
- ethanol + ubiquinone acetaldehyde + ubiquinol
This enzyme is present in acetic acid bacteria where it is involved in acetic acid production.
References
edit- ^ 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
edit- Alcohol+dehydrogenase+(quinone) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
