From Wikipedia, the free encyclopedia
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
^ 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
Activity Regulation Classification Kinetics Types