KEGG   ENZYME: 1.1.5.5Help
Entry
EC 1.1.5.5                  Enzyme                                 

Name
alcohol dehydrogenase (quinone);
type III ADH;
membrane associated quinohaemoprotein alcohol dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With a quinone or similar compound as acceptor
BRITE hierarchy
Sysname
alcohol:quinone oxidoreductase
Reaction(IUBMB)
ethanol + ubiquinone = acetaldehyde + ubiquinol [RN:R09479]
Reaction(KEGG)
Substrate
ethanol [CPD:C00469];
ubiquinone [CPD:C00399]
Product
acetaldehyde [CPD:C00084];
ubiquinol [CPD:C00390]
Comment
Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide.
History
EC 1.1.5.5 created 2009, modified 2010
Pathway
ec00010  Glycolysis / Gluconeogenesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
ec01130  Biosynthesis of antibiotics
Orthology
K22473  alcohol dehydrogenase (quinone), dehydrogenase subunit
K22474  alcohol dehydrogenase (quinone), cytochrome c subunit
Genes
PGE: LG71_00075 LG71_25665
FAU: Fraau_2339 Fraau_2340
GOX: GOX1067 GOX1068
GOH: B932_1062 B932_1063
GOY: GLS_c11360(adhB3) GLS_c11370(adhA)
GAL: A0U94_12970 A0U94_12975
GDI: GDI2040(adhA) GDI2041(adhB)
GDJ: Gdia_0262 Gdia_0263
GXY: GLX_26600 GLX_26610
GXL: H845_1126 H845_603 H845_604
KSC: CD178_00411(adhA)
APK: APA386B_1574(adhB) APA386B_1575(adhA)
ASZ: ASN_1383(adhA) ASN_1513(adhA) ASN_1514(adhB)
 » show all
Taxonomy
Reference
1  [PMID:18321602]
  Authors
Gomez-Manzo S, Contreras-Zentella M, Gonzalez-Valdez A, Sosa-Torres M, Arreguin-Espinoza R, Escamilla-Marvan E
  Title
The PQQ-alcohol dehydrogenase of Gluconacetobacter diazotrophicus.
  Journal
Int J Food Microbiol 125:71-8 (2008)
DOI:10.1016/j.ijfoodmicro.2007.10.015
Reference
2  [PMID:16636451]
  Authors
Shinagawa E, Toyama H, Matsushita K, Tuitemwong P, Theeragool G, Adachi O
  Title
A novel type of formaldehyde-oxidizing enzyme from the membrane of Acetobacter sp. SKU 14.
  Journal
Biosci Biotechnol Biochem 70:850-7 (2006)
DOI:10.1271/bbb.70.850
Reference
3  [PMID:16233574]
  Authors
Chinnawirotpisan P, Theeragool G, Limtong S, Toyama H, Adachi OO, Matsushita K
  Title
Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ethanol assimilation in Acetobacter  pasteurianus SKU1108.
  Journal
J Biosci Bioeng 96:564-71 (2003)
DOI:10.1016/S1389-1723(04)70150-4
Reference
4  [PMID:9526036]
  Authors
Frebortova J, Matsushita K, Arata H, Adachi O
  Title
Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus: a redox-titration study
  Journal
Biochim Biophys Acta 1363:24-34 (1998)
DOI:10.1016/S0005-2728(97)00090-X
Reference
5  [PMID:18838797]
  Authors
Matsushita K, Kobayashi Y, Mizuguchi M, Toyama H, Adachi O, Sakamoto K, Miyoshi H
  Title
A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans.
  Journal
Biosci Biotechnol Biochem 72:2723-31 (2008)
DOI:10.1271/bbb.80363
Reference
6  [PMID:8617755]
  Authors
Matsushita K, Yakushi T, Toyama H, Shinagawa E, Adachi O
  Title
Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans.
  Journal
J Biol Chem 271:4850-7 (1996)
DOI:10.1074/jbc.271.9.4850
Reference
7
  Authors
Matsushita, K., Takaki, Y., Shinagawa, E., Ameyama, M. and Adachi, O.
  Title
Ethanol oxidase respiratory chain of acetic acid bacteria. Reactivity with ubiquinone of pyrroloquinolinequinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and Gluconobacter suboxydans.
  Journal
Biosci Biotechnol Biochem 56:304-310 (1992)
Reference
8  [PMID:7942316]
  Authors
Matsushita K, Toyama H, Adachi O
  Title
Respiratory chains and bioenergetics of acetic acid bacteria.
  Journal
Adv Microb Physiol 36:247-301 (1994)
Reference
9  [PMID:7772016]
  Authors
Cozier GE, Giles IG, Anthony C
  Title
The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens.
  Journal
Biochem J 308 ( Pt 2):375-9 (1995)
Other DBs
ExplorEnz - The Enzyme Database: 1.1.5.5
IUBMB Enzyme Nomenclature: 1.1.5.5
ExPASy - ENZYME nomenclature database: 1.1.5.5
BRENDA, the Enzyme Database: 1.1.5.5

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