1.1.5.5: alcohol dehydrogenase (quinone) This is an abbreviated version! For detailed information about alcohol dehydrogenase (quinone), go to the full flat file .
Reaction
ethanol +
ubiquinone =
acetaldehyde +
ubiquinol
Synonyms ADD, ADH, ADH I, ADH IIB, ADH IIG, ADH-1, ADH-GS, ADH-IIB, ADH-IIG, AdhA, ADHI, ADHIIB, ADHIIG, alcohol dehydrogenase, bacterial methanol dehydrogenase, BDH, BOH, calcium-containing quinoprotein methanol dehydrogenase, EC 1.1.99.8, exaA, ExaA2, ExaA3, formaldehyde-oxidizing enzyme, GLDH, glycerol dehydrogenase, LEMA_P002680.1, lupanine hydroxylase (PQQ/heme c), MDH, MDH-PQQ, MEDH, MEDH-PD, membrane quinohaemoprotein alcohol dehydrogenase, membrane-bound alcohol dehydrogenase, methanol dehydrogenase, More, NAD+-independent, PQQ-containing alcohol dehydrogenase, PedE, PedH, PEGDH, polyethyleneglycol dehydrogenase, polypropylene glycol dehydrogenase, polypropyleneglycol dehydrogenase, polyvinylalcohol dehydrogenase, PPG-DH, PPGDH, PQQ ADH, PQQ alcohol dehydrogenase, PQQ dependent alcohol dehydrogenase, PQQ methanol dehydrogenase, PQQ-ADH, PQQ-alcohol dehydrogenase, PQQ-containing methanol dehydrogenase, PQQ-dependent ADH, PQQ-dependent alcohol dehydrogenase, PQQ-dependent alcohol oxidase, PQQ-dependent ethanol dehydrogenase, PQQ-dependent quinoprotein ethanol dehydrogenase, PQQ-linked alcohol dehydrogenase, PQQ–alcohol dehydrogenase, PVADH, pyrrolo-quinoline quinone-dependent alcohol dehydrogenase, pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenase, pyrroloquinoline quinone -dependent quinoprotein ethanol dehydrogenase, pyrroloquinoline quinone dependent ADH, pyrroloquinoline quinone dependent alcohol dehydrogenase, pyrroloquinoline quinone methanol dehydrogenase, pyrroloquinoline quinone-dependent alcohol dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenase, pyrroloquinoline quinone–alcohol dehydrogenase, pyrroquinoline quinone-dependent alcohol dehydrogenase, Q-bound ADH, QADH, QEDH, QH-ADH, quinocytochrome alcohol dehydrogenase GS, quinocytochrome alcohol dehydrogenase IIB, quinohaemoprotein alcohol dehydrogenase, quinohemoprotein (type II) alcohol dehydrogenase, quinohemoprotein alcohol dehydrogenase, quinohemoprotein dehydrogenase, quinohemoprotein ethanol dehydrogenase, quinohemoprotein-cytochrome c complex alcohol dehydrogenase, quinone dependent alcohol dehydrogenase, quinone-dependent alcohol dehydrogenase, quinoprotein ADH, quinoprotein alcohol dehydrogenase, quinoprotein dehydrogenase, quinoprotein ethanol dehydrogenase, quinoprotein MDG, quinoprotein methanol dehydrogenase, tetrahydrofurfuryl alcohol dehydrogenase, THFA-DH, THFADH, type I ADH (PQQ), type II ADH, type II ADH (PQQ/heme c), type II quinohemoprotein alcohol dehydrogenase, type III ADH (PQQ/heme c /3 hemes c), vanillyl alcohol dehydrogenase, YogA
ECTree
Cofactor
Cofactor on EC 1.1.5.5 - alcohol dehydrogenase (quinone)
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ubiquinone
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the enzyme has a high affinity ubiquinone binding site besides low-affinity ubiquinone reduction and ubiquinol oxidation sites. The bound ubiquinone in the ubiquinol site is involved in the electron transfer between heme c moieties and bulk ubiquinone or ubiquinol in the low affinity sites
ubiquinone-1
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electrons extracted from ethanol at PQQ site are transferred to ubiquinone via heme c in subunit I and two of the three hemes c in subunit II
[2Fe-2S]-center
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ADH contains 5.9 Fe2+ and 2.06 acid-labile sulfurs per heterodimer
cytochrome c
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presence of cytochrome c in both subunits
cytochrome c
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ADH contains 4 c-type cytochromes
cytochrome c
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the enzyme contains 4 cytochromes c per enzyme
heme
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heme
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4 molecules per enzyme molecule
heme
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eight molecules per enzyme molecule
heme
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the two subunits of 78000 Da and 55000 Da contain cytochrome c
heme
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ADH is a typical quinohemoprotein
heme
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the quinohaemoprotein alcohol dehydrogenase contains heme C in both subunits, the ADH complex of contains 18 nmol of heme C per mg of protein (ratio of 3.6 mol of heme C per mol of enzyme)
heme c
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heme c
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four heme c per enzyme involved in electron transfer for ubiquinone reduction and ubiquinol oxidation
heme c
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type III ADH is a quinohemoprotein able to oxidize alcohols
heme c
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type III ADH is a quinohemoprotein able to oxidize alcohols
heme c
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type III ADH is a quinohemoprotein able to oxidize alcohols
heme c
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type III ADH is a quinohemoprotein able to oxidize alcohols
heme c
type III ADH is a quinohemoprotein able to oxidize alcohols
heme c
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electrons extracted from ethanol at PQQ site are transferred to ubiquinone via heme c in subunit I and two of the three hemes c in subunit II
heme c
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subunit I contains pyrroloquinoline quinone and heme c, and subunit II contains three heme c components, determination of redox potentials at pH 4.5-7.0
pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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dependent on
pyrroloquinoline quinone
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dependent on
pyrroloquinoline quinone
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dependent on
pyrroloquinoline quinone
dependent on
pyrroloquinoline quinone
dependent on
pyrroloquinoline quinone
CCU55317
dependent on
pyrroloquinoline quinone
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dependent on, enzyme bound
pyrroloquinoline quinone
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dependent on, 1 molecule per enzyme molecule
pyrroloquinoline quinone
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PQQ, active in electron transfer, a tightly bound ubiquinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase. The enzyme possesses distinct quinone oxidation, reduction and high affinity binding sites, analysis, overview
pyrroloquinoline quinone
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PQQ, subunit I contains pyrroloquinoline quinone and heme c, and subunit II contains three heme c components
pyrroloquinoline quinone
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PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview
pyrroloquinoline quinone
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PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview
pyrroloquinoline quinone
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PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview
pyrroloquinoline quinone
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PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview
pyrroloquinoline quinone
PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview
pyrroloquinoline quinone
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electrons removed from substrate by alcohol dehydrogenase complex are initially transferred to the pyrroloquinoline quinone centre and further tunnelled across four cytochromes c
pyrroloquinoline quinone
PQQ, the PQQ ring is sandwiched between the indole ring of Trp245 and the two sulfur atoms of the disulfide ring structure
pyrroloquinoline quinone
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PQQ, two molecules per enzyme molecule
pyrroloquinoline quinone
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ADH is a typical quinohemoprotein with one pyrroloquinoline quinone
pyrroloquinoline quinone
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the ADH complex contains one mol of pyrroloquinoline quinone
pyrroloquinoline quinone
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one pyrroloquinoline quinone is associated with one molecule of the purified ADH complex
pyrroloquinoline quinone
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i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid
pyrroloquinoline quinone
pyrroloquinoline quinone-dependent dehydrogenase, pyrroloquinoline quinone is coordinated by Q87, I135, R137, S181, R350, L413, N417, W418, and W493. The side chains of W263 and the vicinal disulfide bond between C131 and C132 provide additional stacking interactions
additional information
an NAD(P)-independent enzyme
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additional information
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an NAD(P)-independent enzyme
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