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alcohol dehydrogenase
-
-
-
bacterial methanol dehydrogenase
-
-
-
calcium-containing quinoprotein methanol dehydrogenase
-
-
-
formaldehyde-oxidizing enzyme
glycerol dehydrogenase
-
-
-
lupanine hydroxylase (PQQ/heme c)
-
-
-
MDH
-
-
-
654696, 655785, 657304, 668252, 670785, 671068, 673047, 673048, 676902, 684756, 684949, 687432, 687993, 688333
membrane quinohaemoprotein alcohol dehydrogenase
-
-
-
membrane-bound alcohol dehydrogenase
-
-
-
methanol dehydrogenase
-
-
-
NAD+-independent, PQQ-containing alcohol dehydrogenase
-
-
-
polyethyleneglycol dehydrogenase
-
-
-
polypropylene glycol dehydrogenase
-
-
-
polypropyleneglycol dehydrogenase
-
-
-
polyvinylalcohol dehydrogenase
-
-
-
PQQ alcohol dehydrogenase
-
-
-
-
PQQ dependent alcohol dehydrogenase
PQQ methanol dehydrogenase
-
-
-
PQQ-alcohol dehydrogenase
PQQ-containing methanol dehydrogenase
-
-
-
PQQ-dependent alcohol dehydrogenase
PQQ-dependent alcohol oxidase
-
-
-
PQQ-dependent ethanol dehydrogenase
PQQ-dependent quinoprotein ethanol dehydrogenase
-
-
-
PQQ-linked alcohol dehydrogenase
-
-
-
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 quinonealcohol dehydrogenase
pyrroquinoline quinone-dependent alcohol dehydrogenase
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 alcohol dehydrogenase
quinoprotein dehydrogenase
-
-
-
quinoprotein ethanol dehydrogenase
-
-
-
quinoprotein methanol dehydrogenase
-
-
-
657167, 657304, 673048, 676902, 684947, 684948, 684949, 684950, 685051, 685052, 689139, 689815, 689818, 690095
tetrahydrofurfuryl alcohol dehydrogenase
-
-
-
type II ADH (PQQ/heme c)
-
-
-
type II quinohemoprotein alcohol dehydrogenase
-
-
-
type III ADH (PQQ/heme c /3 hemes c)
-
-
-
vanillyl alcohol dehydrogenase
-
-
-
additional information
-
the enzyme is a type III ADH
ADH
-
-
exaA
-
-
ExaA2
-
-
ExaA3
-
-
formaldehyde-oxidizing enzyme
-
-
formaldehyde-oxidizing enzyme
-
-
-
LEMA_P002680.1
-
PedH
-
-
-
PQQ dependent alcohol dehydrogenase
-
-
PQQ dependent alcohol dehydrogenase
-
-
-
PQQ-ADH
-
-
PQQ-alcohol dehydrogenase
-
-
-
PQQ-alcohol dehydrogenase
-
-
PQQ-dependent ADH
-
PQQ-dependent alcohol dehydrogenase
CCU55317
-
PQQ-dependent alcohol dehydrogenase
CCU55317
-
-
PQQ-dependent alcohol dehydrogenase
-
-
PQQ-dependent alcohol dehydrogenase
-
-
-
PQQ-dependent alcohol dehydrogenase
-
-
-
PQQ-dependent alcohol dehydrogenase
-
-
PQQ-dependent alcohol dehydrogenase
-
-
-
PQQ-dependent alcohol dehydrogenase
-
-
PQQ-dependent ethanol dehydrogenase
-
-
PQQ-dependent ethanol dehydrogenase
-
-
PQQalcohol dehydrogenase
-
PQQalcohol dehydrogenase
-
-
pyrrolo-quinoline quinone-dependent alcohol dehydrogenase
-
-
pyrrolo-quinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroloquinoline quinone dependent ADH
-
-
pyrroloquinoline quinone dependent ADH
-
-
-
pyrroloquinoline quinone dependent alcohol dehydrogenase
-
-
pyrroloquinoline quinone dependent alcohol dehydrogenase
-
-
-
pyrroloquinoline quinone dependent alcohol dehydrogenase
-
-
pyrroloquinoline quinone dependent alcohol dehydrogenase
-
-
-
pyrroloquinoline quinone-dependent alcohol dehydrogenase
-
-
inducible
pyrroloquinoline quinone-dependent alcohol dehydrogenase
CCU55317
-
pyrroloquinoline quinone-dependent alcohol dehydrogenase
CCU55317
-
-
pyrroloquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroloquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroloquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase
-
-
pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase
-
-
-
pyrroloquinoline quinonealcohol dehydrogenase
-
pyrroloquinoline quinonealcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
-
pyrroquinoline quinone-dependent alcohol dehydrogenase
-
-
QADH
-
QH-ADH
-
-
quinohemoprotein alcohol dehydrogenase
-
-
-
quinohemoprotein alcohol dehydrogenase
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
-
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
-
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
-
-
-
quinohemoprotein alcohol dehydrogenase
-
-
quinohemoprotein alcohol dehydrogenase
-
-
-
quinone-dependent alcohol dehydrogenase
-
quinone-dependent alcohol dehydrogenase
-
-
quinone-dependent alcohol dehydrogenase
-
-
quinoprotein alcohol dehydrogenase
-
-
quinoprotein alcohol dehydrogenase
-
-
-
quinoprotein alcohol dehydrogenase
-
-
-
quinoprotein alcohol dehydrogenase
-
-
-
quinoprotein alcohol dehydrogenase
-
-
-
quinoprotein alcohol dehydrogenase
-
-
quinoprotein alcohol dehydrogenase
-
-
-
quinoprotein alcohol dehydrogenase
-
-
quinoprotein alcohol dehydrogenase
-
-
-
YogA
-
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1,2-propanediol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
9.1% activity compared to 1-propanol
-
-
r
1,3-butandiol + ubiquinone
? + ubiquinol
-
very low activity, 0.94% of the activity with ethanol
-
-
?
1,3-propandiol + ubiquinone
? + ubiquinol
-
15% of the activity with ethanol
-
-
?
1,3-propanediol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
12.2% activity compared to 1-propanol
-
-
r
1,4-butanediol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
16.2% activity compared to 1-propanol
-
-
r
1-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
1-butanol + ubiquinone
butanal + ubiquinol
-
88% of the activity with ethanol
-
-
?
1-heptanol + 2,6-dichlorophenolindophenol
heptanal + reduced 2,6-dichlorophenolindophenol
1-hexanol + 2,6-dichlorophenolindophenol
hexanal + reduced 2,6-dichlorophenolindophenol
1-hexanol + ubiquinone
hexanal + ubiquinol
-
93% of the activity with ethanol
-
-
?
1-octanol + ubiquinone
octanal + ubiquinol
-
66% of the activity with ethanol
-
-
?
1-pentanol + 2,6-dichlorophenolindophenol
pentanaldehyde + reduced 2,6-dichlorophenolindophenol
-
85.5% activity compared to 1-propanol
-
-
r
1-pentanol + ubiquinone
pentanal + ubiquinol
-
97% of the activity with ethanol
-
-
?
1-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
1-propanol + phenazine methosulfate
propionaldehyde + reduced phenazine methosulfate
-
100% activity
-
-
r
1-propanol + ubiquinone
propanal + ubiquinol
-
90% of the activity with ethanol
-
-
?
2,3-butanediol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
4.1% activity compared to 1-propanol
-
-
r
2-(S)-butanol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
43.3% activity compared to 1-propanol
-
-
r
2-butanol + ubiquinone
2-butanone + ubiquinol
-
64% of the activity with ethanol
-
-
?
2-propanol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
31.9% activity compared to 1-propanol
-
-
r
2-propanol + ubiquinone
acetone + ubiquinol
-
51% of the activity with ethanol
-
-
?
3-methyl-1-butanol + ubiquinone
3-methyl-1-butanal + ubiquinol
-
48% of the activity with ethanol
-
-
?
5-(hydroxymethyl)furfural + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
?
5-(hydroxymethyl)furoic acid + phenazine methosulfate
? + reduced phenazine methosulfate
wild-type enzyme shows no activity, mutant enzymes F412V/W561A, F412I/W561Q and F412I/W561S are active
-
-
?
5-formylfurfural + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
?
acetaldehyde + 2,6-dichlorophenolindophenol
?
-
42% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
acetaldehyde + ferricyanide
?
-
13% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
acetaldehyde + reduced 2,6-dichlorophenolindophenol
ethanol + 2,6-dichlorophenolindophenol
-
-
-
-
r
acetaldehyde + reduced phenazine methosulfate
ethanol + phenazine methosulfate
-
55.6% activity compared to 1-propanol
-
-
r
acetaldehyde + ubiquinol
ethanol + ubiquinone
allyl alcohol + ferricyanide
acrolein + ferricyanide
-
the best substrate
-
-
?
allylic alcohol + 2,6-dichlorophenolindophenol
?
-
91% activity compared to n-butanol
-
-
?
allylic alcohol + ferricyanide
?
-
96% activity compared to n-butanol
-
-
?
benzyl alcohol + 2,6-dichlorophenolindophenol
benzaldehyde + reduced 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
1-butanol + 2,6-dichlorophenolindophenol
-
32.1% activity compared to 1-propanol
-
-
r
citral + ubiquinol
? + ubiquinone
-
39% of the activity with ethanol
-
-
?
citronellal + ubiquinol
citronellol + ubiquinone
-
45% of the activity with ethanol
-
-
?
citronellol + ubiquinone
citronellal + ubiquinol
-
74% of the activity with ethanol
-
-
?
cyclohexanol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
5.5% activity compared to 1-propanol
-
-
r
D-galactose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
85% activity compared to D-glucose
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
D-mannose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
77% activity compared to D-glucose
-
-
?
D-sorbitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
9.0% activity compared to D-glucose
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
130% activity compared to D-glucose
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
ethanol + acceptor
acetaldehyde + reduced acceptor
ethanol + ferricyanide
acetaldehyde + ferrocyanide
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
ethanol + pyrroloquinoline quinone
acetaldehyde + pyrroloquinoline quinol
ethanol + ubiquinone
acetaldehyde + ubiquinol
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
ethyleneglycol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
109% activity compared to D-glucose
-
-
?
formaldehyde + 2,6-dichlorophenolindophenol
?
-
38% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
formaldehyde + ferricyanide
?
-
34% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
geraniol + ubiquinone
geranial + ubiquinol
-
37% of the activity with ethanol
-
-
?
glutaraldehyde + 2,6-dichlorophenolindophenol
?
-
18% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
glutaraldehyde + ferricyanide
?
iso-propanol + ferricyanide
propan-2-one + ferrocyanide
-
about 10% of the activity with n-butanol
-
-
?
isopropanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
121% activity compared to D-glucose
-
-
?
isopropanol + ferricyanide
propan-2-one + ferrocyanide
-
18% of the activity with allyl alcohol
-
-
?
L-sorbose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
0.6% activity compared to D-glucose
-
-
?
maltotetraose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
24% activity compared to D-glucose
-
-
?
maltotriose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
31% activity compared to D-glucose
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
methanol + ferricyanide
formaldehyde + ferrocyanide
-
9% of the activity with allyl alcohol
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
6.3% activity compared to 1-propanol
-
-
r
methyl-alpha-D-glucopyranoside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
5% activity compared to D-glucose
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
n-butanol + 2,6-dichlorophenolindophenol
n-butanal + reduced 2,6-dichlorophenolindophenol
-
100% activity
-
-
?
n-butanol + ferricyanide
butyraldehyde + ferrocyanide
-
98% of the activity with allyl alcohol
-
-
?
n-butanol + ferricyanide
n-butanal + ferrocyanide
-
-
-
-
?
n-pentanol + ferricyanide
n-pentanal + ferrocyanide
-
about 45% of the activity with n-butanol
-
-
?
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
n-propanol + ferricyanide
n-propanal + ferrocyanide
n-propanol + ferricyanide
propionaldehyde + ferrocyanide
-
90% of the activity with allyl alcohol
-
-
?
n-propanol + oxidized 2,6-dichlorophenolindophenol
n-propanal + reduced 2,6-dichlorophenolindophenol
-
96% activity compared to n-butanol
-
-
?
propan-1,2,3-triol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
25% activity compared to D-glucose
-
-
?
propionaldehyde + 2,6-dichlorophenolindophenol
?
-
33% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
propionaldehyde + ferricyanide
?
-
24% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
propionaldehyde + reduced 2,6-dichlorophenolindophenol
1-propanol + 2,6-dichlorophenolindophenol
-
-
-
-
r
propionaldehyde + reduced phenazine methosulfate
1-propanol + phenazine methosulfate
-
54.5% activity compared to 1-propanol
-
-
r
rac-1,2-propanediol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
128% activity compared to D-glucose
-
-
?
rac-2-methyl-2,4-pentanediol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
164% activity compared to D-glucose
-
-
?
xylitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
20% activity compared to D-glucose
-
-
?
additional information
?
-
1-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
82% activity compared to 1-propanol
-
-
r
1-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
82% activity compared to 1-propanol
-
-
r
1-heptanol + 2,6-dichlorophenolindophenol
heptanal + reduced 2,6-dichlorophenolindophenol
-
44.1% activity compared to 1-propanol
-
-
r
1-heptanol + 2,6-dichlorophenolindophenol
heptanal + reduced 2,6-dichlorophenolindophenol
-
44.1% activity compared to 1-propanol
-
-
r
1-hexanol + 2,6-dichlorophenolindophenol
hexanal + reduced 2,6-dichlorophenolindophenol
-
62.2% activity compared to 1-propanol
-
-
r
1-hexanol + 2,6-dichlorophenolindophenol
hexanal + reduced 2,6-dichlorophenolindophenol
-
62.2% activity compared to 1-propanol
-
-
r
1-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
1-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
1-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
acetaldehyde + ubiquinol
ethanol + ubiquinone
-
-
-
-
r
acetaldehyde + ubiquinol
ethanol + ubiquinone
-
-
-
-
r
acetaldehyde + ubiquinol
ethanol + ubiquinone
-
-
-
-
r
benzyl alcohol + 2,6-dichlorophenolindophenol
benzaldehyde + reduced 2,6-dichlorophenolindophenol
-
3.9% activity compared to 1-propanol
-
-
r
benzyl alcohol + 2,6-dichlorophenolindophenol
benzaldehyde + reduced 2,6-dichlorophenolindophenol
-
3.9% activity compared to 1-propanol
-
-
r
D-glucose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
100% activity
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
100% activity
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
with phenazine methosulfonate
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
with phenazine methosulfonate
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
with phenazine methosulfonate
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
with phenazine methosulfonate
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
88% activity compared to n-butanol
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
88% activity compared to n-butanol
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
16% activity compared to D-glucose
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
16% activity compared to D-glucose
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
ethanol + acceptor
acetaldehyde + reduced acceptor
-
direct electron-transfer processes between the polypyrrole entrapped quinohemoprotein alcohol dehydrogenase and a platinum electrode take place via the conducting-polymer network, mechanism modelling, overview
-
-
?
ethanol + acceptor
acetaldehyde + reduced acceptor
-
direct electron-transfer processes between the polypyrrole entrapped quinohemoprotein alcohol dehydrogenase and a platinum electrode take place via the conducting-polymer network, mechanism modelling, overview
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
-
about 40% of the activity with n-butanol
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
-
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
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
-
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
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
-
-
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
-
95% of the activity with allyl alcohol
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
-
-
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
-
91% activity compared to n-butanol
-
-
?
ethanol + ferricyanide
acetaldehyde + ferrocyanide
-
91% activity compared to n-butanol
-
-
?
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
-
-
?
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
88.9% activity compared to 1-propanol
-
-
r
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
-
-
-
-
?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
-
-
-
-
?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
-
-
-
-
?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
-
-
-
-
?
ethanol + pyrroloquinoline quinone
acetaldehyde + pyrroloquinoline quinol
-
-
-
-
r
ethanol + pyrroloquinoline quinone
acetaldehyde + pyrroloquinoline quinol
-
-
-
-
r
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
CCU55317
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
CCU55317
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
electron transfer mechanism, intramolecular transfer of electrons from pyrroloquinoline quinone to ubiquinone and the quinone binding sites, overview
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
electron transfer mechanism, intramolecular transfer of electrons from pyrroloquinoline quinone to ubiquinone and the quinone binding sites, overview
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
r
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
r
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
r
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
best substrate
-
-
?
ethanol + ubiquinone
acetaldehyde + ubiquinol
-
-
-
-
?
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
-
-
-
-
?
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
-
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
-
-
?
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
-
-
-
-
?
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
-
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
-
-
?
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
-
the ADH complex shows a high affinity for ubiquinone-1 with ethanol as cosubstrate
-
-
?
glutaraldehyde + ferricyanide
?
-
8% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
glutaraldehyde + ferricyanide
?
-
8% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
3.0% activity compared to D-glucose
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
3.0% activity compared to D-glucose
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
241% activity compared to D-glucose
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
241% activity compared to D-glucose
-
-
?
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
120% activity compared to D-glucose
-
-
?
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
120% activity compared to D-glucose
-
-
?
n-propanol + ferricyanide
n-propanal + ferrocyanide
-
about 95% of the activity with n-butanol
-
-
?
n-propanol + ferricyanide
n-propanal + ferrocyanide
-
98% activity compared to n-butanol
-
-
?
additional information
?
-
the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview
-
-
?
additional information
?
-
in ADH, electrons pass from PQQH2 to a heme c on the same quinohemoprotein subunit, and then to ubiquinone in the membrane by way of a separate cytochrome c subunit in the three-component membrane complex, ovreview
-
-
?
additional information
?
-
-
in ADH, electrons pass from PQQH2 to a heme c on the same quinohemoprotein subunit, and then to ubiquinone in the membrane by way of a separate cytochrome c subunit in the three-component membrane complex, ovreview
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
the enzyme activity is correlated with resistance to acetic acid, due to lower enzyme activity in the organism, the growth of Acetobacter pasteurianus on high acetic acid concentrations is limited, overview
-
-
?
additional information
?
-
-
the enzyme activity is correlated with resistance to acetic acid, due to lower enzyme activity in the organism, the growth of Acetobacter pasteurianus on high acetic acid concentrations is limited, overview
-
-
?
additional information
?
-
-
the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview
-
-
?
additional information
?
-
-
by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
?
additional information
?
-
-
the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview
-
-
?
additional information
?
-
-
by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
?
additional information
?
-
-
the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
PQQ-ADH has a Q-1 reductase activity at acidic pH 4.0-5.0
-
-
?
additional information
?
-
CCU55317
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
CCU55317
substrate specificity, overview
-
-
?
additional information
?
-
-
no activity with glucose, benzaldehyde, formaldehyde, acetone, sorbitol or glycerol
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH. The organism shows enantiospecific oxidation of alcoholic compounds, e.g. oxidation of prochiral compound 2-methylpropane-1,3-diol to (R)-beta-hydroxyisobutyric acid with 83% enantiomeric excess
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH. The organism shows enantiospecific oxidation of alcoholic compounds, e.g. oxidation of prochiral compound 2-methylpropane-1,3-diol to (R)-beta-hydroxyisobutyric acid with 83% enantiomeric excess
-
-
?
additional information
?
-
-
the enzyme is involved in the cellular adaptation mechanism to high acetic acid concentrations, overview
-
-
?
additional information
?
-
high alcohol dehydrogenase activity in the Gluconacetobacter europaeus cells and high acetic acid stability of the purified enzyme represent two of the unique features that enable this species to grow and stay metabolically active at extremely high concentrations of acetic acid
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
the enzyme is involved in the cellular adaptation mechanism to high acetic acid concentrations, overview
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
the enzyme activity is correlated with resistance to acetic acid, due to lower enzyme activity in the organism, the growth of Gluconacetobacter intermedius on high acetic acid concentrations is limited, overview
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
the enzyme activity is correlated with resistance to acetic acid, due to lower enzyme activity in the organism, the growth of Gluconacetobacter intermedius on high acetic acid concentrations is limited, overview
-
-
?
additional information
?
-
-
purified ADH oxidizes primary alcohols (C2-C6) but not methanol
-
-
?
additional information
?
-
-
broad substrate specificity of PQQ-ADH
-
-
?
additional information
?
-
-
purified ADH oxidizes primary alcohols (C2-C6) but not methanol
-
-
?
additional information
?
-
-
substrate specificity, assayed with dichlorophenolindophenol and phenazinemethosulfate as electron acceptors, overview
-
-
?
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evolution
CCU55317
high similarity between genes encoding subunits I and II of PQQ-ADH
evolution
-
high similarity between genes encoding subunits I and II of PQQ-ADH
-
malfunction
-
exaA2 and exaA3 mutants are less competitive than the wild type during colonization of rice roots
malfunction
-
inactivation of PA1982 by insertion mutagenesis results in inability of the mutant to utilise ethanol and in reduced growth on geraniol. Growth on ethanol is restored by transferring an intact copy of the PA1982 gene into the mutant
malfunction
-
mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
malfunction
-
mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
-
malfunction
-
mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
-
malfunction
-
exaA2 and exaA3 mutants are less competitive than the wild type during colonization of rice roots
-
malfunction
-
mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
-
malfunction
-
mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
-
malfunction
-
mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing Q in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing Q in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
-
ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
-
physiological function
-
ethanol is an important carbon source for the endophytic life of Azoarcus sp. in Oryza sativa roots
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
physiological function
-
the PQQ-dependent alcohol dehydrogenase of Pseudomonas aeruginosa functions in ethanol metabolism and is involved in catabolism of acyclic terpenes, overview
physiological function
reduced expression of the transcriptional regulator C6TF leads to reduced expression of genes for polyketide synthase PKS2, P450, a cytochrome P450 monoxygenase, YogA, an alcohol dehydrogenase/quinone reductase, RTA1, a lipid transport exporter superfamily member and MFS, a Major Facilitator Superfamily transporter, as well as a marked reduction in phomenoic acid production
physiological function
-
the enzyme plays an important role in the catabolism of alcohols in bacteria. Inactivation of exaA affects the growth of Azospirillum brasilense on glycerol
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
-
physiological function
-
ethanol is an important carbon source for the endophytic life of Azoarcus sp. in Oryza sativa roots
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
-
physiological function
-
the enzyme plays an important role in the catabolism of alcohols in bacteria. Inactivation of exaA affects the growth of Azospirillum brasilense on glycerol
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
-
physiological function
-
reduced expression of the transcriptional regulator C6TF leads to reduced expression of genes for polyketide synthase PKS2, P450, a cytochrome P450 monoxygenase, YogA, an alcohol dehydrogenase/quinone reductase, RTA1, a lipid transport exporter superfamily member and MFS, a Major Facilitator Superfamily transporter, as well as a marked reduction in phomenoic acid production
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
-
physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
-
additional information
-
Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity
additional information
-
Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
115000
-
non-denaturing PAGE
14000
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE
18000
-
x * 78000 + x * 55000 + x * 18000, SDS-PAGE
20000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE
41000
-
1 * 68000 + 1 * 41000, SDS-PAGE
43500
-
1 * 71400 + 1 * 43500, SDS-PAGE
49000
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE
54000
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE
68000
-
1 * 68000 + 1 * 41000, SDS-PAGE
71400
-
1 * 71400 + 1 * 43500, SDS-PAGE
76000
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
78000
-
x * 78000 + x * 55000 + x * 18000, SDS-PAGE
8000
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE
85000
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE
15000
-
-
15000
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE
16000
1 * 74000 + 1 * 44000 + 1 * 16000, SDS-PAGE
16000
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
16000
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
44000
1 * 74000 + 1 * 44000 + 1 * 16000, SDS-PAGE
44000
-
1 * 71000 + 1 * 44000, SDS-PAGE
44000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
44000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
44000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
44000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE
44000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
44000
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
45000
1 * 72000 + 1 * 45000, SDS-PAGE
45000
1 * 72000 + 1 * 45000, SDS-PAGE
45000
CCU55317
1 * 72000 + 1 * 45000, SDS-PAGE
45000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
45000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
50000
-
-
50000
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE
55000
-
x * 78000 + x * 55000 + x * 18000, SDS-PAGE
55000
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
71000
-
1 * 71000 + 1 * 44000, SDS-PAGE
71000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
71000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
71000
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
72000
1 * 72000 + 1 * 45000, SDS-PAGE
72000
1 * 72000 + 1 * 45000, SDS-PAGE
72000
CCU55317
1 * 72000 + 1 * 45000, SDS-PAGE
72000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE
72000
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
72000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
72000
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
72000
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE
74000
1 * 74000 + 1 * 44000 + 1 * 16000, SDS-PAGE
74000
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
80000
-
-
80000
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homodimer
-
two alpha-subunits
?
-
x * 78000 + x * 55000 + x * 18000, SDS-PAGE
?
-
x * 78000 + x * 55000 + x * 18000, SDS-PAGE
-
dimer
-
1 * 71400 + 1 * 43500, SDS-PAGE
dimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
dimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
-
dimer
1 * 72000 + 1 * 45000, SDS-PAGE
dimer
1 * 72000 + 1 * 45000, SDS-PAGE
dimer
-
1 * 72000 + 1 * 45000, SDS-PAGE
-
dimer
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
heterodimer
CCU55317
1 * 72000 + 1 * 45000, SDS-PAGE
heterodimer
-
1 * 72000 + 1 * 45000, SDS-PAGE
-
heterodimer
-
1 * 71000 + 1 * 44000, SDS-PAGE
heterodimer
-
1 * 71000 + 1 * 44000, SDS-PAGE
-
heterodimer
-
1 * 68000 + 1 * 41000, SDS-PAGE
heterodimer
-
1 * 68000 + 1 * 41000, SDS-PAGE
-
heterotrimer
-
1 * 80000 + 1 * 50000 + 1 * 15000, SDS-PAGE
heterotrimer
-
1 * 80000 + 1 * 50000 + 1 * 15000, SDS-PAGE
-
heterotrimer
-
1 * 80000 + 1 * 50000 + 1 * 15000, SDS-PAGE
-
trimer
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE
trimer
-
1 * 72000, subunit I, + 1 * 50000, subunit II, + 1 * 15000, subunit III, SDS-PAGE
-
trimer
1 * 74000 + 1 * 44000 + 1 * 16000, SDS-PAGE
trimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE
trimer
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
trimer
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
trimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE
-
trimer
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE
-
trimer
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE
-
trimer
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE
-
trimer
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
-
1 * 72000, subunit I, + 1 * 44000, subunit II, + 1 * 20000, subunit III, SDS-PAGE
-
trimer
-
1 * 74000, subunit I, + 1 * 44000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
-
1 * 76000, subunit I, + 1 * 55000, subunit II, + 1 * 16000, subunit III, SDS-PAGE
-
trimer
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE
trimer
-
1 * 80000, subunit I, + 1 * 54000, subunit II, + 1 * 8000, subunit III, SDS-PAGE
-
trimer
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
trimer
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
-
trimer
-
heterotrimer with unequal numers of heme groups, overview
trimer
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
trimer
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE
trimer
-
1 * 71000, subunit I, + 1 * 44000, subunit II, SDS-PAGE
-
trimer
-
1 * 85000, subunit I, + 1 * 49000, subunit II, + 1 * 14000, subunit III, SDS-PAGE
-
trimer
-
subunit I contains one PQQ and one heme moiety, subunit II contains three heme moieties, and subunit III is a small protein subunit essential for the enzymatic activity providing electron exchange between PQQ and hemes, overview
trimer
-
subunit I contains one PQQ and one heme moiety, subunit II contains three heme moieties, and subunit III is a small protein subunit essential for the enzymatic activity providing electron exchange between PQQ and hemes, overview
-
trimer
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
trimer
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
-
trimer
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
trimer
-
1 * 72000, subunit I, + 1 * 45000, subunit II, SDS-PAGE
-
additional information
structure-function relationship, overview
additional information
-
structure-function relationship, overview
additional information
-
structure-function relationship, overview
-
additional information
-
structure-function relationship, overview
additional information
-
structure-function relationship, overview
additional information
-
structure-function relationship, overview
additional information
-
the enzyme shows a propeller structure, QEDH contains a disulfide structure that is similar to the analogous structure in QMDH, EC 1.1.2.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Chen, Z.; Baruch, P.; Mathews, F.S.; Matsushita, K.; Yamashita, T.; Toyama, H.; Adachi, O.
Crystallization and preliminary diffraction studies of two quinoprotein alcohol dehydrogenases (ADHs): a soluble monomeric ADH from Pseudomonas putida HK5 (ADH-IIB) and a heterotrimeric membrane-bound ADH from Gluconobacter suboxydans (ADH-GS).
Acta Crystallogr. Sect. D
55
1933-1936
1999
Gluconobacter oxydans
brenda
Ramanavicius, A.; Habermuller, K.; Csoeregi, E.; Laurinavicius, V.; Schuhmann, W.
Polypyrrole-entrapped quinohemoprotein alcohol dehydrogenase. Evidence for direct electron transfer via conducting-polymer chains
Anal. Chem.
71
3581-3586
1999
Gluconobacter sp., Gluconobacter sp. DSM 3504 / ATCC 15163
brenda
Trcek, J.; Toyama, H.; Czuba, J.; Misiewicz, A.; Matsushita, K.
Correlation between acetic acid resistance and characteristics of PQQ-dependent ADH in acetic acid bacteria
Appl. Microbiol. Biotechnol.
70
366-373
2006
Komagataeibacter intermedius (Q335V9), Acetobacter pasteurianus (Q335W4), Acetobacter pasteurianus, Komagataeibacter europaeus (Q44002), Komagataeibacter intermedius JK3 (Q335V9)
brenda
Toyama, H.; Mathews, F.S.; Adachi, O.; Matsushita, K.
Quinohemoprotein alcohol dehydrogenases: structure, function, and physiology
Arch. Biochem. Biophys.
428
10-21
2004
Gluconobacter oxydans, Acidomonas methanolica, Acetobacter pasteurianus, Gluconacetobacter polyoxogenes, Acetobacter aceti (P18278), Acetobacter pasteurianus SKU1108
brenda
Frebortova, J.; Matsushita, K.; Arata, H.; Adachi, O.
Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus: a redox-titration study
Biochim. Biophys. Acta
1363
24-34
1998
Acidomonas methanolica, Acidomonas methanolica JCM 6891
brenda
Shinagawa, E.; Toyama, H.; Matsushita, K.; Tuitemwong, P.; Theeragool, G.; Adachi, O.
A novel type of formaldehyde-oxidizing enzyme from the membrane of Acetobacter sp. SKU 14
Biosci. Biotechnol. Biochem.
70
850-857
2006
Acetobacter sp., Acetobacter sp. SKU 14
brenda
Matsushita, K.; Kobayashi, Y.; Mizuguchi, M.; Toyama, H.; Adachi, O.; Sakamoto, K.; Miyoshi, H.
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
2723-2731
2008
Gluconobacter oxydans, Gluconobacter oxydans IFO 12528
brenda
Laurinavicius, V.; Razumiene, J.; Ramanavicius, A.; Ryabov, A.D.
Wiring of PQQ-dehydrogenases
Biosens. Bioelectron.
20
1217-1222
2004
Gluconobacter sp., Gluconobacter sp. DSM 3504 / ATCC 15163
brenda
Razumiene, J.; Meskys, R.; Gureviciene, V.; Laurinavicius, V.; Reshetova, M.D.; Ryabov, A.D.
4-Ferrocenylphenol as an electron transfer mediator in PQQ-dependent alcohol and glucose dehydrogenase-catalyzed reactions
Electrochem. Commun.
2
307-311
2000
Gluconobacter sp., Gluconobacter sp. DSM 3504 / ATCC 15163
-
brenda
Trcek, J.; Jernejc, K.; Matsushita, K.
The highly tolerant acetic acid bacterium Gluconacetobacter europaeus adapts to the presence of acetic acid by changes in lipid composition, morphological properties and PQQ-dependent ADH expression
Extremophiles
11
627-635
2007
Komagataeibacter europaeus, Komagataeibacter europaeus V3 / LMG 18494
brenda
Gomez-Manzo, S.; Contreras-Zentella, M.; Gonzalez-Valdez, A.; Sosa-Torres, M.; Arreguin-Espinoza, R.; Escamilla-Marvan, E.
The PQQ-alcohol dehydrogenase of Gluconacetobacter diazotrophicus
Int. J. Food Microbiol.
125
71-78
2008
Gluconacetobacter diazotrophicus
brenda
Cozier, G.E.; Giles, I.G.; Anthony, C.
The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens
Biochem. J.
308
375-379
1995
Acetobacter aceti (P18278), Acetobacter aceti
brenda
Quintero, Y.; Poblet, M.; Guillamon, J.M.; Mas, A.
Quantification of the expression of reference and alcohol dehydrogenase genes of some acetic acid bacteria in different growth conditions
J. Appl. Microbiol.
106
666-674
2009
Acetobacter pasteurianus, Acetobacter aceti (P18278)
brenda
Chavez-Pacheco, J.L.; Contreras-Zentella, M.; Membrillo-Hernandez, J.; Arreguin-Espinoza, R.; Mendoza-Hernandez, G.; Gomez-Manzo, S.; Escamilla, J.E.
The quinohaemoprotein alcohol dehydrogenase from Gluconacetobacter xylinus: molecular and catalytic properties
Arch. Microbiol.
192
703-713
2010
Komagataeibacter xylinus, Komagataeibacter xylinus IFO 13693
brenda
Gomez-Manzo, S.; Solano-Peralta, A.; Saucedo-Vazquez, J.P.; Escamilla-Marvan, J.E.; Kroneck, P.M.; Sosa-Torres, M.E.
The membrane-bound quinohemoprotein alcohol dehydrogenase from Gluconacetobacter diazotrophicus PAL5 carries a [2Fe-2S] cluster
Biochemistry
49
2409-2415
2010
Gluconacetobacter diazotrophicus, Gluconacetobacter diazotrophicus PAL5 (ATCC 49037)
brenda
Kanchanarach, W.; Theeragool, G.; Yakushi, T.; Toyama, H.; Adachi, O.; Matsushita, K.
Characterization of thermotolerant Acetobacter pasteurianus strains and their quinoprotein alcohol dehydrogenases
Appl. Microbiol. Biotechnol.
85
741-751
2010
Acetobacter pasteurianus, Acetobacter pasteurianus MSU10, Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus SKU1108, Acetobacter pasteurianus IFO3284
brenda
Yakushi, T.; Matsushita, K.
Alcohol dehydrogenase of acetic acid bacteria: structure, mode of action, and applications in biotechnology
Appl. Microbiol. Biotechnol.
86
1257-1265
2010
Gluconobacter oxydans, Komagataeibacter europaeus, Acidomonas methanolica, Acetobacter pasteurianus, Komagataeibacter xylinus, Gluconacetobacter diazotrophicus, Gluconacetobacter polyoxogenes, Komagataeibacter intermedius, Acetobacter lovaniensis, Acetobacter pasteurianus MSU10, Komagataeibacter intermedius JK3, Gluconacetobacter diazotrophicus PAL5, Acetobacter pasteurianus NCI1452, Komagataeibacter europaeus V3 / LMG 18494, Acidomonas methanolica JCM 6891, Gluconobacter oxydans IFO12528, Acetobacter pasteurianus KKP584, Acetobacter pasteurianus IFO3191, Acetobacter pasteurianus SKU1108, Acetobacter lovaniensis IFO3284, Gluconacetobacter polyoxogenes NBI1028
brenda
Treek, J.; Matsushita, K.
A unique enzyme of acetic acid bacteria, PQQ-dependent alcohol dehydrogenase, is also present in Frateuria aurantia
Appl. Microbiol. Biotechnol.
97
7369-7376
2013
Frateuria aurantia (CCU55317), Frateuria aurantia, Frateuria aurantia LMG 1558 (CCU55317)
brenda
Gvozdev, A.; Tukhvatullin, I.; Gvozdev, R.
Quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases
Biochemistry
77
843-856
2012
Pseudomonas sp.
brenda
Aquino Neto, S.; Suda, E.; Xu, S.; Meredith, M.; De Andrade, A.; Minteer, S.
Direct electron transfer-based bioanodes for ethanol biofuel cells using PQQ-dependent alcohol and aldehyde dehydrogenases
Electrochim. Acta
87
323-329
2013
Gluconobacter sp., Gluconobacter sp. 33, Gluconobacter sp. DSM 3504 / ATCC 15163
-
brenda
Masud, U.; Matsushita, K.; Theeragool, G.
Cloning and functional analysis of adhS gene encoding quinoprotein alcohol dehydrogenase subunit III from Acetobacter pasteurianus SKU1108
Int. J. Food Microbiol.
138
39-49
2010
Acetobacter pasteurianus, Acetobacter pasteurianus SKU1108
brenda
Chattopadhyay, A.; Foerster-Fromme, K.; Jendrossek, D.
PQQ-dependent alcohol dehydrogenase (QEDH) of Pseudomonas aeruginosa is involved in catabolism of acyclic terpenes
J. Basic Microbiol.
50
119-124
2010
Pseudomonas aeruginosa
brenda
Krause, A.; Bischoff, B.; Miche, L.; Battistoni, F.; Reinhold-Hurek, B.
Exploring the function of alcohol dehydrogenases during the endophytic life of Azoarcus sp. strain BH72
Mol. Plant Microbe Interact.
24
1325-1332
2011
Azoarcus sp., Azoarcus sp. BH72
brenda
Aquino Neto, S.; Hickey, D.P.; Milton, R.D.; De Andrade, A.R.; Minteer, S.D.
High current density PQQ-dependent alcohol and aldehyde dehydrogenase bioanodes
Biosens. Bioelectron.
72
247-254
2015
Gluconobacter sp., Gluconobacter sp. DSM 3504
brenda
Elliott, C.E.; Callahan, D.L.; Schwenk, D.; Nett, M.; Hoffmeister, D.; Howlett, B.J.
A gene cluster responsible for biosynthesis of phomenoic acid in the plant pathogenic fungus, Leptosphaeria maculans
Fungal Genet. Biol.
53
50-58
2013
Leptosphaeria maculans (E5AE42), Leptosphaeria maculans JN3 (E5AE42)
brenda
Takeda, K.; Matsumura, H.; Ishida, T.; Samejima, M.; Igarashi, K.; Nakamura, N.; Ohno, H.
The two-step electrochemical oxidation of alcohols using a novel recombinant PQQ alcohol dehydrogenase as a catalyst for a bioanode
Bioelectrochemistry
94
75-78
2013
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Takeda, K.; Ishida, T.; Igarashi, K.; Samejima, M.; Nakamura, N.; Ohno, H.
Effect of amines as activators on the alcohol-oxidizing activity of pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase
Biosci. Biotechnol. Biochem.
78
1195-1198
2014
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Rozeboom, H.J.; Yu, S.; Mikkelsen, R.; Nikolaev, I.; Mulder, H.J.; Dijkstra, B.W.
Crystal structure of quinone-dependent alcohol dehydrogenase from Pseudogluconobacter saccharoketogenes. A versatile dehydrogenase oxidizing alcohols and carbohydrates
Protein Sci.
24
2044-2054
2015
Pseudogluconobacter saccharoketogenes (Q93RE9), Pseudogluconobacter saccharoketogenes, Pseudogluconobacter saccharoketogenes IFO 14464 (Q93RE9), Pseudogluconobacter saccharoketogenes IFO 14464
brenda
Wehrmann, M.; Elsayed, E.; Kbbing, S.; Bendz, L.; Lepak, A.; Schwabe, J.; Wierckx, N.; Bange, G.; Klebensberger, J.
Engineered PQQ-dependent alcohol dehydrogenase for the oxidation of 5-(hydroxymethyl)furoic acid
ACS Catal.
10
7836-7842
2020
Pseudomonas putida (Q88JH0)
-
brenda
Singh, V.S.; Dubey, A.P.; Gupta, A.; Singh, S.; Singh, B.N.; Tripathi, A.K.
Regulation of a glycerol-induced quinoprotein alcohol dehydrogenase by ?54 and a LuxR-type regulator in Azospirillum brasilense Sp7
J. Bacteriol.
199
e00035-17
2017
Azospirillum brasilense, Azospirillum brasilense Sp7
brenda