Information on EC 1.1.5.5 - alcohol dehydrogenase (quinone)

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The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY hide
1.1.5.5
-
RECOMMENDED NAME
GeneOntology No.
alcohol dehydrogenase (quinone)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ethanol + ubiquinone = acetaldehyde + ubiquinol
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
long chain fatty acid ester synthesis (engineered)
-
-
SYSTEMATIC NAME
IUBMB Comments
alcohol:quinone oxidoreductase
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes adhA, adhB, and adhS encoding the three subunits
-
-
Manually annotated by BRENDA team
genes adhA, adhB, and adhS encoding the three subunits
-
-
Manually annotated by BRENDA team
subsp lovaniensis
-
-
Manually annotated by BRENDA team
genes adhA, adhB, and adhS encoding the three subunis
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-
Manually annotated by BRENDA team
genes adhA, adhB, and adhS encoding the three subunits
-
-
Manually annotated by BRENDA team
strain SKU 14, isolated in Thailand
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-
Manually annotated by BRENDA team
strain SKU 14, isolated in Thailand
-
-
Manually annotated by BRENDA team
strain JCM 6891
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-
Manually annotated by BRENDA team
genes adhA, adhB, and adhS, encoding the three subunits
-
-
Manually annotated by BRENDA team
genes exaA2 and exaA3
-
-
Manually annotated by BRENDA team
genes exaA2 and exaA3
-
-
Manually annotated by BRENDA team
genes adhA and adhB encoding subunits I and II
CCU55317
GenBank
Manually annotated by BRENDA team
genes adhA and adhB encoding subunits I and II
CCU55317
GenBank
Manually annotated by BRENDA team
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
genes adhA and adhB, encoding the two subunits
-
-
Manually annotated by BRENDA team
strain IFO 12528, constitutive enzyme
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Manually annotated by BRENDA team
genes adhA, adhB, and adhS, encoding the three subunits
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-
Manually annotated by BRENDA team
Gluconobacter sp.
strain 33
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-
Manually annotated by BRENDA team
Gluconobacter sp. 33
strain 33
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene PA1982 or exaA
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-butandiol + ubiquinone
? + ubiquinol
show the reaction diagram
-
very low activity, 0.94% of the activity with ethanol
-
-
?
1,3-propandiol + ubiquinone
? + ubiquinol
show the reaction diagram
-
15% of the activity with ethanol
-
-
?
1-butanol + ubiquinone
butanal + ubiquinol
show the reaction diagram
-
88% of the activity with ethanol
-
-
?
1-hexanol + ubiquinone
hexanal + ubiquinol
show the reaction diagram
-
93% of the activity with ethanol
-
-
?
1-octanol + ubiquinone
octanal + ubiquinol
show the reaction diagram
-
66% of the activity with ethanol
-
-
?
1-pentanol + ubiquinone
pentanal + ubiquinol
show the reaction diagram
-
97% of the activity with ethanol
-
-
?
1-propanol + ubiquinone
propanal + ubiquinol
show the reaction diagram
-
90% of the activity with ethanol
-
-
?
2-butanol + ubiquinone
2-butanone + ubiquinol
show the reaction diagram
-
64% of the activity with ethanol
-
-
?
2-propanol + ubiquinone
acetone + ubiquinol
show the reaction diagram
-
51% of the activity with ethanol
-
-
?
3-methyl-1-butanol + ubiquinone
3-methyl-1-butanal + ubiquinol
show the reaction diagram
-
48% of the activity with ethanol
-
-
?
acetaldehyde + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
42% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
acetaldehyde + ferricyanide
?
show the reaction diagram
-
13% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
allyl alcohol + ferricyanide
acrolein + ferricyanide
show the reaction diagram
-
the best substrate
-
-
?
allylic alcohol + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
91% activity compared to n-butanol
-
-
?
allylic alcohol + ferricyanide
?
show the reaction diagram
-
96% activity compared to n-butanol
-
-
?
citral + ubiquinol
? + ubiquinone
show the reaction diagram
-
39% of the activity with ethanol
-
-
?
citronellal + ubiquinol
citronellol + ubiquinone
show the reaction diagram
-
45% of the activity with ethanol
-
-
?
citronellol + ubiquinone
citronellal + ubiquinol
show the reaction diagram
-
74% of the activity with ethanol
-
-
?
ethanol + 2,6-dichlorophenol indophenol
acetaldehyde + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
ethanol + acceptor
acetaldehyde + reduced acceptor
show the reaction diagram
ethanol + ferricyanide
acetaldehyde + ferrocyanide
show the reaction diagram
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
show the reaction diagram
formaldehyde + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
38% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
formaldehyde + ferricyanide
?
show the reaction diagram
-
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
show the reaction diagram
-
37% of the activity with ethanol
-
-
?
glutaraldehyde + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
18% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
glutaraldehyde + ferricyanide
?
show the reaction diagram
iso-propanol + ferricyanide
propan-2-one + ferrocyanide
show the reaction diagram
-
about 10% of the activity with n-butanol
-
-
?
isopropanol + ferricyanide
propan-2-one + ferrocyanide
show the reaction diagram
-
18% of the activity with allyl alcohol
-
-
?
methanol + ferricyanide
formaldehyde + ferrocyanide
show the reaction diagram
-
9% of the activity with allyl alcohol
-
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?
n-butanol + 2,6-dichlorophenolindophenol
n-butanal + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
100% activity
-
-
?
n-butanol + ferricyanide
butyraldehyde + ferrocyanide
show the reaction diagram
-
98% of the activity with allyl alcohol
-
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?
n-butanol + ferricyanide
n-butanal + ferrocyanide
show the reaction diagram
-
-
-
-
?
n-pentanol + ferricyanide
n-pentanal + ferrocyanide
show the reaction diagram
-
about 45% of the activity with n-butanol
-
-
?
n-propanol + ferricyanide
n-propanal + ferrocyanide
show the reaction diagram
n-propanol + ferricyanide
propionaldehyde + ferrocyanide
show the reaction diagram
-
90% of the activity with allyl alcohol
-
-
?
n-propanol + oxidized 2,6-dichlorophenolindophenol
n-propanal + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
96% activity compared to n-butanol
-
-
?
propionaldehyde + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
33% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
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-
?
propionaldehyde + ferricyanide
?
show the reaction diagram
-
24% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ethanol + ubiquinone
acetaldehyde + ubiquinol
show the reaction diagram
ethanol + ubiquinone-1
acetaldehyde + ubiquinol-1
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome
-
-
-
cytochrome c
pyrroloquinoline quinone
ubiquinone
-
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
-
ADH contains 5.9 Fe2+ and 2.06 acid-labile sulfurs per heterodimer
additional information
-
an NAD(P)-independent enzyme
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
a heme protein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6-dichloro-4-dicyanovinylphenol
-
i.e. PC-16, competitive quinone reduction inhibition mode, the inhibitor binds to the low affinity quinone binding site(S) QN and/or QL of quinone-bound ADH, overview
antimycin A
Myxothiazol
-
powerful inhibitor of the purified ADH complex, most likely acting at the ubiquinone acceptor site in subunit II
Triton X-100
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethanol
-
ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
additional information
-
acetic acid induces the enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.9
acetaldehyde
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
0.43
allylic alcohol
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
1.3
citral
-
pH 9.0, 30C
2.4
citronellal
-
pH 9.0, 30C
0.0073
citronellol
-
pH 9.0, 30C
0.0038 - 0.66
ethanol
0.025
ferricyanide
-
isolated subunit I
0.11
geraniol
-
pH 9.0, 30C
0.36
n-butanol
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
0.0035 - 0.011
pyrroloquinoline quinone
0.047
ubiquinone-1
-
using ethanol as cosubstrate, pH and temperature not specified in the publication
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30.8
acetaldehyde
Komagataeibacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
67.5
allylic alcohol
Komagataeibacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
71
ethanol
Komagataeibacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
52.3
n-butanol
Komagataeibacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
76.3
ubiquinone-1
Komagataeibacter xylinus
-
using ethanol as cosubstrate, pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
446
acetaldehyde
Komagataeibacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
90
157
allylic alcohol
Komagataeibacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
28106
108
ethanol
Komagataeibacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
69
145
n-butanol
Komagataeibacter xylinus
-
using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication
629
162
ubiquinone-1
Komagataeibacter xylinus
-
using ethanol as cosubstrate, pH and temperature not specified in the publication
1150
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1,3-butanediol
1.3
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1,3-propandiol
3
CCU55317
enzyme in cell membranes, pH 4.5, 20C
3.1
-
purified recombinant enzyme, pH 9.0, 30C, substrate geraniol
3.3
-
purified recombinant enzyme, pH 9.0, 30C, substrate citronellal
3.8
-
purified recombinant enzyme, pH 9.0, 30C, substrate citral
4
-
purified recombinant enzyme, pH 9.0, 30C, substrate 3-methyl-1--butanol
4.4
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-octanol in DMSO; purified recombinant enzyme, pH 9.0, 30C, substrate 2-propanol
4.5
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-hexanol in DMSO
5.4
-
purified recombinant enzyme, pH 9.0, 30C, substrate 2-butanol
5.6
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-octanol in H2O
6.3
-
purified recombinant enzyme, pH 9.0, 30C, substrate citronellol
7.5
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-butanol
7.7
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-propanol
7.9
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-hexanol in H2O
8.2
-
purified recombinant enzyme, pH 9.0, 30C, substrate 1-pentanol
8.5
-
purified recombinant enzyme, pH 9.0, 30C, substrate ethanol
25 - 40
Gluconobacter sp.
-
purified enzyme
32.2
Gluconobacter sp.
-
purified native enzyme
205
purified enzyme
293
-
purified native enzyme
additional information
Gluconobacter sp.
-
171 U/ml
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
CCU55317
-
5.5
-
activity responses to pH are sharp, showing two distinct optimal pH values (pH 5.5 and 6.5) depending on the electron acceptor used (optimum pH 5.5 with ferricyanide as electron acceptor)
6.5
-
activity responses to pH are sharp, showing two distinct optimal pH values (pH 5.5 and 6.5) depending on the electron acceptor used (optimum pH 6.5 when phenazine methosulfate plus 2,6-dichlorophenolindophenol are used as electron acceptors)
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 6
CCU55317
strong decrease of activity at pH levels below pH 4 and above pH 5.5, and no activity at pH 2.0 and pH 7.0, activity range, profile overview
5 - 7.5
-
pH 5.0: about 50% of maximal activity, pH 7.5: about 55% of maximal activity, substrate: ethanol
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 50
CCU55317
activity range, profile overview. No activity above 50C, maximum activity at 20C
25 - 50
-
25C: about 75% of maximal activity, 50C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
-
isoelectric focusing
6.1
-
gradient electrophoresis, determined in pH range 3.4-9.0
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000
-
non-denaturing PAGE
119000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
homodimer
-
two alpha-subunits
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADH-GS, 10 mg/ml protein in 100 mM sodium acetate buffer, pH 4.5, 0.34 mM n-dodecyl-beta-D-maltoside or 0.16 mM C12E8 and either 150 mM ammonium sulfate/6% PEG 3350 or 1.3 M ammonium sulfate only, with or without 2 mM Ca2+, X-ray diffraction structure determination and analysis at 3.0-5.0 A resolution, heavy atom labeling
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
-
stable at 6C, overnight
685650
10
-
at 6C, overnight, about 75% inactivation
685650
11
-
at 6C, overnight, complete inactivation
685650
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
10 min, 95% loss of activity
additional information
-
ADHs from MSU10 and SKU1108 strains exhibit a higher resistance to ethanol and acetic acid than strain IFO3191 enzyme at elevated temperature
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1% Triton X-100 stabilizes the enzyme
Gluconobacter sp.
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, purified enzyme in 10 mM potassium phosphate buffer containing 0.1% (v/v) Triton X-100, 30 days, no appreciable loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 130fold from membranes of glycerol-grown cells by two different steps of anion exchange chromatography, solubilization with 0.1% Triton X-100 or Tween 20, copurification with a cytochrome c
-
native enzyme by anion exchange and hydrophobic interaction chromatography, and dialysis against high-viscosity carboxymethyl cellulose as the absorber
Gluconobacter sp.
-
native enzyme from membranes by anion exchange and cation exchange chromatography, followed by hydroxyapatite chromatography, to near homogeneity
CCU55317
native enzyme from strain JK3, by anion exchange and hydroxylapatite chromatography
native enzyme from strain KKP/584, by anion exchange and hydroxylapatite chromatography
native enzyme from strain V3, by anion exchange and hydroxylapatite chromatography
purification of subunit I and of subunit II
-
QAE-Toyopearl 550C column chromatography, DEAE-Toyopearl 650 M column chromatography, HA-Ultrogel column chromatography, and Sephacryl-S200 gel filtration
-
quinone-bound and quinone-free native enzyme from membranes, purification of an active enzyme is successful with N-dodecyl beta-D-maltoside, but not with Triton X-100
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) pLysS RARE by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene adh, DNA and amino acid sequence determination and analysis, sequence comparisons
gene adhA, DNA and amino acid sequence determination and analysis, sequence comparisons
gene adhS, sequence determination and analysis, encoding quinoprotein alcohol dehydrogenase subunit III
-
gene exaA, expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3) pLysS RARE
-
genes adhA and adhB, encoding subunits I and II, DNA and amino acid sequence determination and analysis,phylogenetic tree
CCU55317
genes exaA2 and exaA3, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
sequence comparisons, phylogenetic tree
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A26V
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
G55D
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
L18Q
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
T104K
-
random mutagenesis, the mutation leads to complpete loss of ethanol oxidizing ability
V107A
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
V36I
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
V54I
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
V70A
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
A26V
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
-
G55D
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
-
V54I
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
-
V70A
-
random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
additional information