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2-methylaminoethanol + 2 O2 + H2O
? + 2 H2O2
-
-
-
-
?
3,3-dimethyl-butanol + O2
3,3-dimethylbutanal + H2O2
-
-
-
-
?
3,3-dimethylbutan-1-ol + 2 O2 + H2O2
?
-
-
-
?
3,3-dimethylbutan-1-ol + O2
?
-
10fold lower activity compared to choline
-
-
?
3-(dimethylamino)propan-1-ol + 2 O2 + H2O
? + 2 H2O2
-
-
-
-
?
3-hydroxypropyl-trimethylamine + 2 O2 + H2O2
?
-
-
-
?
3-trimethylamino-1-propanol + 2 O2 + H2O
3-trimethylaminopropanoate + 2 H2O2
-
-
-
-
?
4-trimethylamino-1-butanol + 2 O2 + H2O
4-trimethylaminobutanoate + 2 H2O2
-
-
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
betaine aldehyde + O2 + H2O
glycine betaine + H2O2
-
-
-
?
choline + 2 O2 + H2O
betaine + 2 H2O2
choline + 2 O2 + H2O2
betaine + 2 H2O2
choline + O2
betaine aldehyde + H2O2
choline + O2 + H2O
betaine + 2 H2O2
-
-
-
?
diethanolamine + O2
?
-
-
-
-
?
diethylamino ethanol + 2 O2 + H2O2
? + 2 H2O2
-
-
-
-
?
diethylaminoethanol + 2 O2 + H2O
? + 2 H2O2
-
-
-
-
?
dimethylaminoethanol + 2 O2 + H2O
? + 2 H2O2
-
-
-
-
?
FADH2 + O2
FAD + H2O2
-
-
-
-
?
glycine betaine + H2O2
betaine aldehyde + O2 + H2O
-
-
-
-
?
monoethanolamine + O2
aminoacetaldehyde + H2O2
N,N-dimethylaminoethanol + O2
(dimethylamino)acetaldehyde + H2O2
N,N-dimethylethanolamine + O2
N,N-dimethylethanalamine + H2O2
-
-
-
-
?
N-methylethanolamine + O2
N-methylethanalamine + H2O2
-
-
-
-
?
tris-(2-hydroxyethyl)-methylammonium methylsulfate + 2 O2 + H2O2
? + 2 H2O2
additional information
?
-
betaine aldehyde + O2 + H2O
betaine + H2O2
-
-
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
-
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
-
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
half-reaction
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
-
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
-
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
half-reaction
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
half-reaction
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
-
-
-
?
choline + 2 O2 + H2O
betaine + 2 H2O2
-
-
-
-
?
choline + 2 O2 + H2O
betaine + 2 H2O2
-
-
-
-
?
choline + 2 O2 + H2O
betaine + 2 H2O2
-
-
-
-
?
choline + 2 O2 + H2O
betaine + 2 H2O2
-
-
-
-
?
choline + 2 O2 + H2O
betaine + 2 H2O2
-
-
-
-
?
choline + 2 O2 + H2O2
betaine + 2 H2O2
-
-
-
?
choline + 2 O2 + H2O2
betaine + 2 H2O2
choline oxidase catalyzes the flavin-mediated, two-step oxidation of choline to glycine betaine with formation of betaine aldehyde as intermediate. Both the oxidation of the alcohol substrate and the aldehyde intermediate require molecular oxygen to accept electrons from the reduced flavin. The reaction of hydride transfer of choline oxidation is rate limiting for the overall turnover of the wild-type and the Glu312Asp enzymes with choline as substrate
-
-
?
choline + 2 O2 + H2O2
betaine + 2 H2O2
two-step oxidation of choline with formation of betaine aldehyde as intermediate, the overall reaction consists of oxidative and reductive half-reactions
-
-
?
choline + 2 O2 + H2O2
betaine + 2 H2O2
-
-
-
-
?
choline + 2 O2 + H2O2
betaine + 2 H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
?
choline + O2
betaine aldehyde + H2O2
choline detection by mono- and bienzyme biosensors
-
-
?
choline + O2
betaine aldehyde + H2O2
choline oxidase as part of a bienzymatic organic phase enzyme electrode analyzed
-
-
?
choline + O2
betaine aldehyde + H2O2
enzyme-based gas sensor, responses and calibration properties of the sensor for both of liquid and gaseous phases, various choline concentrations
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
389716, 389718, 389719, 389720, 389721, 389723, 389724, 389727, 654371, 654773, 654860, 655800, 671605, 672121, 672136, 695885 -
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
r
choline + O2
betaine aldehyde + H2O2
-
FAD-linked reaction
-
-
?
choline + O2
betaine aldehyde + H2O2
-
the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps, overview
-
-
?
choline + O2
betaine aldehyde + H2O2
analysis of asynchronous hydride transfer mechanism for choline oxidation
-
-
?
choline + O2
betaine aldehyde + H2O2
choline shown to be a slow substrate for H351A variant, His351 residue important for substrate binding and hydride transfer reaction
-
-
?
choline + O2
betaine aldehyde + H2O2
localized structural changes trap choline oxidase in a nonfunctional folded conformation, reversible loss of ability to catalyze the oxidation of choline
-
-
?
choline + O2
betaine aldehyde + H2O2
spatial location of the negative charge on residue 312 important for oxidation of alcohol substrate
-
-
?
choline + O2
betaine aldehyde + H2O2
-
half-reaction
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
half-reaction
-
-
?
choline + O2
betaine aldehyde + H2O2
-
half-reaction
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
-
?
choline + O2
betaine aldehyde + H2O2
-
oxidation of choline to glycine betaine via the intermediate betaine aldehyde, glycine betaine production in chloroplasts of transgenic plants, stress-induced expression analysis
-
-
?
monoethanolamine + O2
aminoacetaldehyde + H2O2
-
-
-
-
?
monoethanolamine + O2
aminoacetaldehyde + H2O2
-
-
-
-
?
N,N-dimethylaminoethanol + O2
(dimethylamino)acetaldehyde + H2O2
-
-
-
-
?
N,N-dimethylaminoethanol + O2
(dimethylamino)acetaldehyde + H2O2
-
-
-
-
?
N,N-dimethylaminoethanol + O2
(dimethylamino)acetaldehyde + H2O2
-
-
-
-
?
triethanolamine + O2
?
-
-
-
-
?
triethanolamine + O2
?
-
-
-
?
triethanolamine + O2
?
-
-
-
-
?
triethanolamine + O2
?
-
-
-
-
?
tris-(2-hydroxyethyl)-methylammonium methylsulfate + 2 O2 + H2O2
? + 2 H2O2
-
-
-
-
?
tris-(2-hydroxyethyl)-methylammonium methylsulfate + 2 O2 + H2O2
? + 2 H2O2
-
-
-
-
?
additional information
?
-
-
flavoprotein choline oxidase catalyzes the oxidation of choline to glycine betaine with transient formation of an aldehyde intermediate and molecular oxygen as final electron acceptor
-
-
?
additional information
?
-
poor substrate for wild-type, but substrate for mutants is 1-hexanol, reaction of EC 1.1.3.13
-
-
-
additional information
?
-
-
the enzyme shows activity with trimethylamino alcohols and dimethylamino alcohols, but the Km increases with the number of methyl groups on the ammonium head group. N-replaced choline analogues as substrates lead to decreased maximum reaction velocities. The enzyme from Fusarium oxysporum shows a high affinity for choline and betaine aldehyde
-
-
?
additional information
?
-
-
no activity with betaine, monoethanolamine, triethanolamine, dimethylamino-1-butanol, N,N-dimethylglycine methylester, beta-methylcholine, L-carnitine, propanol, ethanol, and methanol
-
-
?
additional information
?
-
-
the enzyme shows activity with trimethylamino alcohols and dimethylamino alcohols, but the Km increases with the number of methyl groups on the ammonium head group. N-replaced choline analogues as substrates lead to decreased maximum reaction velocities. The enzyme from Fusarium oxysporum shows a high affinity for choline and betaine aldehyde
-
-
?
additional information
?
-
-
no activity with betaine, monoethanolamine, triethanolamine, dimethylamino-1-butanol, N,N-dimethylglycine methylester, beta-methylcholine, L-carnitine, propanol, ethanol, and methanol
-
-
?
additional information
?
-
-
Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate
-
-
?
additional information
?
-
-
Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate
-
-
?
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1.01
3,3-dimethyl-1-butanol
-
pH 8.0, 25°C
0.11 - 8.7
Betaine aldehyde
2.3 - 2.35
betaine-aldehyde
14
N,N-Dimethylaminoethanol
-
-
0.32
N,N-dimethylethanolamine
-
pH 8.0, 25°C
0.52
N-Methylethanolamine
-
pH 8.0, 25°C
additional information
additional information
-
0.11
Betaine aldehyde
mutant S101C, pH 10, 25°C
0.21
Betaine aldehyde
mutant S101T, pH 10, 25°C
0.39
Betaine aldehyde
-
pH 9.5, 25°C
0.54
Betaine aldehyde
mutant S101V, pH 10, 25°C
2.3
betaine-aldehyde
pH 7.0, 25°C
2.35
betaine-aldehyde
-
19°C, pH 7.0
0.25
choline
-
pH 10, 25°C
0.25
choline
wild type enzyme, in 50 mM sodium diphosphate, pH 10.0, at 25°C
0.26
choline
mutant enzyme S101A, in 50 mM sodium diphosphate, pH 10.0, at 25°C
0.28
choline
-
pH 9.5, 25°C
0.4
choline
wild type enzyme, at pH 7.0 and 25°C
0.43
choline
-
pH 8.0, 25°C
0.48
choline
-
pH 10.0, 25°C, mutant N510H
0.5
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, 0°C
0.5
choline
previously stored at pH 6 and 0°C, measured at pH 7 and 25°C
0.55
choline
-
19°C, pH 7.0
0.6
choline
-
pH 7.0, 25°C, wild-type enzyme
0.6
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 8.0, at -20°C or 0°C
0.6
choline
previously stored at pH 8 and -20°C, measured at pH 7 and 25°C
0.6
choline
previously stored at pH 8 and 0°C, measured at pH 7 and 25°C
0.61
choline
wild-type, 30°C, pH 8
0.7
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, -20°C
0.7
choline
previously stored at pH 6 and -20°C, measured at pH 7 and 25°C
0.8
choline
mutant enzyme M62A, at pH 7.0 and 25°C
1.3
choline
substrate choline, pH 7, 25°C
1.7
choline
-
pH 7.0, 25°C, wild type
1.7
choline
-
pH 10.0, 25°C, mutant N510A
1.7 - 1.8
choline
-
enzyme immobilized in polyethylenimine-coated silica-monolith, apparent value, pH and temperature not specified in the publication
1.8
choline
mutant S101A/V355T/F357R/M359R, 30°C, pH 8
2.01
choline
mutant M359R, 30°C, pH 8
2.1
choline
-
free enzyme, apparent value, pH and temperature not specified in the publication
3.3
choline
mutant S101A, 30°C, pH 8
3.4
choline
mutant S101A/V355T/F357R, 30°C, pH 8
4.7
choline
mutant S101A/D250G/F253R/V355T/F357R/M359R, 30°C, pH 8
5.8
choline
mutant V355T/F357R, 30°C, pH 8
7
choline
-
at 38°C and pH 7.6
9
choline
mutant enzyme M62A/F357A, at pH 7.0 and 25°C
12
choline
mutant enzyme F357A, at pH 7.0 and 25°C
29
choline
-
pH 7.0, 25°C mutant H466A
60
choline
-
pH 7.0, 25°C, mutant N510H
155
choline
-
pH 7.0, 25°C, mutant N510A
213
choline
-
pH 7.0, 25°C, mutant N510L
0.006
O2
mutant S101V, pH 10, 25°C
0.014
O2
mutant S101C, pH 10, 25°C
0.055
O2
-
pH 10.0, 25°C, mutant N510A
0.21
O2
mutant S101A, pH 10, 25°C
0.48
O2
mutant S101T, pH 10, 25°C
0.535
O2
-
pH 10.0, 25°C, mutant N510H
0.6
O2
wild type enzyme, in 50 mM potassium phosphate (pH 7.0), at 25°C
0.69
O2
-
pH 10, 25°C, cosubstrate choline
2
O2
wild-type, pH 10, 25°C
2.54
O2
-
pH 10, 25°C, cosubstrate betaine aldehyde
21
O2
-
pH 7.0, 25°C, mutant H466A
67
O2
mutant enzyme H351Q, in 50 mM potassium phosphate (pH 7.0), at 25°C
703
O2
-
pH 7.0, 25°C, wild type
additional information
additional information
-
stopped-flow kinetics
-
additional information
additional information
-
kinetics and redox potentiometric analysis of liganded and unliganded wild-type and mutant enzymes, comparison of spectral parameters of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics and thermodynamics, steady state kinetic mechanism
-
additional information
additional information
-
kinetics, recombinant enzyme, NMR-determination of hydration ratio of betaine aldehyde, overview
-
additional information
additional information
-
kinetics, recombinant enzyme, overview
-
additional information
additional information
-
steady-state kinetics and thermodynamics, effect of pH on the hysteretic behavior of the enzyme at 25°C, kinetic parameters of enzyme stored at pH 6.0 and -20°C, overview
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes at different pH and in presence or absence of imidazole, kinetic isotope effects
-
additional information
additional information
similar level of catalytic activity than free enzyme in solution
-
additional information
additional information
analysis of steady-state kinetic mechanism, activation of alcohol substrate, hydride ion transfer
-
additional information
additional information
-
analysis of steady-state kinetic mechanism, activation of alcohol substrate, hydride ion transfer
-
additional information
additional information
analysis of substrate kinetic isotope effects
-
additional information
additional information
minimal kinetic mechanism for reductive half-reaction of the V464A and V464T mutant enzymes, oxidative half-reactions' steady-state kinetic mechanisms, overview
-
additional information
additional information
-
steady-state kinetics, isotopic effects, detailed overview
-
additional information
additional information
stopped-flow and steady-state kinetics, and sequential steady-state kinetic mechanism, overview
-
additional information
additional information
-
stopped-flow kinetics of oxidative half-reaction, deuterium kinetic isotope effects in steady-state kinetics, e.g.. second-order rate constants, overview
-
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8
3,3-dimethyl-1-butanol
-
pH 8.0, 25°C
0.2 - 133
Betaine aldehyde
1.71 - 11.6
betaine-aldehyde
5.9
N,N-dimethylethanolamine
-
pH 8.0, 25°C
0.37
N-Methylethanolamine
-
pH 8.0, 25°C
additional information
additional information
overall turnover of mutant variant about 60-fold decreased with choline compared to wild-type enzyme
-
0.2
Betaine aldehyde
mutant S101V, pH 10, 25°C
0.7
Betaine aldehyde
mutant S101C, pH 10, 25°C
21
Betaine aldehyde
mutant S101T, pH 10, 25°C
42
Betaine aldehyde
mutant S101A, pH 10, 25°C
43
Betaine aldehyde
mutant enzyme S101A, in 50 mM sodium diphosphate, pH 10.0, at 25°C
133
Betaine aldehyde
-
pH 10, 25°C
133
Betaine aldehyde
wild type enzyme, in 50 mM sodium diphosphate, pH 10.0, at 25°C
133
Betaine aldehyde
wild-type, pH 10, 25°C
1.71
betaine-aldehyde
-
19°C, pH 7.0
11.6
betaine-aldehyde
pH 7.0, 25°C
0.02
choline
-
pH 7.0, 25°C, mutant N510L
0.02
choline
mutant S101A/D250G/F253R/V355T/F357R/M359R, 30°C, pH 8
0.02
choline
mutant S101A/V355T/F357R/M359R, 30°C, pH 8
0.03
choline
-
pH 5.5, 25°C, mutant H466A
0.03
choline
-
pH 5.5, 25°C, recombinant mutant H466A
0.06
choline
-
pH 7.0, 25°C, mutant N510A
0.07
choline
-
pH 6.0, 25°C, recombinant mutant H466A
0.09
choline
-
pH 10.0, 25°C, mutant N510A
0.17
choline
mutant S101A/V355T/F357R, 30°C, pH 8
0.19
choline
mutant V355T/F357R, 30°C, pH 8
0.21
choline
-
pH 5.5, 25°C, mutant H466A, presence of imidazole
0.37
choline
-
pH 7.0, 25°C, recombinant mutant H466A
0.51
choline
-
pH 7.0, 25°C, mutant N510H
0.52
choline
-
pH 7.0, 25°C, mutant H466A, presence of imidazole
0.7
choline
-
pH 10.0, 25°C, mutant H466A, presence of imidazole
0.72
choline
-
pH 8.0, 25°C, recombinant mutant H466A
0.73
choline
-
pH 10.0, 25°C, mutant H466A
0.73
choline
-
pH 10.0, 25°C, recombinant mutant H466A
1.03
choline
apparent, H99N mutant, substrate choline, pH 7, 25°C. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system
1.1
choline
-
pH 7.0, 25°C, mutant H466A
1.86
choline
H99N mutant, substrate choline, pH 7, 25°C. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system
2.24
choline
-
19°C, pH 7.0
2.5
choline
mutant enzyme F357A, at pH 7.0 and 25°C
2.83
choline
-
enzyme immobilized in polyethylenimine-coated silica-monolith, apparent value, pH and temperature not specified in the publication
3
choline
-
free enzyme, apparent value, pH and temperature not specified in the publication
3.4
choline
-
pH 10.0, 25°C, mutant N510H
4.4
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, -20°C
4.4
choline
previously stored at pH 6 and -20°C, measured at pH 7 and 25°C
4.52
choline
mutant S101A, 30°C, pH 8
6.7
choline
mutant enzyme S101A, in 50 mM sodium diphosphate, pH 10.0, at 25°C
6.8
choline
mutant enzyme M62A/F357A, at pH 7.0 and 25°C
9.02
choline
mutant M359R, 30°C, pH 8
12.5
choline
mutant enzyme M62A, at pH 7.0 and 25°C
13.3
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, 0°C
13.3
choline
previously stored at pH 6 and 0°C, measured at pH 7 and 25°C
13.4
choline
pH 7.0, 25°C
13.4
choline
-
pH 7.0, 25°C, wild-type enzyme
14.5
choline
wild-type, 30°C, pH 8
14.9
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 8.0, -20°C
14.9
choline
previously stored at pH 8 and 0°C, measured at pH 7 and 25°C
15.5
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 8.0, 0°C
15.5
choline
previously stored at pH 8 and -20°C, measured at pH 7 and 25°C
20
choline
wild type enzyme, at pH 7.0 and 25°C
60
choline
wild type enzyme, in 50 mM sodium diphosphate, pH 10.0, at 25°C
61
choline
-
pH 7.0, 25°C, wild type
86
choline
-
pH 8.0, 25°C
0.09
O2
-
pH 10.0, 25°C, mutant N510A
0.33
O2
mutant enzyme H351Q, in 50 mM potassium phosphate (pH 7.0), at 25°C
3.4
O2
-
pH 10.0, 25°C, mutant N510H
15
O2
wild type enzyme, in 50 mM potassium phosphate (pH 7.0), at 25°C
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E312A
generated for investigation of the negative charge on Glu312, enzyme inactive
E312Q
generated for investigation of the negative charge on Glu312, Kd value for choline about 500times larger than that of wild-type
F357A
the mutant shows about 240fold reduced catalytic efficiency compared to the wild type enzyme
H351A
generated by site-directed mutagenesis
H351Q
the kcat and kcat/Km values of the H351Q emutant in atmospheric oxygen are 45 and 5000fold lower than those of the wild type enzyme, respectively
H466D
-
site-directed mutagenesis, the mutation alters the flavin binding to the enzyme, while substrate choline is normally bound, binding og glycine btaine is inhibited, spectrometrical analysis, the mutant shows a different flavin-binding stoichiometry of 0.29:1, compared to 1:1 for the wild-type enzyme, stabilized at pH 6.0-10.0, overview, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutant H466A and the wild-type enzyme, the mutant shows no catalytic activity
H99N
mutant, analysis of kinetic parameters
M359R
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13
M62A
the mutant shows about 3fold reduced catalytic efficiency compared to the wild type enzyme
M62A/F357A
the enzyme shows a lack of the isomerization detected in wild type choline oxidase, and a lack of saturation with an oxygen concentration as high as 1 mM, while most other kinetic parameters are similar to those of wild type choline oxidase
N510A
-
site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein, enzyme kinetics decrease of 4300fold in the kcat/Kcholine, 600fold in the kred, 660fold in the kcat, and 50fold in the kcat/Koxygen values
N510D
-
site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein, 75% of the flavin associates noncovalently, inactive mutant
N510H
-
site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein, decreases in the kcat/Kcholine, the kred, the kcat, and the kcat/Koxygen values
N510L
-
site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein
S101A/D250G/F253R/V355T/F357R/M359R
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13, with a 20fold increased kcat compared to that of the wildtype enzyme. This variant enables the oxidation of 10 mM hexanol to hexanal in less than 24h with 100% conversion and catalyzes significantly improved oxidation of saturated, unsaturated, aliphatic, cyclic and benzylic alcohols
S101A/V355T/F357R
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13
S101A/V355T/F357R/M359R
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13
S101V
contrary to wild-type, stopped-flow traces for the reductive half-reaction are biphasic, corresponding to the reactions of proton abstraction and hydride transfer. The rate constants for proton transfer in the S101T/C/V variants decrease logarithmically with increasing hydrophobicity of residue 101
V355T/F357R
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13
A21V
-
site-directed mutagenesis in the FAD binding site
A21V/G62D
-
site-directed mutagenesis, the mutant shows 1.93fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and slightly reduced activity with choline compared to the wild-type enzyme
A21V/G62D/I69V
-
site-directed mutagenesis, the mutant shows 1.68fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme
A21V/G62D/I69V/S348L
-
site-directed mutagenesis, the mutant shows 3.45fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme
A21V/G62D/S348C
-
site-directed mutagenesis, the mutant shows 5.18fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme
A21V/G62D/S348L
-
site-directed mutagenesis, the mutant shows 3.72fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme
A21V/G62D/S348L/V349L
-
site-directed mutagenesis, the mutant shows 5.75fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme
A21V/K394R
-
site-directed mutagenesis, the mutant shows 85% activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme
F351Y
-
site-directed mutagenesis in the substrate binding site, the mutant shows reduced activity with choline compared to the wild-type enzyme
G62D
-
site-directed mutagenesis in the FAD binding site, the mutant shows 2fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme
G62D/F351Y
-
site-directed mutagenesis, the mutant shows 2.14fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme
G62D/R249H/F351Y
-
site-directed mutagenesis, the mutant shows 2.7fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme
I69V
-
site-directed mutagenesis in the FAD binding site, the mutant shows93% activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme
P393Q/S530G
-
site-directed mutagenesis, the mutant shows 1.5fold increased activity with choline compared to the wild-type enzyme
S348L
-
site-directed mutagenesis in the substrate binding site
T116I/K128M
-
site-directed mutagenesis, the mutant shows unaltered activity with choline compared to the wild-type enzyme
T116I/K128M/P393Q/S530G
-
site-directed mutagenesis, the mutant shows 2.32fold increased activity with choline compared to the wild-type enzyme
V349L
-
site-directed mutagenesis in the substrate binding site
A21V
-
site-directed mutagenesis in the FAD binding site
-
G62D
-
site-directed mutagenesis in the FAD binding site, the mutant shows 2fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme
-
I69V
-
site-directed mutagenesis in the FAD binding site, the mutant shows93% activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme
-
S348L
-
site-directed mutagenesis in the substrate binding site
-
V349L
-
site-directed mutagenesis in the substrate binding site
-
E312D
generated for investigation of the negative charge on Glu312, kcat values about 230times lower and and kcat/Km values about 35times lower than in the wild-type, solvent viscosity and substrate kinetic isotope effects indicates presence of internal equilibrium prior to the hydride transfer reaction
E312D
-
mutant, analysis of temperature dependent rate constants
E312D
site-directed mutagenesis, the mutant enzyme shows a 260fold decrease in the rate constant for the hydride transfer reaction and did not transfer the hydride ion in a full quantum mechanical tunneling fashion. The overall turnover of the Glu312Asp enzyme at saturating concentrations of 3-hydroxypropyl-trimethylamine and oxygen is predominantly controlled by the hydride transfer reaction that results in the reduction of the enzyme-bound flavin. The kred value with 3-hydroxypropyl-trimethylamine is 20times higher than the value determined with choline as substrate for the Glu312Asp enzyme. The reductive half-reaction can be effectively, but not completely,rescued upon introducing on the substrate the methylenethat is missing from the side chain of residue 312
H466A
-
decrease in kcat and kcat/Km-value for choline, but not for oxygen, partial rescue of activity in presence of imidazolium
H466A
-
site-directed mutagenesis, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutant H466D and the wild-type enzyme
H466A
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme, the enzyme activity in the mutant strain can partially be rescued by addition of exogenous imidazolium, but not by imidazole, overview
H466Q
inactive
H466Q
the unusual fluorescence behavior of the enzyme is lost in the mutant
S101A
mutant enzyme with increased efficiencies in the oxidative half-reactions and decreased efficiencies in the reductive half-reactions accompanied by a significant decrease in the overall rate of turnover with choline. Ser101 is important, but not essential, for catalysis
S101A
mutant displays increased activity with hexan-1-ol, reaction of EC 1.1.3.13
S101A
similar to wild-type mutant displays in 20 mM Tris-HCl flavin maxima in the near-UV and visible regions typical of oxidized flavins
S101A
stopped-flow traces for the reductive half-reaction are monophasic like wild-type choline oxidase
S101A
the unusual fluorescence behavior of the enzyme persists in the mutant
S101C
contrary to wild-type, stopped-flow traces for the reductive half-reaction are biphasic, corresponding to the reactions of proton abstraction and hydride transfer. The rate constants for proton transfer in the S101T/C/V variants decrease logarithmically with increasing hydrophobicity of residue 101
S101C
in presence of protonated Tris in the active site, the reversible formation of a C4a-S-cysteinyl8alpha-N3-histidyl flavin is observed
S101T
contrary to wild-type, stopped-flow traces for the reductive half-reaction are biphasic, corresponding to the reactions of proton abstraction and hydride transfer. The rate constants for proton transfer in the S101T/C/V variants decrease logarithmically with increasing hydrophobicity of residue 101
S101T
similar to wild-type mutant displays in 20 mM Tris-HCl flavin maxima in the near-UV and visible regions typical of oxidized flavins
V464A
mutant, analysis of kinetic parameters
V464A
site-directed mutagenesis, mutation of the residue near the flavin C(4a) atom and the hydrophobic cavity, replacement of Val464 with alanine or threonine does not affect the reductive half-reaction, but it reduces the oxidative half-reaction by about 50fold, and the 3D structure of the Val464Ala enzyme is essentially identical to that of the wild-type enzyme
V464T
mutant, analysis of kinetic parameters
V464T
site-directed mutagenesis, mutation of the residue near the flavin C(4a) atom and the hydrophobic cavity, replacement of Val464 with alanine or threonine does not affect the reductive half-reaction, but it reduces the oxidative half-reaction by about 50fold
additional information
-
enzyme immobilization by 6-O-ethoxytrimethylammoniumchitosan chloride, and construction of amperometric choline biosensors prepared by layer-by-layer deposition of choline oxidase on the Prussian blue-modified platinum electrode, method optimization
additional information
-
engineering of Eucalyptus plants via expression of bacterial choline oxidase to develop environmental-stress resistant Eucalyptus globulus for expanding the plantation area of this species. Glycine betaine accumulation in transgenic plants
additional information
-
substitution of Asn510 with alanine, but not with histidine, results in a change from stepwise to concerted mechanisms for the cleavages of the OH and CH bonds of choline catalyzed by the enzyme
additional information
-
evaluation of the stress-inducible production of Arthrobacter pascens choline oxidase in transgenic rice as a strategy for producing the stress-protectant glycine betaine, stress induction by 150 mM NaCl, biomass production in wild-type and transgenic plants
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Hatefi, Y.; Stiggall, D.L.
Metal-containing flavoprotein dehydrogenases
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Rattus norvegicus
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Arthrobacter globiformis
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Achromobacter cholinophagum, Cylindrocarpon didymum, Cylindrocarpon didymum M-1
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Covalently bound flavin as prosthetic group of choline oxidase
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Molecular characterization of the bet genes encoding glycine betaine synthesis in Sinorhizobium meliloti 102F34
Microbiology
143
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Arthrobacter globiformis, Arthrobacter pascens, Cylindrocarpon didymum, Sinorhizobium meliloti, Sinorhizobium meliloti 102F34, Cylindrocarpon didymum M-1
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Metabolic engineering of rice leading to biosynthesis of glycinebetaine and tolerance to salt and cold
Plant Mol. Biol.
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Arthrobacter globiformis
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Doretti, L.; Ferrara, D.; Lora, S.; Palma, G.
Amperometric biosensor involving covalent immobilization of choline oxidase and butyrylcholinesterase on a methacrylate-vinylene carbonate co-polymer
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29
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1999
Alcaligenes sp.
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Transformation of Arabidopsis with the codA gene for choline oxidase enhances freezing tolerance of plants
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22
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2000
Arthrobacter globiformis
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An acetylcholinesterase/choline oxidase-based amperometric biosensor as a liquid chromatography detector for acetylcholine and choline determination in brain tissue homogenates
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73
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2001
Alcaligenes sp.
brenda
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Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance
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421
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2004
Arthrobacter globiformis (Q7X2H8), Arthrobacter globiformis
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The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase
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430
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Arthrobacter globiformis
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Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis
Biochemistry
42
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2003
Arthrobacter globiformis
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Ghanem, M.; Gadda, G.
On the catalytic role of the conserved active site residue His466 of choline oxidase
Biochemistry
44
893-904
2005
Arthrobacter globiformis
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Gadda, G.
Kinetic mechanism of choline oxidase from Arthrobacter globiformis
Biochim. Biophys. Acta
1646
112-118
2003
Arthrobacter globiformis
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Gadda, G.
pH and deuterium kinetic isotope effects studies on the oxidation of choline to betaine-aldehyde catalyzed by choline oxidase
Biochim. Biophys. Acta
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2003
Arthrobacter globiformis
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Fan, F.; Gadda, G.
On the catalytic mechanism of choline oxidase
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Arthrobacter globiformis
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Gadda, G.; Fan, F.; Hoang, J.V.
On the contribution of the positively charged headgroup of choline to substrate binding and catalysis in the reaction catalyzed by choline oxidase
Arch. Biochem. Biophys.
451
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2006
Arthrobacter globiformis
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Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3,3-dimethylbutyraldehyde
Biochemistry
45
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2006
Arthrobacter globiformis
brenda
Ghanem, M.; Gadda, G.
Effects of reversing the protein positive charge in the proximity of the flavin N(1) locus of choline oxidase
Biochemistry
45
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2006
Arthrobacter globiformis
brenda
Tavakoli, H.; Ghourchian, H.; Moosavi-Movahedi, A.A.; Chilaka, F.C.
Effects of paraoxon and ethylparathion on choline oxidase from Alcaligenes species: inhibition and denaturation
Int. J. Biol. Macromol.
36
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2005
Alcaligenes sp.
brenda
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Oxygen- and temperature-dependent kinetic isotope effects in choline oxidase: correlating reversible hydride transfer with environmentally enhanced tunneling
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127
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2005
Arthrobacter globiformis
brenda
Su, J.; Hirji, R.; Zhang, L.; He, C.; Selvaraj, G.; Wu, R.
Evaluation of the stress-inducible production of choline oxidase in transgenic rice as a strategy for producing the stress-protectant glycine betaine
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57
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2006
Arthrobacter pascens
brenda
Tavakoli, H.; Ghourchian, H.; Moosavi-Movahedi, A.A.; Saboury, A.A.
Histidine and serine roles in catalytic activity of choline oxidase from Alcaligenes species studied by chemical modifications
Process Biochem.
41
477-482
2006
Alcaligenes sp.
-
brenda
Hoang, J.V.; Gadda, G.
Trapping choline oxidase in a nonfunctional conformation by freezing at low pH
Proteins
66
611-620
2007
Arthrobacter globiformis
brenda
Shi, H.; Yang, Y.; Huang, J.; Zhao, Z.; Xu, X.; Anzai, J.; Osa, T.; Chen, Q.
Amperometric choline biosensors prepared by layer-by-layer deposition of choline oxidase on the Prussian blue-modified platinum electrode
Talanta
70
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2006
Arthrobacter globiformis
brenda
Campanella, L.; Lelo, D.; Martini, E.; Tomassetti, M.
Organophosphorus and carbamate pesticide analysis using an inhibition tyrosinase organic phase enzyme sensor; comparison by butyrylcholinesterase+choline oxidase opee and application to natural waters
Anal. Chim. Acta
587
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2007
Alcaligenes sp. (P16101)
brenda
Fan, F.; Gadda, G.
An internal equilibrium preorganizes the enzyme-substrate complex for hydride tunneling in choline oxidase
Biochemistry
46
6402-6408
2007
Arthrobacter globiformis (Q7X2H8)
brenda
Quaye, O.; Lountos, G.T.; Fan, F.; Orville, A.M.; Gadda, G.
Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase
Biochemistry
47
243-256
2008
Arthrobacter globiformis (Q7X2H8)
brenda
Rungsrisuriyachai, K.; Gadda, G.
On the role of histidine 351 in the reaction of alcohol oxidation catalyzed by choline oxidase
Biochemistry
47
6762-6769
2008
Arthrobacter globiformis (Q7X2H8)
brenda
Lopez, M.S.; Perez, J.P.; Lopez-Cabarcos, E.; Lopez-Ruiz, B.
Amperometric biosensors based on choline oxidase entrapped in polyacrylamide microgels
Electroanalysis
19
370-378
2007
Alcaligenes sp. (P16101)
-
brenda
Kudo, H.; Goto, T.; Saito, T.; Saito, H.; Otsuka, K.; Mitsubayashi, K.
Biochemical sniffer with choline oxidase for measurement of choline vapour
Microchim. Acta
160
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2008
Alcaligenes sp. (P16101)
-
brenda
Ahmad, R.; Kim, M.D.; Back, K.H.; Kim, H.S.; Lee, H.S.; Kwon, S.Y.; Murata, N.; Chung, W.I.; Kwak, S.S.
Stress-induced expression of choline oxidase in potato plant chloroplasts confers enhanced tolerance to oxidative, salt, and drought stresses
Plant Cell Rep.
27
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2008
Solanum tuberosum
brenda
Hoang, J.V.; Gadda, G.
Trapping choline oxidase in a nonfunctional conformation by freezing at low pH
Proteins Struct. Funct. Bioinform.
66
611-620
2007
Arthrobacter globiformis (Q7X2H8)
brenda
Hekmat, A.; Saboury, A.A.; Moosavi-Movahedi, A.A.; Ghourchian, H.; Ahmad, F.
Effects of pH on the activity and structure of choline oxidase from Alcaligenes species
Acta Biochim. Pol.
55
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2008
Alcaligenes sp.
brenda
Heinze, B.; Hoven, N.; OConnell, T.; Maurer, K.H.; Bartsch, S.; Bornscheuer, U.T.
Recovery of choline oxidase activity by in vitro recombination of individual segments
Appl. Microbiol. Biotechnol.
81
275-282
2008
Arthrobacter pascens
brenda
Quaye, O.; Gadda, G.
Effect of a conservative mutation of an active site residue involved in substrate binding on the hydride tunneling reaction catalyzed by choline oxidase
Arch. Biochem. Biophys.
489
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2009
Arthrobacter globiformis
brenda
Gadda, G.
Hydride transfer made easy in the reaction of alcohol oxidation catalyzed by flavin-dependent oxidases
Biochemistry
47
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2008
Arthrobacter globiformis (Q7X2H8), Arthrobacter globiformis
brenda
Finnegan, S.; Gadda, G.
Substitution of an active site valine uncovers a kinetically slow equilibrium between competent and incompetent forms of choline oxidase
Biochemistry
47
13850-13861
2008
Arthrobacter globiformis (Q7X2H8), Arthrobacter globiformis
brenda
Orville, A.M.; Lountos, G.T.; Finnegan, S.; Gadda, G.; Prabhakar, R.
Crystallographic, spectroscopic, and computational analysis of a flavin C4a-oxygen adduct in choline oxidase
Biochemistry
48
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2009
Arthrobacter globiformis (Q7X2H8)
brenda
Hekmat, A.; Saboury, A.; Divsalar, A.; Khanmohammadi, M.
Conformational and structural changes of choline oxidase from Alcaligenes species by changing pH values
Bull. Korean Chem. Soc.
29
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2008
Alcaligenes sp.
-
brenda
Singh, A.K.; Singh, B.P.; Prasad, G.B.; Gaur, S.N.; Arora, N.
Safety assessment of bacterial choline oxidase protein introduced in transgenic crops for tolerance against abiotic stress
J. Agric. Food Chem.
56
12099-12104
2008
Arthrobacter globiformis
brenda
Quaye, O.; Cowins, S.; Gadda, G.
Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase
J. Biol. Chem.
284
16990-16997
2009
Arthrobacter globiformis (Q7X2H8)
brenda
Finnegan, S.; Yuan, H.; Wang, Y.F.; Orville, A.M.; Weber, I.T.; Gadda, G.
Structural and kinetic studies on the Ser101Ala variant of choline oxidase: catalysis by compromise
Arch. Biochem. Biophys.
501
207-213
2010
Arthrobacter globiformis (Q7X2H8)
brenda
He, P.; Greenway, G.; Haswell, S.
Development of enzyme immobilized monolith micro-reactors integrated with microfluidic electrochemical cell for the evaluation of enzyme kinetics
Microfluid Nanofluidics
8
565-573
2010
Alcaligenes sp.
-
brenda
Ribitsch, D.; Winkler, S.; Gruber, K.; Karl, W.; Wehrschuetz-Sigl, E.; Eiteljoerg, I.; Schratl, P.; Remler, P.; Stehr, R.; Bessler, C.; Mussmann, N.; Sauter, K.; Maurer, K.H.; Schwab, H.
Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents
Appl. Microbiol. Biotechnol.
87
1743-1752
2010
Glutamicibacter nicotianae, Glutamicibacter nicotianae DSM Z-ID 96-878
brenda
Quaye, O.; Nguyen, T.; Gannavaram, S.; Pennati, A.; Gadda, G.
Rescuing of the hydride transfer reaction in the Glu312Asp variant of choline oxidase by a substrate analogue
Arch. Biochem. Biophys.
499
1-5
2010
Arthrobacter globiformis (Q7X2H8)
brenda
Rungsrisuriyachai, K.; Gadda, G.
Role of asparagine 510 in the relative timing of substrate bond cleavages in the reaction catalyzed by choline oxidase
Biochemistry
49
2483-2490
2010
Arthrobacter globiformis
brenda
Finnegan, S.; Agniswamy, J.; Weber, I.T.; Gadda, G.
Role of valine 464 in the flavin oxidation reaction catalyzed by choline oxidase
Biochemistry
49
2952-2961
2010
Arthrobacter globiformis (Q7X2H8)
brenda
Gannavaram, S.; Gadda, G.
Relative timing of hydrogen and proton transfers in the reaction of flavin oxidation catalyzed by choline oxidase
Biochemistry
52
1221-1226
2013
Arthrobacter globiformis, Arthrobacter globiformis ATCC 8010
brenda
Enokibara, S.
Purification and characterization of an alkaliphilic choline oxidase of Fusarium oxysporum
Biosci. Biotechnol. Biochem.
76
2219-2224
2012
Fusarium oxysporum, Fusarium oxysporum V2
brenda
Matsunaga, E.; Nanto, K.; Oishi, M.; Ebinuma, H.; Morishita, Y.; Sakurai, N.; Suzuki, H.; Shibata, D.; Shimada, T.
Agrobacterium-mediated transformation of Eucalyptus globulus using explants with shoot apex with introduction of bacterial choline oxidase gene to enhance salt tolerance
Plant Cell Rep.
31
225-235
2012
Arthrobacter globiformis
brenda
Salvi, F.; Wang, Y.F.; Weber, I.T.; Gadda, G.
Structure of choline oxidase in complex with the reaction product glycine betaine
Acta Crystallogr. Sect. D
70
405-413
2014
Arthrobacter globiformis (Q7X2H8), Arthrobacter globiformis
brenda
Sanz-Vicente, I.; Dominguez, A.; Ferrandez, C.; Galban, J.
Enzymatic methods for choline-containing water soluble phospholipids based on fluorescence of choline oxidase: Application to lyso-PAF
Anal. Biochem.
519
30-37
2017
Alcaligenes sp.
brenda
Smitherman, C.; Rungsrisuriyachai, K.; Germann, M.W.; Gadda, G.
Identification of the catalytic base for alcohol activation in choline oxidase
Biochemistry
54
413-421
2015
Arthrobacter globiformis (Q7X2H8)
brenda
Salvi, F.; Rodriguez, I.; Hamelberg, D.; Gadda, G.
Role of F357 as an oxygen gate in the oxidative half-reaction of choline oxidase
Biochemistry
55
1473-1484
2016
Arthrobacter globiformis (Q7X2H8), Arthrobacter globiformis
brenda
Santos, R.M.; Laranjinha, J.; Barbosa, R.M.; Sirota, A.
Simultaneous measurement of cholinergic tone and neuronal network dynamics in vivo in the rat brain using a novel choline oxidase based electrochemical biosensor
Biosens. Bioelectron.
69
83-94
2015
Rattus norvegicus
brenda
Keighron, J.D.; Akesson, S.; Cans, A.S.
Coimmobilization of acetylcholinesterase and choline oxidase on gold nanoparticles: stoichiometry, activity, and reaction efficiency
Langmuir
30
11348-11355
2014
Alcaligenes sp.
brenda
Sigolaeva, L.V.; Guenther, U.; Pergushov, D.V.; Gladyr, S.Y.; Kurochkin, I.N.; Schacher, F.H.
Sequential pH-dependent adsorption of ionic amphiphilic diblock copolymer micelles and choline oxidase onto conductive substrates: toward the design of biosensors
Macromol. Biosci.
14
1039-1051
2014
Alcaligenes sp.
brenda
Yu, X.; Kikuchi, A.; Matsunaga, E.; Morishita, Y.; Nanto, K.; Sakurai, N.; Suzuki, H.; Shibata, D.; Shimada, T.; Watanabe, K.
The choline oxidase gene codA confers salt tolerance to transgenic Eucalyptus globulus in a semi-confined condition
Mol. Biotechnol.
54
320-330
2013
Arthrobacter globiformis (Q7X2H8)
brenda
Yu, X.; Kikuchi, A.; Matsunaga, E.; Shimada, T.; Watanabe, K.
Environmental biosafety assessment on transgenic Eucalyptus globulus harboring the choline oxidase (codA) gene in semi-confined condition
Plant Biotechnol.
30
73-76
2013
Arthrobacter globiformis (Q7X2H8)
brenda
Ortega, E.; de Marcos, S.; Sanz-Vicente, I.; Ubide, C.; Ostra, M.; Vidal, M.; Galban, J.
Fluorescence of the flavin group in choline oxidase. Insights and analytical applications for the determination of choline and betaine aldehyde
Talanta
147
253-260
2016
Arthrobacter globiformis (Q7X2H8)
brenda
Gadda, G.; Yuan, H.
Substitutions of S101 decrease proton and hydride transfers in the oxidation of betaine aldehyde by choline oxidase
Arch. Biochem. Biophys.
634
76-82
2017
Arthrobacter globiformis (Q7X2H8)
brenda
Su, D.; Yuan, H.; Gadda, G.
A reversible, charge-induced intramolecular C4a-S-cysteinyl-flavin in choline oxidase variant S101C
Biochemistry
56
6677-6690
2017
Arthrobacter globiformis (Q7X2H8)
brenda
Heath, R.S.; Birmingham, W.R.; Thompson, M.P.; Taglieber, A.; Daviet, L.; Turner, N.J.
An engineered alcohol oxidase for the oxidation of primary alcohols
ChemBioChem
20
276-281
2019
Arthrobacter globiformis (Q7X2H8)
brenda
Li, Y.; Ma, Y.; Li, P.; Zhang, X.; Ribitsch, D.; Alcalde, M.; Hollmann, F.; Wang, Y.
Enantioselective sulfoxidation of thioanisole by cascading a choline oxidase and a peroxygenase in the presence of natural deep eutectic solvents
ChemPlusChem
85
254-257
2020
Glutamicibacter nicotianae (A0A4Y3W1Z2), Glutamicibacter nicotianae
brenda
Magar, H.; Ghica, M.; Abbas, M.; Brett, C.
Highly sensitive choline oxidase enzyme inhibition biosensor for lead ions based on multiwalled carbon nanotube modified glassy carbon electrodes
Electroanalysis
29
1741-1748
2017
Alcaligenes sp. (P16101)
-
brenda
Ouiram, T.; Moonla, C.; Preechaworapun, A.; Muangpil, S.; Maneeprakorn, W.; Tangkuaram, T.
Choline oxidase based composite ZrO2@AuNPs with Cu2O@MnO2 platform for signal enhancing the choline biosensors
Electroanalysis
33
455-463
2021
Alcaligenes sp. (P16101)
-
brenda
Nikzad, N.; Karami, Z.
Label-free colorimetric sensor for sensitive detection of choline based on DNAzyme-choline oxidase coupling
Int. J. Biol. Macromol.
115
1241-1248
2018
Alcaligenes sp. (P16101)
brenda
Su, D.; Smitherman, C.; Gadda, G.
A metastable photoinduced protein-flavin adduct in choline oxidase, an enzyme not involved in light-dependent processes
J. Phys. Chem. B
124
3936-3943
2020
Arthrobacter globiformis (Q7X2H8)
brenda
You, L.; Song, Q.; Wu, Y.; Li, S.; Jiang, C.; Chang, L.; Yang, X.; Zhang, J.
Accumulation of glycine betaine in transplastomic potato plants expressing choline oxidase confers improved drought tolerance
Planta
249
1963-1975
2019
Arthrobacter globiformis (Q7X2H8), Arthrobacter globiformis
brenda
Raldugina, G.; Evsukov, S.; Bogoutdinova, L.; Gulevich, A.; Baranova, E.
Morpho-physiological testing of NaCl sensitivity of tobacco plants overexpressing choline oxidase gene
Plants (Basel)
10
1102
2021
Arthrobacter globiformis (Q7X2H8)
brenda