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IUBMB CommentsA flavoprotein (FAD). In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) . The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in those plants, animals and bacteria that use two separate enzymes.
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betaine aldehyde + O2 + H2O = betaine + H2O2
choline + 2 O2 + H2O = betaine + 2 H2O2
choline + O2 = betaine aldehyde + H2O2
betaine aldehyde + O2 + H2O = betaine + H2O2
-
-
-
-
betaine aldehyde + O2 + H2O = betaine + H2O2
His466 is a catalytic residue involved in the oxidation but not the reduction, reaction mechanism
-
betaine aldehyde + O2 + H2O = betaine + H2O2
reaction mechanism, the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps
-
choline + 2 O2 + H2O = betaine + 2 H2O2
overall reaction
-
-
-
choline + 2 O2 + H2O = betaine + 2 H2O2
two-step, four-electron oxidation (alcohol oxidation, aldehyd hydration, aldehyde oxidation)
choline + 2 O2 + H2O = betaine + 2 H2O2
reaction mechanism of reductive and oxidative half-reactions, determination of a mechanism of flavin oxidation that directly results in the formation of oxidized flavin and hydrogen peroxide without stabilization of reaction intermediates, overview
-
choline + 2 O2 + H2O = betaine + 2 H2O2
reaction mechanism of reductive and oxidative half-reactions, determination of a mechanism of flavin oxidation that directly results in the formation of oxidized flavin and hydrogen peroxide without stabilization of reaction intermediates, overview
-
-
choline + O2 = betaine aldehyde + H2O2
-
-
-
-
choline + O2 = betaine aldehyde + H2O2
choline hydroxyl proton is not in flight in the transition state for CH bond cleavage, steps of flavin reduction by choline and betaine aldehyde is rate rate limiting for the overall turnover
-
choline + O2 = betaine aldehyde + H2O2
mechanism, carbon-hydrogen bond cleavage of choline is nearly irreversible and fully rate-limiting at low pH
-
choline + O2 = betaine aldehyde + H2O2
sequential mechanism with oxygen reacting with the reduced enzyme before release of the betaine-aldede or glycine-betaine, kinetic step in the oxidation of choline to the ladehyde is partially rate-limiting
-
choline + O2 = betaine aldehyde + H2O2
His466 is a catalytic residue involved in the oxidation but not the reduction, reaction mechanism
-
choline + O2 = betaine aldehyde + H2O2
reaction mechanism via FAD, the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps, hydride transfer and oxygen radical mechanisms, overview
-
choline + O2 = betaine aldehyde + H2O2
reaction mechanism via FAD, the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps, the enzyme correlates reversible hydride transfer with environmentally enhanced tunneling, oxygen- and temperature-dependent kinetic isotope effects, overview
-
choline + O2 = betaine aldehyde + H2O2
reaction mechanism, the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps
-
choline + O2 = betaine aldehyde + H2O2
reaction mechanism, the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps, His466 is a catalytic residue involved in flavin-binding
-
choline + O2 = betaine aldehyde + H2O2
steady state kinetic mechanism, the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps, detailed reaction mechanism
-
choline + O2 = betaine aldehyde + H2O2
the catalytic reaction involves an active site His residue and a Ser residue in proximity to the active site
-
choline + O2 = betaine aldehyde + H2O2
the enzyme catalyzes the oxidation of choline to glycine betaine via the intermediate betaine aldehyde
-
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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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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
FADH2 + O2
FAD + H2O2
-
-
-
-
?
glycine betaine + H2O2
betaine aldehyde + O2 + H2O
-
-
-
-
?
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
-
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 + 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
-
-
389716, 389718, 389719, 389720, 389721, 389723, 389724, 389727, 654773, 671605, 672136 -
-
?
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
-
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
-
-
-
-
?
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
-
-
-
-
?
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
?
-
-
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
-
-
?
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FMN
the enzyme-bound flavin shows a progressive shift of the fluorescence excitation maximum (lambdaex) from 468 to 399 nm with increasing pH value between pH 6.0 and 10.0, consistent with a metastable photoinduced protein-flavin adduct. In contrast, the maximal lambdaem is independent of pH, with values of about 526 nm
FAD
-
-
FAD
-
8alpha substituted flavin covalently linked to N1 of H87
FAD
one moiety per enzyme monomer, covalently bound
FAD
-
covalently bound to the enzyme, complete reduction of the enzyme-bound flavin is observed in a stopped-flow spectrophotometer upon anaerobic mixing with betaine aldehyde or choline at pH 8.0, with similar kred values
FAD
-
covalently bound to the enzyme, spectral analysis of denatured wild-type and mutant enzymes, overview
FAD
-
dependent on, covalently bound to the enzyme
FAD
-
dependent on, covalently bound to the enzyme, involving His466, in an 1:1 stoichiometry, spectrometrical analysis, effects of pH, mutant enzyme H466D shows a 0.29:1 stoichiometry, overview, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutants H466D and H466A
FAD
-
dependent on, enzyme bound
FAD
covalent binding of FAD to purified proteins ascertained, rates of flavin reduction determined in wild-type and mutant variants
FAD
groups responsible for the change in the protein conformation are not likely to be in the enzyme active site, direct effect on the microenvironment of the enzyme-bound flavin and activity of the enzyme
FAD
His351 stabilizes transition state for hydride transfer reaction to flavin, is not involved in the activation of the reduced flavin for reaction with oxygen
FAD
covalently bound in both mutants (V464A and V464T)
FAD
-
Ala21 is part of an alpha-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme
FAD
required for catalysis, covalently bound to the Nepsilon2 atom of His99 of the wild-type enzyme
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1.1.3.17 choline oxidase
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