Any feedback?
Information on EC 1.1.3.17 - choline oxidase and Organism(s) Arthrobacter globiformis and UniProt Accession Q7X2H8
for references in articles please use BRENDA:EC1.1.3.17Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.3.17 choline oxidaseIUBMB Comments
A 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.
Specify your search results
Word Map
- 1.1.3.17
- acetylcholine
-
electrode
- acetylcholinesterase
-
biosensors
- betaine
-
electrochemical
-
ache
-
amperometric
- arthrobacter
- globiformis
- glycinebetaine
-
organophosphorus
-
co-immobilized
- luminol
-
post-column
-
screen-printed
-
prussian
-
electropolymerized
- butyrylcholine
- 4-aminoantipyrine
-
bienzymatic
-
four-electron
- analysis
-
choline-containing
-
polypyrrole
-
alkoxide
-
3.1.1.8
-
nafion
-
enzyme-modified
-
electrodeposited
-
co-crosslinking
- agriculture
- synthesis
- nutrition
- biotechnology
The taxonomic range for the selected organisms is: Arthrobacter globiformis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
+
=
+
Synonyms
choline oxidase, an_coda, apcho-syn, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 + 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
-
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
choline:oxygen 1-oxidoreductase
A 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) [6]. 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.
CAS REGISTRY NUMBER
COMMENTARY
9028-67-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
betaine aldehyde + O2 + H2O
glycine betaine + H2O2
-
-
-
?
3,3-dimethylbutan-1-ol + O2
?
-
10fold lower activity compared to choline
-
-
?
FADH2 + O2
FAD + H2O2
-
-
-
-
?
N,N-dimethylaminoethanol + O2
(dimethylamino)acetaldehyde + H2O2
-
-
-
-
?
N,N-dimethylethanolamine + O2
N,N-dimethylethanalamine + 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 + O2
betaine aldehyde + H2O2
-
-
-
?
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
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
-
-
-
?
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
-
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
-
-
?
additional information
?
-
poor substrate for wild-type, but substrate for mutants is 1-hexanol, reaction of EC 1.1.3.13
-
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
betaine aldehyde + O2 + H2O
glycine betaine + H2O2
-
-
-
?
betaine aldehyde + O2 + H2O
betaine + H2O2
-
-
-
-
?
FADH2 + O2
FAD + 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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
required for catalysis, covalently bound to the Nepsilon2 atom of His99 of the wild-type enzyme
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, 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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycine betaine
pH dependence of the kcat and kcat/Km values for glycine betaine inhibition shown, inhibition of H351A enzyme maximal at low pH and reduced with increasing pH
3,3-dimethylbutyraldehyde
-
product analogue inhibition, 74-90% reduced flavin reduction dependent on pH
additional information
-
low pH induces a localized and reversible conformational change that is associated with the complete and reversible loss of catalytic activity
-
glycine betaine
-
binds to the active site, different binding of wild-type and mutant enzymes, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.5
choline
previously stored at pH 6 and 0°C, measured at pH 7 and 25°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
0.7
choline
previously stored at pH 6 and -20°C, measured at pH 7 and 25°C
4.7
choline
mutant S101A/D250G/F253R/V355T/F357R/M359R, 30°C, pH 8
0.6
O2
wild type enzyme, in 50 mM potassium phosphate (pH 7.0), at 25°C
67
O2
mutant enzyme H351Q, in 50 mM potassium phosphate (pH 7.0), at 25°C
0.5
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, 0°C
0.6
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 8.0, at -20°C or 0°C
0.7
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, -20°C
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
stopped-flow and steady-state kinetics, and sequential steady-state kinetic mechanism, overview
-
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
-
steady-state kinetics, isotopic effects, detailed 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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
overall turnover of mutant variant about 60-fold decreased with choline compared to wild-type enzyme
-
43
Betaine aldehyde
mutant enzyme S101A, in 50 mM sodium diphosphate, pH 10.0, at 25°C
133
Betaine aldehyde
wild type enzyme, in 50 mM sodium diphosphate, pH 10.0, at 25°C
0.02
choline
mutant S101A/D250G/F253R/V355T/F357R/M359R, 30°C, pH 8
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
1.86
choline
H99N mutant, substrate choline, pH 7, 25°C. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system
4.4
choline
previously stored at pH 6 and -20°C, measured at pH 7 and 25°C
6.7
choline
mutant enzyme S101A, in 50 mM sodium diphosphate, pH 10.0, at 25°C
13.3
choline
previously stored at pH 6 and 0°C, measured at pH 7 and 25°C
14.9
choline
previously stored at pH 8 and 0°C, measured at pH 7 and 25°C
15.5
choline
previously stored at pH 8 and -20°C, measured at pH 7 and 25°C
60
choline
wild type enzyme, in 50 mM sodium diphosphate, pH 10.0, at 25°C
0.33
O2
mutant enzyme H351Q, in 50 mM potassium phosphate (pH 7.0), at 25°C
15
O2
wild type enzyme, in 50 mM potassium phosphate (pH 7.0), at 25°C
4.4
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, -20°C
13.3
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, 0°C
14.9
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 8.0, -20°C
15.5
choline
-
pH 7.0, 25°C, recombinant enzyme stored at pH 8.0, 0°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kcat/Koxygen values are independent of the pH between pH 5.0 and 10.0, average value is 1.7 mM
-
0.005
choline
mutant S101A/D250G/F253R/V355T/F357R/M359R, 30°C, pH 8
25.6
choline
mutant enzyme S101A, in 50 mM sodium diphosphate, pH 10.0, at 25°C
237
choline
wild type enzyme, in 50 mM sodium diphosphate, pH 10.0, at 25°C
0.0049
O2
mutant enzyme H351Q, in 50 mM potassium phosphate (pH 7.0), at 25°C
25
O2
wild type enzyme, in 50 mM potassium phosphate (pH 7.0), at 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.08
H99N mutant, substrate choline, pH 7, 25°C. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system
0.09
mutant S101A/D250G/F253R/V355T/F357R/M359R, substrate choline, 30°C, pH 8
0.28
apparent, H99N mutant, substrate choline, pH 7, 25°C. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system
0.3
additional information
additional information
comparison of thermodynamic and kinetic parameters of the hydride transfer reaction under reversible and irreversible catalytic regimes, significantly larger enthalpies of activation in the reversible catalytic regime, first example of the use of temperature-dependent kinetic isotope effects to measure thermodynamic parameters for hydride ion tunneling associated with the presence of conformational changes occurring in the enzyme-substrate complex
additional information
pH dependence of substrate deuterium isotope effects and of the kcat and kcat/Km values for choline in the mutant variant H351A determined, steady-state kinetic parameters compared between H351A mutant and wild-type, His351 important but not essential for the reductive half-reaction of choline oxidation, contributes to substrate binding and to the overall polarity of the active site
additional information
temperature effects on the apparent rate constant for slow transition from inactive to active form, pH effects on the hysteretic behavior, effect of storage pH and temperature on activity
additional information
X-ray data collection and mutant analysis, steady-state kinetic parameters, pH profiles, substrate kinetic isotope effects for mutants and wild-type determined
additional information
-
pH-dependent catalytic efficiency, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
10
activity assay at, in 50 mM sodium pyrophosphate, neutral hydroquinone species of the flavin stabilized in the H351A enzyme at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
6
4°C, the anionic flavosemiquinone is slowly oxidized under aerobic conditions
6 - 8
H99N mutant, lower KM compared to pH 8-11. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system
6.5 - 9.6
pH effects on the rate constants for fast transition from inactive to active form measured, choline concentrations in the range from 0.1 to 10 mM, temperature effects on enzyme reactivation determined at pH 6
8
the anionic flavosemiquinone of choline oxidase is unusually insensitive to both molecular oxygen and artificial electron acceptors
8 - 11
H99N mutant, no impact on KM, highest KM. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system
6 - 10
6.5 - 9.6
-
low pH induces a localized and reversible conformational change that is associated with the complete and reversible loss of catalytic activity, overview
additional information
5 - 10
determined at 10, 25 and 40°C, 50 mM sodium pyrophosphate, potassium phosphate used for pH 7 and 7.5, measured at a fixed concentration of 0.2 mM oxygen and of 0.25 mM oxygen for the data at 25°C
5 - 10
pH profiles of kinetic parameters with choline as a substrate
5 - 10
varying concentrations of both choline and oxygen, between pH 7 and pH 10, Km values for oxygen less than 15 microM
6 - 10
-
kcat/Kox with choline or 1,2-[2H4]choline as a substrate for choline oxidase is independent of pH between pH 6.0 and pH 10.0
additional information
-
pH profile of the reaction catalyzed at different conditions, recombinant enzyme, overview
additional information
-
pH-dependent catalytic efficiency, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
25
-
assay at
25
time courses of oxygen consumption and enzymatic activity, incubation of the inactive enzyme at 25°C above pH 6.5 reveals fast and partial reactivation, slow onset of steady state during enzymatic turnover
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 45
monitoring initial rates of oxygen consumption with oxygen electrode thermostated at, 0.2 mM oxygen in 50 mM sodium pyrophosphate, pH 8
20 - 39
effect of temperature on the rate of reactivation at pH 6
additional information
additional information
analysis of temperature effect on rate constant for flavin reduction
additional information
-
temperature profile of the reaction catalyzed at different conditions, recombinant enzyme, overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
evolution
-
the enzyme belongs to the glucose-methanol-choline oxidoreductase enzyme superfamily, which shares a highly conserved His-Asn catalytic pair in the active site, Asn510 in the Arthrobacter globiformis enzyme
malfunction
-
replacing Asn510 with alanine or histidine negatively affects both the reductive and oxidative half-reactions catalyzed by choline oxidase. 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
metabolism
in mutant S101C, formation of the C4a-S-cysteinylflavin linkage between the side chain of C101 and the 8alpha-N3-histidyl flavin in the active site is triggered by the binding of protonated Tris in the active site of the enzyme. The C4a-S-cysteinyl-flavin is stabilized between about pH 7.0 and pH 9.5, in which the side chain of C101 is unprotonated and the N5 atom of the C4a-S-cysteinyl-flavin is protonated. The presence of Tris bound at the active site of the enzyme is required to deprotonate the cysteine and to trigger the formation of the C4a-S-cysteinyl-flavin, and for the stabilization of the C4a-S-cysteinyl-flavin
metabolism
observation of an unusual fluorescence excitation spectrum in choline oxidase at alkaline pH. Physiologically, choline oxidase oxidizes choline to betaine through two FAD-associated reactions and is not a photoenzyme. 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. The unusual behavior of the enzyme persists in the mutated S101A enzyme variant but is eliminated in the H466Q variant
physiological function
the reaction catalyzed by choline oxidase is of importance due to the trigger of glycine betaine accumulation in the cytoplasm of a number of plants and pathogenic bacteria in response to hyperosmotic and adverse temperature conditions to prevent dehydration and eventual cell death
physiological function
the choline oxidase gene codA confers salt tolerance to transgenic Eucalyptus globulus
physiological function
expression of CodA in potato plastid genome results in much higher mRNA level of CodA in leaves than in tubers. Glycine betaine accumulates in similar levels in both leaves and tubers of CodA-transplastomic potato plants. The glycine betaine content is moderately increased in transgenic plants, and compartmentation of glycine betaine in plastids confers considerably higher tolerance to drought stress compared to wild-type plants, with higher levels of relative water content and chlorophyll content under drought stress. Transplastomic plants present a significantly higher photosynthetic performance as well as antioxidant enzyme activities during drought stress
physiological function
transgenic Nicotiana tabacum lines with confirmed expression of choline oxidase are characterized by high regeneration capacity from callus in the presence of 200 mM NaCl, partial retention of viability at 400 mM NaCl, correlating with the implicit response of regenerants and whole plants to the effects of salinity. They are less sensitive to the presence of 200 mM NaCl in the cultivation medium, compared to wild-type
additional information
in the active site of choline oxidase, Glu312 participates in binding the trimethylammonium group of choline, thereby positioning the alcohol substrate properly for efficient hydride transfer to the enzyme-bound flavin. Glu312 is the only negatively charged residue in the active site of the enzyme
additional information
the side chain of Val464 in the active site cavity in choline oxidase provides a nonpolar site that is required to guide oxygen in proximity of the C(4a) atom of the flavin, where it will subsequently react via electrostatic catalysis
additional information
-
Asn510 participating in both the reductive and oxidative half-reactions but having a minimal rle in substrate binding
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60612
2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence
60614
2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
active site of wild-type choline oxidase, resolution of 1.86 A
crystal structure determined by synchrotron X-ray radiation, refined to a resolution of 1.86 A, data collected at 100 K
hanging drop vapor diffusion method, 1.2-1.8 M ammonium sulfate and 10% (v/v) DMSO in 0.1 M Bis-Tris propane (pH 8.5), flash-frozen in liquid nitrogen. Analysis of the flavin C4a-oxygen adduct in choline oxidase
in complex with glycine betaine, hanging drop vapor diffusion method, using 0.1 M magnesium acetate pH 6.0, 50 mM calcium chloride, 2.5% (v/v) glycerol, 10% (w/v) PEG 6000
mutant enzyme S101A, hanging drop vapor diffusion method, using 80 mM sodium cacodylate, 20% (v/v) PEG6000, 20% (v/v) glycerol, 150 mM Mg-acetate at pH 6.0
purified recombinnat wild-type enzyme and mutant V464A, hanging drop vapor diffusion, room temperature, from 10-15% v/v PEG 6000, 50-200 mM magnesium acetate, 200 mM trimethylamine, and 0.08 M sodium cacodylate, pH 6.0, X-ray diffraction structure determination and analysis at 2.2 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E312A
generated for investigation of the negative charge on Glu312, enzyme inactive
E312D
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
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
H466Q
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
S101A
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
S101C
S101T
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
V464A
V464T
H466A
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
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
additional information
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
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
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
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
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
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
prolonged incubation of the inactive enzyme at pH 6 and temperatures above 20°C reveals slow and full recovery of activity over 3 hours, linked to conformational change reverting the enzyme to the native form, rate of approaching steady state independent of concentrations of choline and enzyme, increased to a limiting value with increasing pH
689966
additional information
comparison of pka values of the mutants V464A and V464T
696243
additional information
-
comparison of pka values of the mutants V464A and V464T
696243
additional information
-
low pH induces a localized and reversible conformational change that is associated with the complete and reversible loss of catalytic activity
677058
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
mutant S101A/V355T/F357R/M359R, 3 h, 10% residual activity. Mutant S101A/D250G/F253R/V355T/F357R/M359R, 3 h, almost 50% residual activity
52
metling temperature of mutant S101A/D250G/F253R/V355T/F357R/M359R
additional information
additional information
freezing at low pH leads to reversible conformational change, associated with complete and reversible loss of catalytic activity
additional information
-
temperature dependence of rate constants of the E312D mutant is analysed, substrate choline
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
storage at -20°C and pH 6 results in a change in the conformation, loss of catalytic activity at pH 6, reactivation of the enzyme slow at pH 6 and temperatures between 20 and 39°C, facilitated by elevated pH values at 25°C and pH above 6.5
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
storage at pH 6 and -20°C results in a change of conformation of the enzyme, which is associated with complete loss of catalytic activity when the enzyme is assayed at pH 6.0
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified with the bound flavin cofactor in the fully oxidized state
recombinant wild-type and mutants from Escherichia coli strain Rosetta(DE3)pLysS
wild-type and mutant protein, purified enzymes have 50-70% of the enzyme-bound flavin cofactor as an air-stable anionic flavosemiquinone, converts slowly to oxidized state by extensive dialysis at pH 6 and 4°C
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta(DE3)pLysS cells
expressed in Escherichia coli, strain Rosetta(DE3)pLysS, pET/codAmg plasmid, wild-type and Glu312 variants generated by site-directed mutagenesis
expressed in Escherichia coli, wild-type and H351A variant, plasmid pET/codAmg1-H351A
expression of wild-type and mutants in Escherichia coli strain Rosetta(DE3)pLysS
mutant enzyme S101A is expressed in Escherichia coli Rosetta(DE3)pLysS cells
recombinant expression in Escherichia coli strain Rosetta (DE3)pLysS
Arabidopsis thaliana transformed with codA gene from Arthrobacter globiformis which encodes choline oxidase
-
Balb/c mice used for toxicity studies of choline oxidase - no significant difference from control in terms of growth, body weight, food consumption, and blood biochemical indices. Analysis of various tissues show no significant effect
-
codA gene introduced into Synecochoccus sp. PCC 7942 and Arabidopsis thaliana leads to accumulation of glycinebetaine and enhanced tolerance to salt and cold stress, rice Oryza sativa L. genetically engineered, Agrobacterium-mediated transformation, ability to synthesize glycinebetaine is established by introducing the codA gene for choline oxidase from Arthrobacter globiformis
-
expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)pLysS
-
gene codA, expression in Euccalyptus globulus via Agrobaccterium tumefaciens strain EHA105 transfection method using vectors pBI121 and pGW23codA
-
recombinant expression in Escherichia coli strain Rosetta (DE3)pLysS
-
expressed in Escherichia coli Rosetta(DE3)pLysS cells
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
conformational change reverting the enzyme to the native form, rate of approaching steady state independent of concentrations of choline and enzyme, increased to a limiting value with increasing pH
fully oxidized form of the enzyme is obtained via slow oxidation of the flavosemiquinone by extensive dialysis at pH 6 and 4°C
incubation of the inactive enzyme at pH values of pH 6.5 and above, and 25°C results in a fast and partial reactivation of the enzyme, which occurrs with slow onset of steady state during enzymatic turnover, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
expression of CodA in potato plastid genome results in much higher mRNA level of CodA in leaves than in tubers. Glycine betaine accumulates in similar levels in both leaves and tubers of CodA-transplastomic potato plants. The glycine betaine content is moderately increased in transgenic plants, and compartmentation of glycine betaine in plastids confers considerably higher tolerance to drought stress compared to wild-type plants, with higher levels of relative water content and chlorophyll content under drought stress. Transplastomic plants present a significantly higher photosynthetic performance as well as antioxidant enzyme activities during drought stress
agriculture
analysis
-
the immobilized enzyme is used in amperometric biosensors for choline detection, method evaluation
biotechnology
-
the immobilized enzyme is used in amperometric biosensors
nutrition
-
introducing of the codA gene into a cereal crop allows the biosynthesis of glycinebetaine
additional information
-
enzyme is of both biotechnological and medical interest, since glycine betaine can be accumulated in the cytoplasm of cells to prevent dehydration and plasmolysis in adverse hyperosmotic environments in pathogenic bacteria
agriculture
-
transformation enables the plants to accumulate glycinebetaine in chloroplasts and significantly enhances the freezing tolerance of plants
agriculture
-
introducing of the codA gene into a cereal crop allows the biosynthesis of glycinebetaine by transgenic plants without any need for an exogenous supply of choline or glycinebetaine aldehyde
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ikuta, S.; Imamura, S.; Misaki, H.; Horiuti, Y.
Purification and characterization of choline oxidase from Arthrobacter globiformis
J. Biochem.
82
1741-1749
1977
Arthrobacter globiformis
Ohishi, N.; Yagi, K.
Covalently bound flavin and prosthetic group of choline oxidase
Biochem. Biophys. Res. Commun.
86
1084-1088
1979
Arthrobacter globiformis
Yamada, H.; Mori, N.; Tani, Y.
Properties of choline oxidase of cylindrocarpon didymum M-1
Agric. Biol. Chem.
43
2173-2177
1979
Arthrobacter globiformis, Cylindrocarpon didymum, Cylindrocarpon didymum M-1
-
Ohta-Fukuyama, M.; Miyake, Y.; Emi, S.; Yamano, T.
Identification and properties of the prosthetic group of choline oxidase from Alcaligenes sp.
J. Biochem.
88
197-203
1980
Alcaligenes sp., Arthrobacter globiformis
Mori, N.; Tani, Y.; Yamada, H.; Hayashi, R.
Covalently bound flavin as prosthetic group of choline oxidase
Agric. Biol. Chem.
45
539-540
1981
Alcaligenes sp., Arthrobacter globiformis, Cylindrocarpon didymum, Cylindrocarpon didymum M-1
-
Pocard, J.A.; Vincent, N.; Boncompagni, E.; Tombras Smith, L.; Poggi, M.C.; Le Rudulier, D.
Molecular characterization of the bet genes encoding glycine betaine synthesis in Sinorhizobium meliloti 102F34
Microbiology
143
1369-1379
1997
Arthrobacter globiformis, Arthrobacter pascens, Cylindrocarpon didymum, Sinorhizobium meliloti, Sinorhizobium meliloti 102F34, Cylindrocarpon didymum M-1
Sakamoto, A.; Alia; Murata, N.
Metabolic engineering of rice leading to biosynthesis of glycinebetaine and tolerance to salt and cold
Plant Mol. Biol.
38
1011-1019
1998
Arthrobacter globiformis
Sakamoto, A.; Valverde, R.; Alia; Chen, T.H.H.; Murata, N.
Transformation of Arabidopsis with the codA gene for choline oxidase enhances freezing tolerance of plants
Plant J.
22
449-453
2000
Arthrobacter globiformis
Fan, F.; Ghanem, M.; Gadda, G.
Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance
Arch. Biochem. Biophys.
421
149-158
2004
Arthrobacter globiformis (Q7X2H8), Arthrobacter globiformis
Gadda, G.; Powell, N.L.; Menon, P.
The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase
Arch. Biochem. Biophys.
430
264-273
2004
Arthrobacter globiformis
Rand, T.; Halkier, T.; Hansen, O.C.
Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis
Biochemistry
42
7188-7194
2003
Arthrobacter globiformis
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
Gadda, G.
Kinetic mechanism of choline oxidase from Arthrobacter globiformis
Biochim. Biophys. Acta
1646
112-118
2003
Arthrobacter globiformis
Gadda, G.
pH and deuterium kinetic isotope effects studies on the oxidation of choline to betaine-aldehyde catalyzed by choline oxidase
Biochim. Biophys. Acta
1650
4-9
2003
Arthrobacter globiformis
Fan, F.; Gadda, G.
On the catalytic mechanism of choline oxidase
J. Am. Chem. Soc.
127
2067-2074
2005
Arthrobacter globiformis
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
182-187
2006
Arthrobacter globiformis
Fan, F.; Germann, M.W.; Gadda, G.
Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3,3-dimethylbutyraldehyde
Biochemistry
45
1979-1986
2006
Arthrobacter globiformis
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
3437-3447
2006
Arthrobacter globiformis
Fan, F.; Gadda, G.
Oxygen- and temperature-dependent kinetic isotope effects in choline oxidase: correlating reversible hydride transfer with environmentally enhanced tunneling
J. Am. Chem. Soc.
127
17954-17961
2005
Arthrobacter globiformis
Hoang, J.V.; Gadda, G.
Trapping choline oxidase in a nonfunctional conformation by freezing at low pH
Proteins
66
611-620
2007
Arthrobacter globiformis
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
852-858
2006
Arthrobacter globiformis
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)
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)
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)
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)
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
10-14
2009
Arthrobacter globiformis
Gadda, G.
Hydride transfer made easy in the reaction of alcohol oxidation catalyzed by flavin-dependent oxidases
Biochemistry
47
13745-13753
2008
Arthrobacter globiformis (Q7X2H8), Arthrobacter globiformis
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
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
720-728
2009
Arthrobacter globiformis (Q7X2H8)
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
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)
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)
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)
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
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)
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
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
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
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)
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
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)
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)
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)
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)
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)
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)
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)
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
EXTERNAL LINKS (specific for EC-Number 1.1.3.17)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
