1.1.3.17: choline oxidase
This is an abbreviated version!
For detailed information about choline oxidase, go to the full flat file.
Word Map on EC 1.1.3.17
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1.1.3.17
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acetylcholine
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electrode
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acetylcholinesterase
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biosensors
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betaine
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electrochemical
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ache
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amperometric
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arthrobacter
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globiformis
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glycinebetaine
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organophosphorus
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co-immobilized
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luminol
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post-column
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screen-printed
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prussian
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electropolymerized
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butyrylcholine
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4-aminoantipyrine
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bienzymatic
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four-electron
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analysis
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choline-containing
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polypyrrole
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alkoxide
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3.1.1.8
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nafion
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enzyme-modified
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electrodeposited
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co-crosslinking
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agriculture
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synthesis
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nutrition
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biotechnology
- 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
Reaction
Synonyms
alkaliphilic choline oxidase, ANI01nite_22550, An_CodA, APChO-syn, CHO, choline oxidase, choline-oxygen 1-oxidoreductase, choline:oxygen 1-reductase, ChOx, ChOx protein, codA, COX
ECTree
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Substrates Products
Substrates Products on EC 1.1.3.17 - choline oxidase
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REACTION DIAGRAM
3,3-dimethylbutan-1-ol + O2
?
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10fold lower activity compared to choline
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-
?
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
glycine betaine + H2O2
-
-
-
?
FADH2 + O2
FAD + H2O2
-
-
-
-
?
N,N-dimethylethanolamine + O2
N,N-dimethylethanalamine + H2O2
-
-
-
-
?
betaine aldehyde + O2 + H2O
betaine + 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
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-
?
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
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-
?
choline + O2
betaine aldehyde + H2O2
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-
-
-
?
choline + O2
betaine aldehyde + H2O2
choline detection by mono- and bienzyme biosensors
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-
?
choline + O2
betaine aldehyde + H2O2
choline oxidase as part of a bienzymatic organic phase enzyme electrode analyzed
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-
?
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
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-
?
choline + O2
betaine aldehyde + H2O2
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-
389716, 389718, 389719, 389720, 389721, 389723, 389724, 389727, 654371, 654773, 654860, 655800, 671605, 672121, 672136, 695885
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-
?
choline + O2
betaine aldehyde + H2O2
-
-
-
?
choline + O2
betaine aldehyde + H2O2
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FAD-linked reaction
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-
?
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
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-
?
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
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-
?
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
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-
?
choline + O2
betaine aldehyde + H2O2
spatial location of the negative charge on residue 312 important for oxidation of alcohol substrate
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-
?
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
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-
?
(dimethylamino)acetaldehyde + H2O2
-
-
-
-
?
N,N-dimethylaminoethanol + O2
(dimethylamino)acetaldehyde + H2O2
-
-
-
-
?
N,N-dimethylaminoethanol + O2
(dimethylamino)acetaldehyde + H2O2
-
-
-
-
?
? + 2 H2O2
-
-
-
-
?
tris-(2-hydroxyethyl)-methylammonium methylsulfate + 2 O2 + H2O2
? + 2 H2O2
-
-
-
-
?
?
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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
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-
?
additional information
?
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poor substrate for wild-type, but substrate for mutants is 1-hexanol, reaction of EC 1.1.3.13
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-
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additional information
?
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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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-
?
additional information
?
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no activity with betaine, monoethanolamine, triethanolamine, dimethylamino-1-butanol, N,N-dimethylglycine methylester, beta-methylcholine, L-carnitine, propanol, ethanol, and methanol
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-
?
additional information
?
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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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-
?
additional information
?
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no activity with betaine, monoethanolamine, triethanolamine, dimethylamino-1-butanol, N,N-dimethylglycine methylester, beta-methylcholine, L-carnitine, propanol, ethanol, and methanol
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-
?
additional information
?
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Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate
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-
?
additional information
?
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Phe351 is positioned right in the active site of An_CodA and very likely interacts with the bound substrate
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-
?