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
-
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
-
amperometric
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arthrobacter
-
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
-
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
-
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
1.1.3.17 choline oxidaseAdvanced search results
results (
results (KM Value
KM Value on EC 1.1.3.17 - choline oxidase
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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
-
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
0.6
choline
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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
0.7
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
1.7 - 1.8
choline
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enzyme immobilized in polyethylenimine-coated silica-monolith, apparent value, pH and temperature not specified in the publication
2.1
choline
-
free enzyme, apparent value, pH and temperature not specified in the publication
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
additional information
additional information
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stopped-flow kinetics
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additional information
additional information
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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
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additional information
additional information
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kinetics and thermodynamics, steady state kinetic mechanism
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additional information
additional information
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kinetics, recombinant enzyme, NMR-determination of hydration ratio of betaine aldehyde, overview
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additional information
additional information
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kinetics, recombinant enzyme, overview
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additional information
additional information
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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
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additional information
additional information
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steady-state kinetics of wild-type and mutant enzymes at different pH and in presence or absence of imidazole, kinetic isotope effects
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additional information
additional information
similar level of catalytic activity than free enzyme in solution
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additional information
additional information
analysis of steady-state kinetic mechanism, activation of alcohol substrate, hydride ion transfer
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additional information
additional information
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analysis of steady-state kinetic mechanism, activation of alcohol substrate, hydride ion transfer
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additional information
additional information
analysis of substrate kinetic isotope effects
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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
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additional information
additional information
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steady-state kinetics, isotopic effects, detailed overview
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additional information
additional information
stopped-flow and steady-state kinetics, and sequential steady-state kinetic mechanism, overview
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additional information
additional information
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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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