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
-
acetylcholinesterase
-
biosensors
-
betaine
-
electrochemical
-
ache
-
amperometric
-
arthrobacter
-
globiformis
-
glycinebetaine
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organophosphorus
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co-immobilized
-
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
-
electrodeposited
-
co-crosslinking
-
agriculture
-
synthesis
-
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
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pH Range
pH Range on EC 1.1.3.17 - choline oxidase
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5 - 10
6
4°C, the anionic flavosemiquinone is slowly oxidized under aerobic conditions
6 - 10
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
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
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
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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
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low pH induces a localized and reversible conformational change that is associated with the complete and reversible loss of catalytic activity, overview
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
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pH profile of the reaction catalyzed at different conditions, recombinant enzyme, overview
additional information
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pH-dependent catalytic efficiency, overview