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
-
acetylcholine
-
electrode
-
acetylcholinesterase
-
biosensors
-
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
-
electrodeposited
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co-crosslinking
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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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Specific Activity
Specific Activity on EC 1.1.3.17 - choline oxidase
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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
biosensor using choline oxidase entrapped within polyacrylamide microparticles, microgel analysis by Scanning electron microscopy, Galai-Cis particle analyzer, X-ray diffraction and differential scanning calorimetry, influence of the polymer cross-linking content, potential, pH and temperature the biosensor response investigated, design of a bienzyme biosensor by including acetylcholinesterase
additional information
inhibition bienzymatic (butyrylcholinesterase and choline oxidase) organic phase enzyme electrode analyzed, comparison to a tyrosinase inhibition organic phase enzyme electrode operating in water-saturated chloroform medium, analytical data for measurements of organophosphorus pesticides
additional information
sensor consisting of Clark-type dissolved oxygen electrode and choline oxidase immobilized membrane, choline concentration measured by the oxygen consumption induced by an enzyme reaction of choline oxidase, calibration curves for choline in the liquid and gas phases, response time for choline vapour 15% slower than that of biosensor for choline solution
additional information
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pH-dependent catalytic efficiency, overview
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
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activity measurement in a coupled assay with NAD+-dependent betaine aldehyde dehydrogenase, BADH
additional information
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transgenic plants under the control of the stress-inducible SWPA2 promoter generated, RT-PCR analysis under stress-inducing conditions, glycine betaine accumulation, oxidative stress tolerance, salt stress tolerance and drought stress tolerance of transgenic plants