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
-
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
- 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
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results (Cofactor
Cofactor on EC 1.1.3.17 - choline oxidase
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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
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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
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covalently bound to the enzyme, spectral analysis of denatured wild-type and mutant enzymes, overview
FAD
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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
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
-
Ala21 is part of an alpha-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme
FAD
required for catalysis, covalently bound to the Nepsilon2 atom of His99 of the wild-type enzyme
