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
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1.1.3.17 choline oxidaseAdvanced search results
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results (General Information
General Information on EC 1.1.3.17 - choline oxidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
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replacing Asn510 with alanine or histidine negatively affects both the reductive and oxidative half-reactions catalyzed by choline oxidase. Substitution of Asn510 with alanine, but not with histidine, results in a change from stepwise to concerted mechanisms for the cleavages of the OH and CH bonds of choline catalyzed by the enzyme
metabolism
physiological function
additional information
evolution
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choline oxidases belong to the superfamily of glucose-methanol-choline (GMC) oxidoreductases. The three-dimensional structures of the GMC members are highly conserved while their primary sequences can strongly differ according to their different substrate specificities
evolution
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the enzyme belongs to the glucose-methanol-choline oxidoreductase enzyme superfamily, which shares a highly conserved His-Asn catalytic pair in the active site, Asn510 in the Arthrobacter globiformis enzyme
evolution
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choline oxidases belong to the superfamily of glucose-methanol-choline (GMC) oxidoreductases. The three-dimensional structures of the GMC members are highly conserved while their primary sequences can strongly differ according to their different substrate specificities
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metabolism
in mutant S101C, formation of the C4a-S-cysteinylflavin linkage between the side chain of C101 and the 8alpha-N3-histidyl flavin in the active site is triggered by the binding of protonated Tris in the active site of the enzyme. The C4a-S-cysteinyl-flavin is stabilized between about pH 7.0 and pH 9.5, in which the side chain of C101 is unprotonated and the N5 atom of the C4a-S-cysteinyl-flavin is protonated. The presence of Tris bound at the active site of the enzyme is required to deprotonate the cysteine and to trigger the formation of the C4a-S-cysteinyl-flavin, and for the stabilization of the C4a-S-cysteinyl-flavin
metabolism
observation of an unusual fluorescence excitation spectrum in choline oxidase at alkaline pH. Physiologically, choline oxidase oxidizes choline to betaine through two FAD-associated reactions and is not a photoenzyme. 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. The unusual behavior of the enzyme persists in the mutated S101A enzyme variant but is eliminated in the H466Q variant
physiological function
the reaction catalyzed by choline oxidase is of importance due to the trigger of glycine betaine accumulation in the cytoplasm of a number of plants and pathogenic bacteria in response to hyperosmotic and adverse temperature conditions to prevent dehydration and eventual cell death
physiological function
the choline oxidase gene codA confers salt tolerance to transgenic Eucalyptus globulus
physiological function
expression of CodA in potato plastid genome results in much higher mRNA level of CodA in leaves than in tubers. Glycine betaine accumulates in similar levels in both leaves and tubers of CodA-transplastomic potato plants. The glycine betaine content is moderately increased in transgenic plants, and compartmentation of glycine betaine in plastids confers considerably higher tolerance to drought stress compared to wild-type plants, with higher levels of relative water content and chlorophyll content under drought stress. Transplastomic plants present a significantly higher photosynthetic performance as well as antioxidant enzyme activities during drought stress
physiological function
transgenic Nicotiana tabacum lines with confirmed expression of choline oxidase are characterized by high regeneration capacity from callus in the presence of 200 mM NaCl, partial retention of viability at 400 mM NaCl, correlating with the implicit response of regenerants and whole plants to the effects of salinity. They are less sensitive to the presence of 200 mM NaCl in the cultivation medium, compared to wild-type
additional information
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Asn510 participating in both the reductive and oxidative half-reactions but having a minimal rle in substrate binding
additional information
in the active site of choline oxidase, Glu312 participates in binding the trimethylammonium group of choline, thereby positioning the alcohol substrate properly for efficient hydride transfer to the enzyme-bound flavin. Glu312 is the only negatively charged residue in the active site of the enzyme
additional information
the side chain of Val464 in the active site cavity in choline oxidase provides a nonpolar site that is required to guide oxygen in proximity of the C(4a) atom of the flavin, where it will subsequently react via electrostatic catalysis
additional information
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enzyme structure modeling, overview
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