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
-
electrochemical
-
ache
-
amperometric
-
arthrobacter
-
globiformis
-
glycinebetaine
-
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
-
analysis
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choline-containing
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polypyrrole
-
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
1.1.3.17 choline oxidaseAdvanced search results
results (
results (pH Stability
pH Stability on EC 1.1.3.17 - choline oxidase
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pH STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
additional information
additional information
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at higher pH a transition from alpha-helix to beta-structure occurs while at lower pH the content of alpha-helix structure increases (circular dichroism). Enzyme is more instable at higher pH (melting temperature decreases). At high alkaline pH values the enzyme reveals more accessible hydrophobic patches relative to acidic pH (fluorescence measurement)
697063
additional information
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more rapid inactivation at alkaline than at acidic pH at both 27°C and 37°C. pH-dependent secondary structure changes are analysed
695307
additional information
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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
677058
additional information
prolonged incubation of the inactive enzyme at pH 6 and temperatures above 20°C reveals slow and full recovery of activity over 3 hours, linked to conformational change reverting the enzyme to the native form, rate of approaching steady state independent of concentrations of choline and enzyme, increased to a limiting value with increasing pH
689966
additional information
comparison of pka values of the mutants V464A and V464T
696243
additional information
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comparison of pka values of the mutants V464A and V464T
696243
