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Literature summary for 1.1.3.17 extracted from

  • Gadda, G.
    Hydride transfer made easy in the reaction of alcohol oxidation catalyzed by flavin-dependent oxidases (2008), Biochemistry, 47, 13745-13753.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
anaylsis of biophysical properties of choline oxidase Arthrobacter globiformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information analysis of steady-state kinetic mechanism, activation of alcohol substrate, hydride ion transfer Arthrobacter globiformis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000
-
homodimer mass Arthrobacter globiformis

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis Q7X2H8
-
-

Reaction

Reaction Comment Organism Reaction ID
choline + 2 O2 + H2O = betaine + 2 H2O2 two-step, four-electron oxidation (alcohol oxidation, aldehyd hydration, aldehyde oxidation) Arthrobacter globiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
choline + O2
-
Arthrobacter globiformis betaine aldehyde + H2O2
-
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Subunits

Subunits Comment Organism
homodimer each subunit covalently linked to FAD Arthrobacter globiformis

Synonyms

Synonyms Comment Organism
choline oxidase
-
Arthrobacter globiformis
choline-oxygen 1-oxidoreductase
-
Arthrobacter globiformis

pH Range

pH Minimum pH Maximum Comment Organism
6
-
4°C, the anionic flavosemiquinone is slowly oxidized under aerobic conditions Arthrobacter globiformis
8
-
the anionic flavosemiquinone of choline oxidase is unusually insensitive to both molecular oxygen and artificial electron acceptors Arthrobacter globiformis