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Literature summary extracted from

  • Fan, F.; Germann, M.W.; Gadda, G.
    Mechanistic studies of choline oxidase with betaine aldehyde and its isosteric analogue 3,3-dimethylbutyraldehyde (2006), Biochemistry, 45, 1979-1986.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.17 3,3-dimethylbutyraldehyde product analogue inhibition, 74-90% reduced flavin reduction dependent on pH Arthrobacter globiformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.17 additional information
-
 additional information kinetics, recombinant enzyme, NMR-determination of hydration ratio of betaine aldehyde, overview Arthrobacter globiformis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.17 choline + O2 Arthrobacter globiformis the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps, overview betaine aldehyde + H2O2
-
 ?
1.1.3.17 FADH2 + O2 Arthrobacter globiformis
-
 FAD + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.17 Arthrobacter globiformis
-
 strain ATCC 8010
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.3.17 betaine aldehyde + O2 + H2O = betaine + H2O2 reaction mechanism, the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps Arthrobacter globiformis
a
1.1.3.17 choline + O2 = betaine aldehyde + H2O2 reaction mechanism, the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps Arthrobacter globiformis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.17 3,3-dimethylbutan-1-ol + O2 10fold lower activity compared to choline Arthrobacter globiformis ?
-
 ?
1.1.3.17 choline + O2
-
 Arthrobacter globiformis betaine aldehyde + H2O2
-
 ?
1.1.3.17 choline + O2 the enzyme catalyzes the four-electron-oxidation of choline to glycine betaine via the intermediate betaine aldehyde in two sequential FAD-dependent reaction steps, overview Arthrobacter globiformis betaine aldehyde + H2O2
-
 ?
1.1.3.17 FADH2 + O2
-
 Arthrobacter globiformis FAD + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.17 CHO
-
 Arthrobacter globiformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.17 25
-
 assay at Arthrobacter globiformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.17 8
-
 assay at Arthrobacter globiformis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.3.17 5 10
-
 Arthrobacter globiformis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.17 FAD 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 Arthrobacter globiformis