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Literature summary extracted from

  • Hoang, J.V.; Gadda, G.
    Trapping choline oxidase in a nonfunctional conformation by freezing at low pH (2007), Proteins, 66, 611-620.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.3.17 additional information enzyme is of both biotechnological and medical interest, since glycine betaine can be accumulated in the cytoplasm of cells to prevent dehydration and plasmolysis in adverse hyperosmotic environments in pathogenic bacteria Arthrobacter globiformis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.17 additional information low pH induces a localized and reversible conformational change that is associated with the complete and reversible loss of catalytic activity 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 steady-state kinetics and thermodynamics, effect of pH on the hysteretic behavior of the enzyme at 25°C, kinetic parameters of enzyme stored at pH 6.0 and -20°C, overview Arthrobacter globiformis
1.1.3.17 0.5
-
 choline pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, 0°C Arthrobacter globiformis
1.1.3.17 0.6
-
 choline pH 7.0, 25°C, recombinant enzyme stored at pH 8.0, at -20°C or 0°C Arthrobacter globiformis
1.1.3.17 0.7
-
 choline pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, -20°C 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 FAD-linked reaction 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 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

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.1.3.17 incubation of the inactive enzyme at pH values of pH 6.5 and above, and 25°C results in a fast and partial reactivation of the enzyme, which occurrs with slow onset of steady state during enzymatic turnover, overview Arthrobacter globiformis

Storage Stability

EC Number Storage Stability Organism
1.1.3.17 storage at pH 6 and -20°C results in a change of conformation of the enzyme, which is associated with complete loss of catalytic activity when the enzyme is assayed at pH 6.0 Arthrobacter globiformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.17 choline + O2 FAD-linked reaction Arthrobacter globiformis betaine aldehyde + H2O2
-
 ?
1.1.3.17 FADH2 + O2
-
 Arthrobacter globiformis FAD + H2O2
-
 ?

Temperature Optimum [°C]

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.17 4.4
-
 choline pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, -20°C Arthrobacter globiformis
1.1.3.17 13.3
-
 choline pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, 0°C Arthrobacter globiformis
1.1.3.17 14.9
-
 choline pH 7.0, 25°C, recombinant enzyme stored at pH 8.0, -20°C Arthrobacter globiformis
1.1.3.17 15.5
-
 choline pH 7.0, 25°C, recombinant enzyme stored at pH 8.0, 0°C Arthrobacter globiformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.17 7
-
 assay at Arthrobacter globiformis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.3.17 6.5 9.6 low pH induces a localized and reversible conformational change that is associated with the complete and reversible loss of catalytic activity, overview Arthrobacter globiformis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.3.17 additional information
-
 low pH induces a localized and reversible conformational change that is associated with the complete and reversible loss of catalytic activity Arthrobacter globiformis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.17 FAD dependent on, covalently bound to the enzyme Arthrobacter globiformis