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Literature summary for 1.1.3.17 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
Search for more literature for 1.1.3.17

Application

Application Comment Organism
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

Inhibitors Comment Organism Structure
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
0.5
-
 choline pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, 0°C Arthrobacter globiformis
0.6
-
 choline pH 7.0, 25°C, recombinant enzyme stored at pH 8.0, at -20°C or 0°C Arthrobacter globiformis
0.7
-
 choline pH 7.0, 25°C, recombinant enzyme stored at pH 6.0, -20°C Arthrobacter globiformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
choline + O2 Arthrobacter globiformis FAD-linked reaction betaine aldehyde + H2O2
-
 ?
FADH2 + O2 Arthrobacter globiformis
-
 FAD + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
 strain ATCC 8010
-

Reaction

Reaction Comment Organism Reaction ID
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)

Renatured (Comment) Organism
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

Storage Stability Organism
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)

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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

pH Stability pH Stability Maximum Comment Organism
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

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