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Literature summary for 1.1.3.17 extracted from

  • Ghanem, M.; Gadda, G.
    On the catalytic role of the conserved active site residue His466 of choline oxidase (2005), Biochemistry, 44, 893-904.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Arthrobacter globiformis

Protein Variants

Protein Variants Comment Organism
H466A decrease in kcat and kcat/Km-value for choline, but not for oxygen, partial rescue of activity in presence of imidazolium Arthrobacter globiformis
H466A site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme, the enzyme activity in the mutant strain can partially be rescued by addition of exogenous imidazolium, but not by imidazole, overview Arthrobacter globiformis

Inhibitors

Inhibitors Comment Organism Structure
glycine betaine binds to the active site, different binding of wild-type and mutant enzymes, overview Arthrobacter globiformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics of wild-type and mutant enzymes at different pH and in presence or absence of imidazole, kinetic isotope effects Arthrobacter globiformis
1.7
-
choline pH 7.0, 25°C, wild type Arthrobacter globiformis
21
-
O2 pH 7.0, 25°C, mutant H466A Arthrobacter globiformis
29
-
choline pH 7.0, 25°C mutant H466A Arthrobacter globiformis
703
-
O2 pH 7.0, 25°C, wild type Arthrobacter globiformis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
strain ATCC 8010
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type enzyme in oxidized state to homogeneity Arthrobacter globiformis

Reaction

Reaction Comment Organism Reaction ID
betaine aldehyde + O2 + H2O = betaine + H2O2 His466 is a catalytic residue involved in the oxidation but not the reduction, reaction mechanism Arthrobacter globiformis
choline + O2 = betaine aldehyde + H2O2 His466 is a catalytic residue involved in the oxidation but not the reduction, reaction mechanism Arthrobacter globiformis

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
CHO
-
Arthrobacter globiformis

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
0.03
-
choline pH 5.5, 25°C, mutant H466A Arthrobacter globiformis
0.03
-
choline pH 5.5, 25°C, recombinant mutant H466A Arthrobacter globiformis
0.07
-
choline pH 6.0, 25°C, recombinant mutant H466A Arthrobacter globiformis
0.21
-
choline pH 5.5, 25°C, mutant H466A, presence of imidazole Arthrobacter globiformis
0.37
-
choline pH 7.0, 25°C, recombinant mutant H466A Arthrobacter globiformis
0.52
-
choline pH 7.0, 25°C, mutant H466A, presence of imidazole Arthrobacter globiformis
0.7
-
choline pH 10.0, 25°C, mutant H466A, presence of imidazole Arthrobacter globiformis
0.72
-
choline pH 8.0, 25°C, recombinant mutant H466A Arthrobacter globiformis
0.73
-
choline pH 10.0, 25°C, mutant H466A Arthrobacter globiformis
0.73
-
choline pH 10.0, 25°C, recombinant mutant H466A Arthrobacter globiformis
1.1
-
choline pH 7.0, 25°C, mutant H466A Arthrobacter globiformis
61
-
choline pH 7.0, 25°C, wild type 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
5.5 10
-
Arthrobacter globiformis

Cofactor

Cofactor Comment Organism Structure
FAD covalently bound to the enzyme, spectral analysis of denatured wild-type and mutant enzymes, overview Arthrobacter globiformis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics Arthrobacter globiformis