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Literature summary extracted from

  • Rungsrisuriyachai, K.; Gadda, G.
    Role of asparagine 510 in the relative timing of substrate bond cleavages in the reaction catalyzed by choline oxidase (2010), Biochemistry, 49, 2483-2490.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.17 expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)pLysS Arthrobacter globiformis

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.17 additional information substitution of Asn510 with alanine, but not with histidine, results in a change from stepwise to concerted mechanisms for the cleavages of the OH and CH bonds of choline catalyzed by the enzyme Arthrobacter globiformis
1.1.3.17 N510A site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein, enzyme kinetics decrease of 4300fold in the kcat/Kcholine, 600fold in the kred, 660fold in the kcat, and 50fold in the kcat/Koxygen values Arthrobacter globiformis
1.1.3.17 N510D site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein, 75% of the flavin associates noncovalently, inactive mutant Arthrobacter globiformis
1.1.3.17 N510H site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein, decreases in the kcat/Kcholine, the kred, the kcat, and the kcat/Koxygen values Arthrobacter globiformis
1.1.3.17 N510L site-directed mutagenesis of a catalytic residue resulting in low incorporation of FAD into the protein 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, isotopic effects, detailed overview Arthrobacter globiformis
1.1.3.17 0.055
-
 O2 pH 10.0, 25°C, mutant N510A Arthrobacter globiformis
1.1.3.17 0.48
-
 choline pH 10.0, 25°C, mutant N510H Arthrobacter globiformis
1.1.3.17 0.535
-
 O2 pH 10.0, 25°C, mutant N510H Arthrobacter globiformis
1.1.3.17 0.6
-
 choline pH 7.0, 25°C, wild-type enzyme Arthrobacter globiformis
1.1.3.17 1.7
-
 choline pH 10.0, 25°C, mutant N510A Arthrobacter globiformis
1.1.3.17 60
-
 choline pH 7.0, 25°C, mutant N510H Arthrobacter globiformis
1.1.3.17 155
-
 choline pH 7.0, 25°C, mutant N510A Arthrobacter globiformis
1.1.3.17 213
-
 choline pH 7.0, 25°C, mutant N510L 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 + 2 O2 + H2O Arthrobacter globiformis
-
 betaine + 2 H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.17 Arthrobacter globiformis
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.3.17 commercial preparation
-
 Arthrobacter globiformis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.17 betaine aldehyde + O2 + H2O half-reaction Arthrobacter globiformis betaine + H2O2
-
 ?
1.1.3.17 choline + 2 O2 + H2O
-
 Arthrobacter globiformis betaine + 2 H2O2
-
 ?
1.1.3.17 choline + O2 half-reaction Arthrobacter globiformis betaine aldehyde + H2O2
-
 ?
1.1.3.17 additional information flavoprotein choline oxidase catalyzes the oxidation of choline to glycine betaine with transient formation of an aldehyde intermediate and molecular oxygen as final electron acceptor 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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.17 0.02
-
 choline pH 7.0, 25°C, mutant N510L Arthrobacter globiformis
1.1.3.17 0.06
-
 choline pH 7.0, 25°C, mutant N510A Arthrobacter globiformis
1.1.3.17 0.09
-
 O2 pH 10.0, 25°C, mutant N510A Arthrobacter globiformis
1.1.3.17 0.09
-
 choline pH 10.0, 25°C, mutant N510A Arthrobacter globiformis
1.1.3.17 0.51
-
 choline pH 7.0, 25°C, mutant N510H Arthrobacter globiformis
1.1.3.17 3.4
-
 O2 pH 10.0, 25°C, mutant N510H Arthrobacter globiformis
1.1.3.17 3.4
-
 choline pH 10.0, 25°C, mutant N510H Arthrobacter globiformis
1.1.3.17 13.4
-
 choline pH 7.0, 25°C, wild-type enzyme Arthrobacter globiformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.17 7 10 assay at Arthrobacter globiformis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.17 FAD
-
 Arthrobacter globiformis

General Information

EC Number General Information Comment Organism
1.1.3.17 evolution the enzyme belongs to the glucose-methanol-choline oxidoreductase enzyme superfamily, which shares a highly conserved His-Asn catalytic pair in the active site, Asn510 in the Arthrobacter globiformis enzyme Arthrobacter globiformis
1.1.3.17 malfunction replacing Asn510 with alanine or histidine negatively affects both the reductive and oxidative half-reactions catalyzed by choline oxidase. Substitution of Asn510 with alanine, but not with histidine, results in a change from stepwise to concerted mechanisms for the cleavages of the OH and CH bonds of choline catalyzed by the enzyme Arthrobacter globiformis
1.1.3.17 additional information Asn510 participating in both the reductive and oxidative half-reactions but having a minimal rle in substrate binding Arthrobacter globiformis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.3.17 0.00009
-
 choline pH 7.0, 25°C, mutant N510L Arthrobacter globiformis
1.1.3.17 0.0004
-
 choline pH 7.0, 25°C, mutant N510A Arthrobacter globiformis
1.1.3.17 0.0085
-
 choline pH 7.0, 25°C, mutant N510H Arthrobacter globiformis
1.1.3.17 0.055
-
 choline pH 10.0, 25°C, mutant N510A Arthrobacter globiformis
1.1.3.17 1.7
-
 O2 pH 10.0, 25°C, mutant N510A Arthrobacter globiformis
1.1.3.17 6.36
-
 O2 pH 10.0, 25°C, mutant N510H Arthrobacter globiformis
1.1.3.17 7.1
-
 choline pH 10.0, 25°C, mutant N510H Arthrobacter globiformis
1.1.3.17 22
-
 choline pH 7.0, 25°C, wild-type enzyme Arthrobacter globiformis