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Literature summary for 1.1.3.17 extracted from

  • Fan, F.; Ghanem, M.; Gadda, G.
    Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance (2004), Arch. Biochem. Biophys., 421, 149-158.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6
-
choline pH 7.0, 25°C Arthrobacter globiformis
2.3
-
betaine-aldehyde pH 7.0, 25°C Arthrobacter globiformis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60612
-
2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence Arthrobacter globiformis
60614
-
2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence Arthrobacter globiformis
117000 122000 gel filtration Arthrobacter globiformis

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis Q7X2H8
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme, expression in Escherichia coli Arthrobacter globiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
betaine aldehyde + O2 + H2O
-
Arthrobacter globiformis betaine + H2O2
-
?
choline + O2
-
Arthrobacter globiformis betaine aldehyde + H2O2
-
?

Subunits

Subunits Comment Organism
dimer 2 * 60614, MALDI-TOF-MS, 2 * 60612, deduced from gene sequence Arthrobacter globiformis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
11.6
-
betaine-aldehyde pH 7.0, 25°C Arthrobacter globiformis
13.4
-
choline pH 7.0, 25°C Arthrobacter globiformis

Cofactor

Cofactor Comment Organism Structure
FAD one moiety per enzyme monomer, covalently bound Arthrobacter globiformis