Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.3.17 extracted from

  • Finnegan, S.; Gadda, G.
    Substitution of an active site valine uncovers a kinetically slow equilibrium between competent and incompetent forms of choline oxidase (2008), Biochemistry, 47, 13850-13861.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Escherichia coli Arthrobacter globiformis

Protein Variants

Protein Variants Comment Organism
V464A mutant, analysis of kinetic parameters Arthrobacter globiformis
V464T mutant, analysis of kinetic parameters Arthrobacter globiformis

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis Q7X2H8
-
-

Renatured (Commentary)

Renatured (Comment) Organism
fully oxidized form of the enzyme is obtained via slow oxidation of the flavosemiquinone by extensive dialysis at pH 6 and 4°C Arthrobacter globiformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.3
-
V464A mutant, substrate choline (10 mM), pH 7 Arthrobacter globiformis
0.3
-
V464T mutant, substrate choline (10 mM), pH 7 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
choline oxidase
-
Arthrobacter globiformis

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
comparison of pka values of the mutants V464A and V464T Arthrobacter globiformis

Cofactor

Cofactor Comment Organism Structure
FAD covalently bound in both mutants (V464A and V464T) Arthrobacter globiformis