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Literature summary for 1.1.3.17 extracted from

  • Ghanem, M.; Gadda, G.
    Effects of reversing the protein positive charge in the proximity of the flavin N(1) locus of choline oxidase (2006), Biochemistry, 45, 3437-3447.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
H466A site-directed mutagenesis, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutant H466D and the wild-type enzyme Arthrobacter globiformis
H466D site-directed mutagenesis, the mutation alters the flavin binding to the enzyme, while substrate choline is normally bound, binding og glycine btaine is inhibited, spectrometrical analysis, the mutant shows a different flavin-binding stoichiometry of 0.29:1, compared to 1:1 for the wild-type enzyme, stabilized at pH 6.0-10.0, overview, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutant H466A and the wild-type enzyme, the mutant shows no catalytic activity Arthrobacter globiformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics and redox potentiometric analysis of liganded and unliganded wild-type and mutant enzymes, comparison of spectral parameters of wild-type and mutant enzymes, overview 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
-
?
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, His466 is a catalytic residue involved in flavin-binding Arthrobacter globiformis

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
FAD dependent on, covalently bound to the enzyme, involving His466, in an 1:1 stoichiometry, spectrometrical analysis, effects of pH, mutant enzyme H466D shows a 0.29:1 stoichiometry, overview, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutants H466D and H466A Arthrobacter globiformis