Literature summary for 1.1.3.17 extracted from

Quaye, O.; Nguyen, T.; Gannavaram, S.; Pennati, A.; Gadda, G.
Rescuing of the hydride transfer reaction in the Glu312Asp variant of choline oxidase by a substrate analogue (2010), Arch. Biochem. Biophys., 499, 1-5.

Search for more literature for 1.1.3.17

Protein Variants

Protein Variants	Comment	Organism
E312D	site-directed mutagenesis, the mutant enzyme shows a 260fold decrease in the rate constant for the hydride transfer reaction and did not transfer the hydride ion in a full quantum mechanical tunneling fashion. The overall turnover of the Glu312Asp enzyme at saturating concentrations of 3-hydroxypropyl-trimethylamine and oxygen is predominantly controlled by the hydride transfer reaction that results in the reduction of the enzyme-bound flavin. The kred value with 3-hydroxypropyl-trimethylamine is 20times higher than the value determined with choline as substrate for the Glu312Asp enzyme. The reductive half-reaction can be effectively, but not completely,rescued upon introducing on the substrate the methylenethat is missing from the side chain of residue 312	Arthrobacter globiformis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	stopped-flow and steady-state kinetics, and sequential steady-state kinetic mechanism, overview	Arthrobacter globiformis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
choline + 2 O2 + H2O2	Arthrobacter globiformis	-	betaine + 2 H2O2	-	?

Organism

Organism	UniProt	Comment	Textmining
Arthrobacter globiformis	Q7X2H8	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-hydroxypropyl-trimethylamine + 2 O2 + H2O2	-	Arthrobacter globiformis	?	-	?
choline + 2 O2 + H2O2	-	Arthrobacter globiformis	betaine + 2 H2O2	-	?
choline + 2 O2 + H2O2	choline oxidase catalyzes the flavin-mediated, two-step oxidation of choline to glycine betaine with formation of betaine aldehyde as intermediate. Both the oxidation of the alcohol substrate and the aldehyde intermediate require molecular oxygen to accept electrons from the reduced flavin. The reaction of hydride transfer of choline oxidation is rate limiting for the overall turnover of the wild-type and the Glu312Asp enzymes with choline as substrate	Arthrobacter globiformis	betaine + 2 H2O2	-	?

Synonyms

Synonyms	Comment	Organism
choline-oxygen 1-oxidoreductase	-	Arthrobacter globiformis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Arthrobacter globiformis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
10	-	assay at	Arthrobacter globiformis

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Arthrobacter globiformis

General Information

General Information	Comment	Organism
additional information	in the active site of choline oxidase, Glu312 participates in binding the trimethylammonium group of choline, thereby positioning the alcohol substrate properly for efficient hydride transfer to the enzyme-bound flavin. Glu312 is the only negatively charged residue in the active site of the enzyme	Arthrobacter globiformis
physiological function	the reaction catalyzed by choline oxidase is of importance due to the trigger of glycine betaine accumulation in the cytoplasm of a number of plants and pathogenic bacteria in response to hyperosmotic and adverse temperature conditions to prevent dehydration and eventual cell death	Arthrobacter globiformis

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Release 2023.1 (January 2023)