Choline oxidase

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In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction

choline + O₂ $\rightleftharpoons$ betaine aldehyde + H₂O₂

Thus, the two substrates of this enzyme are choline and O₂, whereas its two products are betaine aldehyde and H₂O₂.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is choline:oxygen 1-oxidoreductase. This enzyme participates in glycine, serine, and threonine metabolism. It employs one cofactor, FAD.

[edit] References

IUBMB entry for 1.1.3.17
BRENDA references for 1.1.3.17 (Recommended.)
PubMed references for 1.1.3.17
PubMed Central references for 1.1.3.17
Google Scholar references for 1.1.3.17
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Fan F, Gadda G (2005). "On the catalytic mechanism of choline oxidase". J. Am. Chem. Soc. 127: 2067–74. PMID 15713082.
Takabe T (2003). "Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica". J. Biol. Chem. 278: 4932–42. PMID 12466265.