Thiamine oxidase

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In enzymology, a thiamine oxidase (EC 1.1.3.23) is an enzyme that catalyzes the chemical reaction

thiamine + 2 O₂ + H₂O $\rightleftharpoons$ thiamine acetic acid + 2 H₂O₂

The 3 substrates of this enzyme are thiamine, O₂, and H₂O, whereas its two products are thiamine acetic acid 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 thiamine:oxygen 5-oxidoreductase. Other names in common use include thiamin dehydrogenase, thiamine dehydrogenase, and thiamin:oxygen 5-oxidoreductase. This enzyme participates in thiamine metabolism. It employs one cofactor, FAD.

[edit] References

IUBMB entry for 1.1.3.23
BRENDA references for 1.1.3.23 (Recommended.)
PubMed references for 1.1.3.23
PubMed Central references for 1.1.3.23
Google Scholar references for 1.1.3.23
Edmondson DE, Kenney WC, Singer TP (1976). "Structural elucidation and properties of 8alpha-(N1-histidyl)riboflavin: the flavin component of thiamine dehydrogenase and beta-cyclopiazonate oxidocyclase". Biochemistry. 15: 2937–45. doi:10.1021/bi00659a001. PMID 8076.
Gomez-Moreno C, Edmondson DE (1985). "Evidence for an aldehyde intermediate in the catalytic mechanism of thiamine oxidase". Arch. Biochem. Biophys. 239: 46–52. doi:10.1016/0003-9861(85)90810-0. PMID 2988447.
Neal RA (1970). "Bacterial metabolism of thiamine. 3. Metabolism of thiamine to 3-(2'-methyl-4'-amino-5'-pyrimidylmethyl)-4-methyl-thiazole-5-acetic acid (thiamine acetic acid) by a flavoprotein isolated from a soil microorganism". J. Biol. Chem. 245: 2599–604. PMID 4987737.