Thiamine oxidase

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

thiamine + 2 O₂ + H₂O ${\displaystyle \rightleftharpoons }$ thiamine acetic acid + 2 H₂O₂

The 3 substrates of this enzyme are thiamine, O₂, and H₂O, whereas its two products are 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.

References[]

• 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 (14): 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 (1): 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 (10): 2599–604. PMID 4987737.