In enzymology, a thiamine oxidase (EC 1.1.3.23) is an enzyme that catalyzes the chemical reaction
| thiamin oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.3.23 | ||||||||
| CAS no. | 96779-44-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- thiamine + 2 O2 + H2O 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.
References
edit- 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.
