Trimethylamine-N-oxide reductase
In enzymology, a trimethylamine-N-oxide reductase (EC 1.6.6.9) is an enzyme that catalyzes the chemical reaction
- NADH + H+ + trimethylamine N-oxide NAD+ + trimethylamine + H2O
| trimethylamine-N-oxide reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.6.6.9 | ||||||||
| CAS number | 37256-34-1 | ||||||||
| 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 | ||||||||
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The 3 substrates of this enzyme are NADH, H+, and trimethylamine N-oxide, whereas its 3 products are NAD+, trimethylamine, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a nitrogenous group as acceptor. The systematic name of this enzyme class is NADH:trimethylamine-N-oxide oxidoreductase. Other names in common use include trimethylamine N-oxide reductase, trimethylamine oxide reductase, TMAO reductase, and TOR. This enzyme participates in methane metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1TMO.
References
- Unemoto T, Hayashi M, Miyaki K, Hayashi M (1965). "Intracellular localization and properties of trimethylamine-N-oxide reductase in Vibrio parahaemolyticus". Biochim. Biophys. Acta. 110 (2): 319–28. doi:10.1016/s0926-6593(65)80039-x. PMID 4286289.