Trimethylamine N-oxide reductase
- Trimethylamine N-oxide reductase
Trimethylamine "N"-oxide reductase (TOR or TMAO reductase, EC 1.7.2.3) is a microbial enzyme that can reduce trimethylamine "N"-oxide (TMAO) into trimethylamine (TMA), as part of the electron transport chain. The enzyme has been purified from "E. coli" and the photosynthetic bacteria "Roseobacter denitrificans". [cite journal |author=Arata H, Shimizu M, Takamiya K |title=Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans |journal=J. Biochem. |volume=112 |issue=4 |pages=470–5 |year=1992 |pmid=1337081] Both the "R. denitrificans" and "E. coli" enzymes can accept electrons from cytochromes. [cite journal |author=Gon S, Giudici-Orticoni MT, Méjean V, Iobbi-Nivol C |title=Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli |journal=J. Biol. Chem. |volume=276 |issue=15 |pages=11545–51 |year=2001 |pmid=11056172 |url=http://www.jbc.org/cgi/content/full/276/15/11545 |doi=10.1074/jbc.M008875200]
trimethylamine + 2 (ferricytochrome c)-subunit + H2O → trimethylamine "N"-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
Trimethylamine oxide is found at high concentrations in the tissues of fish, and the bacterial reduction of this compound to foul-smelling trimethylamine is a major process in the spoilage of fish. [cite journal |author=Barrett EL, Kwan HS |title=Bacterial reduction of trimethylamine oxide |journal=Annu. Rev. Microbiol. |volume=39 |issue= |pages=131–49 |year=1985 |pmid=3904597 |doi=10.1146/annurev.mi.39.100185.001023]
ee also
*Oxidative phosphorylation
*Microbial metabolism
References
External links
* [http://www.expasy.org/enzyme/1.7.2.3 ENZYME entry for EC 1.7.2.3]
* [http://www.brenda-enzymes.org/php/result_flat.php4?ecno=1.7.2.3 BRENDA entry for EC 1.7.2.3]
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