Trimethylamine-N-oxide reductase (cytochrome c) explained
| trimethylamine-N-oxide reductase (cytochrome c) |
| Ec Number: | 1.7.2.3 |
| Cas Number: | 37256-34-1 |
| Go Code: | 0050626 |
In enzymology, a trimethylamine-N-oxide reductase (cytochrome c) is an enzyme that catalyzes the chemical reaction
trimethylamine + 2 (ferricytochrome c)-subunit + H2O
trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H
+The 3 substrates of this enzyme are trimethylamine, (ferricytochrome c)-subunit, and H2O, whereas its 3 products are trimethylamine N-oxide, (ferrocytochrome c)-subunit, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is trimethylamine:cytochrome c oxidoreductase. Other names in common use include TMAO reductase, and TOR. This enzyme participates in two-component system - general.
References
- Arata H, Shimizu M, Takamiya K . Tokyo . Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans . J. Biochem. . 112. 470 - 5 . 1337081 . 4 . October 1992.
- 10.1515/bchm.1997.378.3-4.293 . Knablein J, Dobbek H, Ehlert S, Schneider F . 1997 . Isolation, cloning, sequence analysis and X-ray structure of dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus . Biol. Chem. . 378 . 293 - 302 . 9165084 . 3–4 .
- Czjzek M, Dos Santos JP, Pommier J, Giordano G, Mejean V, Haser R . 1998 . Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution . J. Mol. Biol. . 284 . 435 - 47 . 9813128 . 10.1006/jmbi.1998.2156 . 2 .
- Gon S, Giudici-Orticoni MT, Mejean V, Iobbi-Nivol C . 2001 . Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli . J. Biol. Chem. . 276 . 11545 - 51 . 11056172 . 10.1074/jbc.M008875200 . 15 . free .
