The Enzyme Database

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EC 1.7.2.3     
Accepted name: trimethylamine-N-oxide reductase (cytochrome c)
Reaction: trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
For diagram of dimethyl sulfide catabolism, click here
Other name(s): TMAO reductase; TOR
Systematic name: trimethylamine:cytochrome c oxidoreductase
Comments: The cytochrome c involved in photosynthetic bacteria is a pentaheme protein. Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor. The reductant is a membrane-bound multiheme cytochrome c. Also reduces dimethyl sulfoxide to dimethyl sulfide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-34-1
References:
1.  Arata, H., Shimizu, M. and Takamiya, K. Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans. J. Biochem. (Tokyo) 112 (1992) 470–475. [PMID: 1337081]
2.  Knablein, J., Dobbek, H., Ehlert, S. and Schneider, F. Isolation, cloning, sequence analysis and X-ray structure of dimethyl sulfoxide trimethylamine N-oxide reductase from Rhodobacter capsulatus. Biol. Chem. 378 (1997) 293–302. [PMID: 9165084]
3.  Czjzek, M., Dos Santos, J.P., Pommier, J., Giordano, G., Méjean, V. and Haser, R. Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 Å resolution. J. Mol. Biol. 284 (1998) 435–447. [PMID: 9813128]
4.  Gon, S., Giudici-Orticoni, M.T., Mejean, V. and Iobbi-Nivol, C. Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli. J. Biol. Chem. 276 (2001) 11545–11551. [PMID: 11056172]
[EC 1.7.2.3 created 2002]
 
 


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