EC 1.7.2.3 - Trimethylamine-N-oxide reductase (cytochrome c)

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IntEnz Enzyme Nomenclature
EC 1.7.2.3

Names

Accepted name:
trimethylamine-N-oxide reductase (cytochrome c)
Other names:
TMAO reductase
TOR
Systematic name:
trimethylamine:cytochrome c oxidoreductase

Reaction

Cofactor

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050626
UniProtKB/Swiss-Prot: (18) [show] [UniProt]

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: 470-475 (1992). [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: 293-302 (1997). [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: 435-447 (1998). [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: 11545-11551 (2001). [PMID: 11056172]

[EC 1.7.2.3 created 2002]