Trimethylamine N-Oxide Reductase
Part 5. Molybdenum/Tungsten
Published Online: 15 APR 2006
Copyright © 2006 John Wiley & Sons, Ltd. All rights reserved.
Handbook of Metalloproteins
How to Cite
Iobbi-Nivol, C., Haser, R., Méjean, V. and Czjzek, M. 2006. Trimethylamine N-Oxide Reductase. Handbook of Metalloproteins. 5.
- Published Online: 15 APR 2006
Trimethylamine N-oxide (TMAO) is a compound widely distributed in marine fish and invertebrates; and TMAO reducing enzymes are found not only in marine bacteria and photosynthetic bacteria living in ponds but also in enterobacteria. The various respiratory systems reducing TMAO, described so far, share a high level of homology either in their general structure, or in the regulation or mechanism of electron transfer. According to their content of molybdenum cofactor, the enzymes in charge of TMAO reduction are classified in the structural dimethylsulfoxide (DMSO) reductase family. TMAO reductases, however, in contrast to DMSO reductases are highly specific enzymes and reduce only their physiological substrate. The crystal structure was determined for the TMAO reductase from Shewanella massilia, and its structural differences with DMSO reductases in the environment of the active site. A tyrosine residue in the proximity of the molybdenum ion in DMSO reductases is absent in TMAO reductases and could be related to the differences in substrate specificities.
- trimethylamine N-oxide reductase;
- oxomolybdenum enzymes;
- substrate specificity;
- crystal structure;
- marine bacteria