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High substrate specificity and induction characteristics of trimethylamine-N-oxide reductase of Escherichia coli

1996; Elsevier BV; Volume: 1294; Issue: 1 Linguagem: Inglês

10.1016/0167-4838(95)00271-5

1878-1454

Chantal Iobbi‐Nivol, Janine Pommier, Joanne L. Simala‐Grant, Vincent Méjean, Gérard Giordano,

Bacterial Genetics and Biotechnology

Using a wide variety of N- and S-oxide compounds we have shown by kinetic analysis that only two N-oxidestrimethylamine-N-oxide and 4-methylmorpholine-N-oxide, can be considered good substrates for trimethylamine-N-oxide (TMAO) reductase on the basis of their kcatKm ratio. This result demonstrates that TMAO reductase possesses a high substrate specificity. Induction of the torCAD operon using the same S- and N-oxide compounds was also analyzed. We demonstrate that there is no correlation between the ability for a compound to be reduced by TMAO reductase and to induce TMAO reductase synthesis.