Biochim Biophys Acta. 1996 May 2;1294(1):77-82.

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

Iobbi-Nivol C, Pommier J, Simala-Grant J, Méjean V, Giordano G.

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Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie, Marseille, France.

Abstract

Using a wide variety of N- and S-oxide compounds we have shown by kinetic analysis that only two N-oxides, trimethylamine-N-oxide and 4-methylmorpholine-N-oxide, can be considered good substrates for trimethylamine-N-oxide (TMAO) reductase on the basis of their kcat/Km 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.

PMID:: 8639717; [PubMed - indexed for MEDLINE]

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

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