High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli
Identifieur interne : 002894 ( Istex/Curation ); précédent : 002893; suivant : 002895High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli
Auteurs : Chantal Iobbi-Nivol [France] ; Janine Pommier [France] ; Joanne Simala-Grant [Canada] ; Vincent Méjean [France] ; Gérard Giordano [France]Source :
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology [ 0167-4838 ] ; 1996.
Abstract
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 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.
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DOI: 10.1016/0167-4838(95)00271-5
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Aiguier, 13402 Marseille</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology</title><title level="j" type="abbrev">BBAPRO</title><idno type="ISSN">0167-4838</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996">1996</date><biblScope unit="volume">1294</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="77">77</biblScope><biblScope unit="page" to="82">82</biblScope></imprint><idno type="ISSN">0167-4838</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0167-4838</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 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.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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