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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cyclic N-Oxides / metabolism
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Cyclic N-Oxides / pharmacology
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Enzyme Induction
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Gene Expression Regulation, Bacterial*
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Kinetics
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Molecular Structure
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Morpholines / metabolism
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NADH, NADPH Oxidoreductases / biosynthesis
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NADH, NADPH Oxidoreductases / genetics
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NADH, NADPH Oxidoreductases / metabolism*
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Operon
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Oxidoreductases Acting on CH-NH Group Donors
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Substrate Specificity
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Sulfoxides / metabolism
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Sulfoxides / pharmacology
Substances
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Cyclic N-Oxides
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Morpholines
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Sulfoxides
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4-methylmorpholine N-oxide
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methylamine dehydrogenase
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Oxidoreductases Acting on CH-NH Group Donors
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NADH, NADPH Oxidoreductases