High substrate specificity and induction characteristics of trimethylamine-N-oxide reductase of Escherichia coli.
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.
Iobbi-Nivol
C
C
Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie, Marseille, France.
Pommier
J
J
Simala-Grant
J
J
Méjean
V
V
Giordano
G
G
D003497:Cyclic N-Oxides / Q000378:metabolism / Q000494:pharmacology; D004790:Enzyme Induction; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D007700:Kinetics; D015394:Molecular Structure; D009025:Morpholines / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D009876:Operon; D000587:Oxidoreductases Acting on CH-NH Group Donors; D013379:Substrate Specificity; D013454:Sulfoxides / Q000378:metabolism / Q000494:pharmacology
D003497:Cyclic N-Oxides; D009025:Morpholines; D013454:Sulfoxides; C067960:4-methylmorpholine N-oxide; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D009247:NADH, NADPH Oxidoreductases