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NfsA is the major oxygen-insensitive nitroreductase ofEscherichia coli , similar in amino acid sequence to Frp, a flavin reductase ofVibrio harveyi . Here, we show that a single amino acid substitution at position 99, which may destroy three hydrogen bonds in the putative active center, transforms NfsA from a nitroreductase into a flavin reductase that is as active as the authentic Frp and a tartrazine reductase that is 30-fold more active than wild-type NfsA.

journal of bacteriology

Conversion of NfsA, the Major <i>Escherichia coli</i> Nitroreductase, to a Flavin Reductase with an Activity Similar to That of Frp, a Flavin Reductase in <i>Vibrio harveyi</i> , by a Single Amino Acid Substitution

Conversion of NfsA, the Major Escherichia coli Nitroreductase, to a Flavin Reductase with an Activity Similar to That of Frp, a Flavin Reductase in Vibrio harveyi , by a Single Amino Acid Substitution