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 |
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| Authors: | Shuhei Zenno Toshiro Kobori Masaru Tanokura and Kaoru Saigo |
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| Institution: | Department of Biophysics and Biochemistry, Graduate School of Science,1. and Biotechnology Research Center,3. University of Tokyo, Bunkyo-ku, Tokyo 113, and Yokohama Research Center, Chisso Corporation, Kanazawa-ku, Yokohama 236,2. Japan |
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| Abstract: | NfsA is the major oxygen-insensitive nitroreductase of Escherichia coli, similar in amino acid sequence to Frp, a flavin reductase of Vibrio 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. |
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