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J. Bacteriol., Jan 1998, 422-425, Vol 180, No. 2
Copyright © 1998, American Society for Microbiology

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 [In Process Citation]

S Zenno, T Kobori, M Tanokura and K Saigo
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan. tmichiue@hgc.ims.u-tokyo.ac.jp

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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