PMID:9440535
| Citation |
Zenno, S, Kobori, T, Tanokura, M and Saigo, K (1998) 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. J. Bacteriol. 180:422-5 |
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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. |
| Links | |
| Keywords |
Amino Acid Sequence; Escherichia coli/enzymology; FMN Reductase; Follistatin-Related Proteins; Glycoproteins/chemistry; Glycoproteins/metabolism; Hydrogen Bonding; Kinetics; Molecular Sequence Data; NADH, NADPH Oxidoreductases/biosynthesis; NADH, NADPH Oxidoreductases/chemistry; NADH, NADPH Oxidoreductases/metabolism; Nitroreductases/metabolism; Sequence Homology, Amino Acid; Vibrio/enzymology |
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