E. coli nitroreductase explained

E. coli nitroreductase is a flavoprotein found in the bacteria Escherichia coli. It catalyses the reduction of nitro groups in a wide range of substrates to produce the corresponding hydroxylamine. Although its role in vivo is unclear, it has been identified as useful in the metabolism of a number of prodrugs in anti-cancer gene therapy.[1]

There are at least two oxygen-insensitive nitroreductases in E. coli. The major one is NfsA (EC 1.7.1.B3).[2] The other is NfsB (EC 1.5.1.34).[3]

See also

References

  1. Denny, W.A. "Nitroreductase-based GDEPT" Current Pharmaceutical Design, 2002, 8(15), 1349–1361.
  2. Zenno . S . Koike . H . Kumar . AN . Jayaraman . R . Tanokura . M . Saigo . K . Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase. . Journal of Bacteriology . August 1996 . 178 . 15 . 4508–14 . 10.1128/jb.178.15.4508-4514.1996 . 8755878. 178217 .
  3. Race . PR . Lovering . AL . Green . RM . Ossor . A . White . SA . Searle . PF . Wrighton . CJ . Hyde . EI . Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme. . The Journal of Biological Chemistry . 8 April 2005 . 280 . 14 . 13256–64 . 10.1074/jbc.M409652200 . 15684426. free .

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