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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 (P17117, EC 1.7.1.B3).[2] The other is NfsB (P38489, EC 1.5.1.34).[3]
See also edit
References edit
- ^ Denny, W.A. "Nitroreductase-based GDEPT" Current Pharmaceutical Design, 2002, 8(15), 1349–1361.
- ^ Zenno, S; Koike, H; Kumar, AN; Jayaraman, R; Tanokura, M; Saigo, K (August 1996). "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. 178 (15): 4508–14. doi:10.1128/jb.178.15.4508-4514.1996. PMC 178217. PMID 8755878.
- ^ Race, PR; Lovering, AL; Green, RM; Ossor, A; White, SA; Searle, PF; Wrighton, CJ; Hyde, EI (8 April 2005). "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. 280 (14): 13256–64. doi:10.1074/jbc.M409652200. PMID 15684426.
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