Nitroreductase
| Nitroreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Nitroreductase | ||||||||
| Pfam | PF00881 | ||||||||
| InterPro | IPR000415 | ||||||||
| CDD | cd02062 | ||||||||
| |||||||||
Nitroreductases are a family of evolutionarily related proteins involved in the reduction of nitrogen-containing compounds, including those containing the nitro functional group. Members of this family utilise FMN as a cofactor and are often found to be homodimers.[1][2]
Members of this family include oxygen-insensitive NAD(P)H nitroreductase (FMN-dependent nitroreductase) (6,7-dihydropteridine reductase) (EC 1.5.1.34) and NADH dehydrogenase (EC 1.6.99.3). A number of these proteins are described as oxidoreductases. They are primarily found in bacterial lineages though a number of eukaryotic homologs have been identified: C. elegans P34273, D. melanogaster Q8T3Q0, Q9VTE7, mouse Q9DCX8 and human O75989. This protein is not found in photosynthetic eukaryotes. The sequences containing this entry in photosynthetic organisms are possible false positives.
The nitroreductase of Enterobacter cloacae was identified by Bryant and Deluca[3] in E. cloaca isolated from a munitions facility, on the basis of its ability to metabolize TNT (trinitrotoluene). Since then many homologues have been identified and the family is now known to include members in diverse organisms, that catalize diverse reactions. The iodotyrosine deiodenase of mammals is a dehalogenase, the BluB of Sinorhizobium meliloti canibalizes the bound FMN to furnish a critical intermediate in vitamin B12 biosynthesis.
Crystal structures of the E. cloacae and E. coli enzymes have been published with a variety of substrates and analogues bound.
Subfamilies
Human proteins containing this domain
IYD;
References
- ↑ Hecht HJ, Erdmann H, Park HJ, Sprinzl M, Schmid RD (December 1995). "Crystal structure of NADH oxidase from Thermus thermophilus". Nat. Struct. Biol. 2 (12): 1109–14. doi:10.1038/nsb1295-1109. PMID 8846223.
- ↑ de Oliveira IM, Henriques JA, Bonatto D (April 2007). "In silico identification of a new group of specific bacterial and fungal nitroreductases-like proteins". Biochem. Biophys. Res. Commun. 355 (4): 919–25. doi:10.1016/j.bbrc.2007.02.049. PMID 17331467.
- ↑ Bryant, C.; DeLuca, M. (1991-03-05). "Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae.". Journal of Biological Chemistry 266 (7): 4119–4125. ISSN 0021-9258. PMID 1999405.
This article incorporates text from the public domain Pfam and InterPro IPR000415