| 词条 | Nitroreductase |
| 释义 |
Members of this family include oxygen-insensitive NAD(P)H nitroreductase (FMN-dependent nitroreductase) (6,7-dihydropteridine reductase) ({{EC number|1.5.1.34}}) and NADH dehydrogenase ({{EC number|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 {{Uniprot|P34273}}, D. melanogaster {{Uniprot|Q8T3Q0}}, {{Uniprot|Q9VTE7}}, mouse {{Uniprot|Q9DCX8}} and human {{Uniprot|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. An example of a potential cold-active enzyme for prodrug therapy was described using a cold-active nitroreductase, Ssap-NtrB[4] (Çelik and Yetis, 2012). Despite Ssap-NtrB derived from a mesophilic bacterium, it showed optimal activity at 20°C against cancer prodrugs. Authors comment that the cold-activity of this novel enzyme will be useful for therapies in combination with crymotherapy, exposing the target tissue to low temperatures in order to trigger the enzyme activity to activate the drug only where is required. Moreover, the enzyme could also be used for bioremediation of compounds of explosive and volatile nature in regions where high activity at low temperatures is needed. Subfamilies
Human proteins containing this domainIYD; References1. ^{{cite journal |vauthors=Hecht HJ, Erdmann H, Park HJ, Sprinzl M, Schmid RD | title = Crystal structure of NADH oxidase from Thermus thermophilus | journal = Nat. Struct. Biol. | volume = 2 | issue = 12 | pages = 1109–14 |date=December 1995 | pmid = 8846223 | doi = 10.1038/nsb1295-1109| url = | issn = }} {{InterPro content|IPR000415}}{{membrane-protein-stub}}2. ^{{cite journal |vauthors=de Oliveira IM, Henriques JA, Bonatto D | title = In silico identification of a new group of specific bacterial and fungal nitroreductases-like proteins | journal = Biochem. Biophys. Res. Commun. | volume = 355 | issue = 4 | pages = 919–25 |date=April 2007 | pmid = 17331467 | doi = 10.1016/j.bbrc.2007.02.049 | url = | issn = }} 3. ^{{Cite journal|last=Bryant|first=C.|last2=DeLuca|first2=M.|date=1991-03-05|title=Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae.|url=http://www.jbc.org/content/266/7/4119|journal=Journal of Biological Chemistry|language=en|volume=266|issue=7|pages=4119–4125|issn=0021-9258|pmid=1999405}} 4. ^{{Cite journal|last=Çelik|first=Ayhan|last2=Yetiş|first2=Gülden|date=2012-06-01|title=An unusually cold active nitroreductase for prodrug activations|url=http://www.sciencedirect.com/science/article/pii/S0968089612002799|journal=Bioorganic & Medicinal Chemistry|volume=20|issue=11|pages=3540–3550|doi=10.1016/j.bmc.2012.04.004}} 2 : Protein domains|Single-pass transmembrane proteins |
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