Structural highlights
3r6w is a 2 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , |
| Related: | 2v9c, 3lt5, 3keg |
| Gene: | azoR1, PA0785 ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[AZOR1_PSEAE] Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity (By similarity).
Publication Abstract from PubMed
Azoreductases are well known for azo pro-drug activation by gut flora. We show that azoreductases have a wider role in drug metabolism than previously thought as they can also reduce and hence activate nitrofurazone. Nitrofurazone, a nitroaromatic drug, is a broad spectrum antibiotic which has until now been considered as activated in bacteria by nitroreductases. The structure of the azoreductase with nitrofurazone bound was solved at 2.08 A and shows nitrofurazone in an active conformation. Based on the structural information, the kinetics and stoichiometry of nitrofurazone reduction by azoreductase from P. aeruginosa, we propose a mechanism of activation which accounts for the ability of azoreductases to reduce both azo and nitroaromatic drugs. This mode of activation can explain the cytotoxic side-effects of nitrofurazone through human azoreductase homologues.
Activation of nitrofurazone by azoreductases: multiple activities in one enzyme.,Ryan A, Kaplan E, Laurieri N, Lowe E, Sim E Sci Rep. 2011;1:63. Epub 2011 Aug 12. PMID:22355582[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ryan A, Kaplan E, Laurieri N, Lowe E, Sim E. Activation of nitrofurazone by azoreductases: multiple activities in one enzyme. Sci Rep. 2011;1:63. Epub 2011 Aug 12. PMID:22355582 doi:10.1038/srep00063
