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Biochem Biophys Res Commun. 2012 Jul 13;423(4):638-41. doi: 10.1016/j.bbrc.2012.05.156. Epub 2012 Jun 8.

Confirmation of Frm2 as a novel nitroreductase in Saccharomyces cerevisiae.

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  • 1Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, South Korea.

Abstract

Nitroreductases comprise a group of FMN- or FAD-dependent enzymes that reduce nitrosubstituted compounds by using NAD(P)H, and are found in bacterial species and yeast. Although there is little information on the biological functions of nitroreductases, some studies suggest their possible involvement in oxidative stress responses. In the yeast Saccharomyces cerevisiae, a putative nitroreductase protein, Frm2, has been identified based on its sequence similarity with known bacterial nitroreductases. Frm2 has been reported to function in the lipid signaling pathway. To study the functions of Frm2, we measured the nitroreductase activity of purified Frm2 on 4-nitroquinoline-N-oxide (4-NQO) using NADH. LC-MS analysis of the reaction products revealed that Frm2 reduced NQO into 4-aminoquinoline-N-oxide (4-AQO) via 4-hydroxyaminoquinoline (4-HAQO). An Frm2 deletion mutant exhibited growth inhibition in the presence of 4-NQO. Thus, in this study, we demonstrate a novel nitroreductase activity of Frm2 and its involvement in the oxidative stress defense system.

Copyright © 2012 Elsevier Inc. All rights reserved.

PMID:
22687599
[PubMed - indexed for MEDLINE]
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