Confirmation of Frm2 as a novel nitroreductase in Saccharomyces cerevisiae

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Title
Confirmation of Frm2 as a novel nitroreductase in Saccharomyces cerevisiae
Author(s)
Seo Young Bang; Jeong Hoon Kim; Phil Young Lee; Kwang-Hee Bae; J S Lee; P S Kim; D H Lee; P K Myung; Byoung Chul ParkSung Goo Park
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 423, no. 4, pp. 638-641
Publication Year
2012
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.
Keyword
4-AQO4-NQOFrm2NitroreductaseOxidative stress
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2012.05.156
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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