Confirmation of Frm2 as a novel nitroreductase in Saccharomyces cerevisiae

Cited 15 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorSeo Young Bang-
dc.contributor.authorJeong Hoon Kim-
dc.contributor.authorPhil Young Lee-
dc.contributor.authorKwang-Hee Bae-
dc.contributor.authorJ S Lee-
dc.contributor.authorP S Kim-
dc.contributor.authorD H Lee-
dc.contributor.authorP K Myung-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorSung Goo Park-
dc.date.accessioned2017-04-19T09:32:14Z-
dc.date.available2017-04-19T09:32:14Z-
dc.date.issued2012-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1016/j.bbrc.2012.05.156ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10813-
dc.description.abstractNitroreductases 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.-
dc.publisherElsevier-
dc.titleConfirmation of Frm2 as a novel nitroreductase in Saccharomyces cerevisiae-
dc.title.alternativeConfirmation of Frm2 as a novel nitroreductase in Saccharomyces cerevisiae-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number4-
dc.citation.endPage641-
dc.citation.startPage638-
dc.citation.volume423-
dc.contributor.affiliatedAuthorSeo Young Bang-
dc.contributor.affiliatedAuthorJeong Hoon Kim-
dc.contributor.affiliatedAuthorPhil Young Lee-
dc.contributor.affiliatedAuthorKwang-Hee Bae-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.alternativeName방서영-
dc.contributor.alternativeName김정훈-
dc.contributor.alternativeName이필영-
dc.contributor.alternativeName배광희-
dc.contributor.alternativeName이종석-
dc.contributor.alternativeName김판수-
dc.contributor.alternativeName이도희-
dc.contributor.alternativeName명평근-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName박성구-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 423, no. 4, pp. 638-641-
dc.identifier.doi10.1016/j.bbrc.2012.05.156-
dc.subject.keyword4-AQO-
dc.subject.keyword4-NQO-
dc.subject.keywordFrm2-
dc.subject.keywordNitroreductase-
dc.subject.keywordOxidative stress-
dc.subject.local4-AQO-
dc.subject.local4-NQO-
dc.subject.localFrm2-
dc.subject.localnitroreductase-
dc.subject.localNitroreductase-
dc.subject.localOxidative stre-
dc.subject.localOxidative stress-
dc.subject.localOXIDATIVE STRESS-
dc.subject.localOxidative Stress-
dc.subject.localoxidative stress-
dc.description.journalClassY-
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
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.