verA Gene is Involved in the Step to Make the Xanthone Structure of Demethylsterigmatocystin in Aflatoxin Biosynthesis
| العنوان: | verA Gene is Involved in the Step to Make the Xanthone Structure of Demethylsterigmatocystin in Aflatoxin Biosynthesis |
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| المؤلفون: | Hiromitsu Nakajima, Hiroyuki Nakagawa, Hidemi Hatabayashi, Kimiko Yabe, Jingjing Cai, Hongmei Zeng |
| المصدر: | International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 21, Iss 6389, p 6389 (2020) Volume 21 Issue 17 |
| بيانات النشر: | MDPI AG, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | 0301 basic medicine, Aflatoxin, hypA (aflY), verA (aflN), 030106 microbiology, dmtA (aflO), ordB (aflX), Article, Catalysis, lcsh:Chemistry, Inorganic Chemistry, 03 medical and health sciences, chemistry.chemical_compound, enzyme gene, Biosynthesis, Gene cluster, Xanthone, ver-1 (aflM), Physical and Theoretical Chemistry, Binding site, lcsh:QH301-705.5, Molecular Biology, Spectroscopy, chemistry.chemical_classification, Enzyme Gene, Molecular mass, Organic Chemistry, General Medicine, Computer Science Applications, stcP, 030104 developmental biology, Enzyme, lcsh:Biology (General), lcsh:QD1-999, HAMA intermediate, chemistry, Biochemistry, aflatoxin biosynthesis |
| الوصف: | In the biosynthesis of aflatoxin, verA, ver-1, ordB, and hypA genes of the aflatoxin gene cluster are involved in the pathway from versicolorin A (VA) to demethylsterigmatocystin (DMST). We herein isolated each disruptant of these four genes to determine their functions in more detail. Disruptants of ver-1, ordB, and hypA genes commonly accumulated VA in their mycelia. In contrast, the verA gene disruptant accumulated a novel yellow fluorescent substance (which we named HAMA) in the mycelia as well as culture medium. Feeding HAMA to the other disruptants commonly caused the production of aflatoxins B1 (AFB1) and G1 (AFG1). These results indicate that HAMA pigment is a novel aflatoxin precursor which is involved at a certain step after those of ver-1, ordB, and hypA genes between VA and DMST. HAMA was found to be an unstable substance to easily convert to DMST and sterigmatin. A liquid chromatography-mass spectrometry (LC-MS) analysis showed that the molecular mass of HAMA was 374, and HAMA gave two close major peaks in the LC chromatogram in some LC conditions. We suggest that these peaks correspond to the two conformers of HAMA one of them would be selectively bound on the substrate binding site of VerA enzyme and then converted to DMST. VerA enzyme may work as a key enzyme in the creation of the xanthone structure of DMST from HAMA. |
| وصف الملف: | application/pdf |
| تدمد: | 1422-0067 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55f3ed257706f6cb9ec7a034ef260debTest https://doi.org/10.3390/ijms21176389Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....55f3ed257706f6cb9ec7a034ef260deb |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14220067 |
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