期刊
JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY
卷 57, 期 2, 页码 191-196出版社
KOREAN SOC APPLIED BIOLOGICAL CHEMISTRY
DOI: 10.1007/s13765-014-4017-0
关键词
azaphilone pigment biosynthesis; fatty acid synthase; Monascus purpureus polyketide biosynthesis
资金
- Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Education [2011-0021169, 2013R1A1A2059458]
- National Research Foundation of Korea [2011-0021169, 2013R1A1A2059458] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
The biosynthetic gene cluster of Monascus azaphilone pigments (MAzPs) encodes a canonical fatty acid synthase, MpFAS2. It is thus proposed that MpFAS2 plays a role in MAzP biosynthesis by supplying short chain (C8 and C10) fatty acyl moieties. Targeted gene inactivation of MpfasB2 in Monascus purpureus generated an F9 mutant, which developed white hyphae that discharged a yellow color on potato dextrose agar. High-performance liquid chromatography analysis demonstrated that F9 was incapable of producing MAzP and accumulated a wide array of chromophoric compounds instead. The main compound found in F9 was monascusone A, a hydrogenated azaphilone lacking a fatty acyl moiety. Gas chromatography analysis of the fatty acid methyl esters indicated that there was no significant difference in the cellular fatty acyl (C16 and C18) contents between WT and F9. The present study demonstrates that the dedicated fatty acid synthase is required to decorate the azaphilone polyketides in MAzP biosynthesis.
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