期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 139, 期 15, 页码 5317-5320出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b02432
关键词
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资金
- NIH [1DP1GM106413, 1R35GM118056, R01GM117016, T32GM067555]
- JSPS Program for Advancing Strategic International Networks to Accelerate the Circulation of Talented Researchers [G2604]
- Fellowship of Astellas Foundation for Research on Metabolic Disorders
- NSF [CHE-1048804]
- NIH NCRR [S10RR025631]
- Grants-in-Aid for Scientific Research [15KT0068] Funding Source: KAKEN
Fungal polyketide synthases (PKSs) can function collaboratively to synthesize natural products of significant structural diversity. Here we present a new mode of collaboration between a highly reducing PIKS (HRPKS) and a PKS-nonribosomal peptide synthetase (PKS-NRPS) in the synthesis of oxaleimides from the Penicillium species. The HRPKS is recruited in the synthesis of an olefin-containing free amino acid, which is activated and incorporated by the adenylation domain of the PKS-NRPS. The precisely positioned olefin from the unnatural amino acid is proposed to facilitate a scaffold rearrangement of the FKS-NRPS product to forge the maleimide and succinimide cores of oxaleimides.
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