期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 135, 期 12, 页码 4616-4619出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja312503y
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资金
- National Science Council of Taiwan [102-2917-I-564-008]
- NIH [1R01GM085128, 1DP1GM106413]
- Northern Illinois University
- NSF [CHE-1048804]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1048804] Funding Source: National Science Foundation
Fumagillin 1 is a meroterpenoid from Aspergillus fumigatus that is known for its anti-angiogenic activity by binding to human methionine aminopeptidase 2. The genetic and molecular basis for biosynthesis of 1 had been an enigma despite the availability of the A. fumigatus genome sequence. Here, we report the identification and verification of the fma gene cluster, followed by characterization of the polyketide synthase and acyltransferase involved in biosynthesis of the dioic acid portion of 1. More significantly, we uncovered the elusive beta-trans-bergamotene synthase in A. fumigatus as a membrane-bound terpene cyclase.
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