Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 6, Pages 2844-2847Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja206713a
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Funding
- National Basic Research Program of China [2010CB833805]
- Chinese Academy of Sciences [KZCX2-YW-JC202, KSCX2-YW-G-065, LYQY200805, KZCX2-EW-G-12]
- Scientific Research Foundation for Returned Overseas Chinese Scholars of State Education Ministry
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The tirandamycins (TAMs) are a small group of Streptomyces-derived natural products that target bacterial RNA polymerase. Within the TAM biosynthetic cluster, trdE encodes a glycoside hydrolase whose role in TAM biosynthesis has been undefined until now. We report that in vivo trdE inactivation leads to accumulation of pre-tirandamycin, the earliest intermediate released from its mixed polyketide/nonribosomal peptide biosynthetic assembly line. In vitro and site-directed mutagenesis studies showed that TrdE, a putative glycoside hydrolase, catalyzes in a highly atypical fashion the installation of the Delta(11,12) double bond during TAM biosynthesis.
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