Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 133, Issue 9, Pages 2852-2855Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja1111173
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Funding
- National Natural Science Foundation [2083-2009, 30525001, 20921091]
- Ministry of Science and Technology [2009ZX09501-008]
- 973 Program [2010-CB833200]
- Chinese Academy of Sciences [KJCX2-YW-H08, KSCX2-YW-G-06]
- Science and Technology Commission of Shanghai Municipality of China [09QH1402700]
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Thiopeptides are a class of clinically interesting and highly modified peptide antibiotics. Their biosyntheses share a common paradigm for characteristic core formation but differ in tailoring to afford individual members. Herein we report an unusual deesterification-amidation process in thiostrepton maturation to furnish the terminal amide moiety. TsrB, serving as a carboxylesterase, catalyzes the hydrolysis of the methyl ester intermediate to provide the carboxylate intermediate, which can be converted to the amide product by an amidotransferase, TsrC. These findings revealed a C-terminal methylation of the precursor peptide, which is cryptic in thiostrepton biosynthesis but potentially common in the formation of its homologous series of thiopeptides that vary in the C-terminal form as methyl ester, carboxylate, or amide.
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