Mutagenesis of the thiostrepton precursor peptide at Thr7 impacts both biosynthesis and function.
نویسندگان
چکیده
The seventh residue of thiostrepton is predicted to be critical for antibacterial activity. Substitution of Thr7 in the thiostrepton precursor peptide disrupts both biological activity and the successful biosynthesis of analogs.
منابع مشابه
Heterologous production of thiostrepton A and biosynthetic engineering of thiostrepton analogs.
Thiostrepton A 1, produced by Streptomyces laurentii ATCC 31255 (S. laurentii), is one of the more well-recognized thiopeptide metabolites. Thiostrepton A 1 and other thiopeptides are of great interest due to their potent activities against emerging antibiotic-resistant Gram-positive pathogens. Although numerous lines of evidence have established that the thiopeptides arise from the post-transl...
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The natural product thiopeptide antibiotic thiostrepton is shown to undergo facile epimerization at its thiazoline residue in favor of the naturally observed D-configuration, suggesting that a classical epimerase enzyme may not be involved in its biosynthesis.
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عنوان ژورنال:
- Chemical communications
دوره 48 4 شماره
صفحات -
تاریخ انتشار 2012