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Mutagenesis of the thiostrepton precursor peptide at Thr7 impacts both biosynthesis and function.


ABSTRACT: 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.

SUBMITTER: Li C 

PROVIDER: S-EPMC3849712 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

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Mutagenesis of the thiostrepton precursor peptide at Thr7 impacts both biosynthesis and function.

Li Chaoxuan C   Zhang Feifei F   Kelly Wendy L WL  

Chemical communications (Cambridge, England) 20111108 4


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. ...[more]

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