Issue 4, 2012
From the journal:

Chemical Communications

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

Chaoxuan Li,a   Feifei Zhanga  and  Wendy L. Kelly*a  

* Corresponding authors

a School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia USA
E-mail: wendy.kelly@chemistry.gatech.edu
Fax: (001) 404-894-229
Tel: (001) 404-385-1154

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.

Graphical abstract: Mutagenesis of the thiostrepton precursor peptide at Thr7 impacts both biosynthesis and function

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Article information

DOI
https://doi.org/10.1039/C1CC14281J
Article type
Communication
Submitted
15 Jul 2011
Accepted
21 Oct 2011
First published
08 Nov 2011

Chem. Commun., 2012,48, 558-560

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

C. Li, F. Zhang and W. L. Kelly, Chem. Commun., 2012, 48, 558 DOI: 10.1039/C1CC14281J

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