title: 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.
authors: School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia, USA.
authors: Chaoxuan
authors: C
authors: Li
authors: Feifei
authors: F
authors: Zhang
authors: Wendy L
authors: WL
authors: Kelly
mesh_terms: D000900:Anti-Bacterial Agents / Q000378:metabolism* / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects; D001424:Bacterial Infections / Q000188:drug therapy; D016296:Mutagenesis; D009154:Mutation; D013302:Streptomyces / Q000235:genetics / Q000378:metabolism*; D013883:Thiostrepton / Q000378:metabolism* / Q000494:pharmacology*; D013912:Threonine / Q000235:genetics / Q000378:metabolism
chemical_list: D000900:Anti-Bacterial Agents; D013912:Threonine; D013883:Thiostrepton