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• W2029384328 abstract "The unique glycopeptide antibiotic A47934, produced by Streptomyces toyocaensis, possesses a nonglycosylated heptapeptide core that is sulfated on the phenolic hydroxyl of the N-terminal 4-hydroxy-L-phenylglycine residue. Genetic and biochemical experiments confirmed that StaL is a sulfotransferase capable of sulfating the predicted crosslinked heptapeptide substrate to produce A47934 both in vivo and in vitro. Incubation of purified His6-StaL with various substrates in vitro revealed substrate specificity and yielded two sulfo-glycopeptide antibiotics: sulfo-teicoplanin aglycone and sulfo-teicoplanin. Quantification of the antibacterial activity of desulfo-A47934, A47934, teicoplanin, and sulfo-teicoplanin demonstrated that sulfation slightly increased the minimum inhibitory concentration. This unique modification by sulfation expands glycopeptide diversity with potential application for the development of new antibiotics." @default.
• W2029384328 created "2016-06-24" @default.
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• W2029384328 date "2006-02-01" @default.
• W2029384328 modified "2023-10-16" @default.
• W2029384328 title "Biosynthesis of Sulfated Glycopeptide Antibiotics by Using the Sulfotransferase StaL" @default.
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• W2029384328 doi "https://doi.org/10.1016/j.chembiol.2005.12.003" @default.
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