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J Am Chem Soc. 2014 Jan 8;136(1):84-7. doi: 10.1021/ja411159k. Epub 2013 Dec 16.

The glycosyltransferase involved in thurandacin biosynthesis catalyzes both O- and S-glycosylation.

Author information

1
Howard Hughes Medical Institute and Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign , 600 South Mathews Avenue, Urbana, Illinois 61801, United States.

Abstract

The S-glycosyltransferase SunS is a recently discovered enzyme that selectively catalyzes the conjugation of carbohydrates to the cysteine thiol of proteins. This study reports the discovery of a second S-glycosyltransferase, ThuS, and shows that ThuS catalyzes both S-glycosylation of the thiol of cysteine and O-glycosylation of the hydroxyl group of serine in peptide substrates. ThuS-catalyzed S-glycosylation is more efficient than O-glycosylation, and the enzyme demonstrates high tolerance with respect to both nucleotide sugars and peptide substrates. The biosynthesis of the putative products of the thuS gene cluster was reconstituted in vitro, and the resulting S-glycosylated peptides thurandacin A and B exhibit highly selective antimicrobial activity toward Bacillus thuringiensis.

PMID:
24325644
PMCID:
PMC3913795
DOI:
10.1021/ja411159k
[Indexed for MEDLINE]
Free PMC Article

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