@article { ISI:000458826800012,
	title = {Facile Formation of -thioGlcNAc Linkages to Thiol-Containing Sugars, Peptides, and Proteins using a Mutant GH20 Hexosaminidase},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {58},
	number = {6},
	year = {2019},
	month = {FEB 4},
	pages = {1632-1637},
	abstract = {Thioglycosides are hydrolase-resistant mimics of O-linked glycosides that can serve as valuable probes for studying the role of glycosides in biological processes. The development of an efficient, enzyme-mediated synthesis of thioglycosides, including S-GlcNAcylated proteins, is reported, using a thioglycoligase derived from a GH20 hexosaminidase from Streptomyces plicatus in which the catalytic acid/base glutamate has been mutated to an alanine (SpHex E314A). This robust, easily-prepared, engineered enzyme uses GlcNAc and GalNAc donors and couples them to a remarkably diverse set of thiol acceptors. Thioglycoligation using 3-, 4-, and 6-thiosugar acceptors from a variety of sugar families produces S-linked disaccharides in nearly quantitative yields. The set of possible thiol acceptors also includes cysteine-containing peptides and proteins, rendering this mutant enzyme a promising catalyst for the production of thio analogues of biologically important GlcNAcylated peptides and proteins.},
	issn = {1433-7851},
	doi = {10.1002/anie.201809928},
	author = {Tegl, Gregor and Hanson, John and Chen, Hong-Ming and Kwan, David H. and Santana, Andres G. and Withers, Stephen G.}
}
