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Updated: Aug 29, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Introducing transglycosylation activity into human salivary alpha-amylase (HSA)
Judit Remenyik1, Chandran Ragunath, Narayanan Ramasubbu
1Research Group for Carbohydrates, Hungarian Academy of Sciences and University of Debrecen, P.O. Box 55, 4010 Debrecen, Hungary.
Abstract:
Synthesis of 4-nitrophenyl 1-thio-beta-D-maltoside, maltotrioside, and maltotetraoside in yields up to 60% has been achieved by a Tyr151Met (Y151M) mutant of human salivary alpha-amylase. Y151M is capable of transferring maltose and maltotriose residues from a maltotetraose donor onto different p-nitrophenyl glycosides. (1)H and (13)C NMR studies revealed that the mutated enzyme preserved the stereo- and regioselectivity. The glycosylation took place at position 4 of the glycosyl acceptor, forming the alpha(1-4)glycosidic bond, exclusively. [reaction: see text]
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