Introducing transglycosylation activity into human salivary alpha-amylase (HSA) |
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Authors: | Remenyik Judit Ragunath Chandran Ramasubbu Narayanan Gyémánt Gyöngyi Lipták András Kandra Lili |
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Institution: | Research Group for Carbohydrates, Hungarian Academy of Sciences and University of Debrecen, P.O. Box 55, 4010 Debrecen, Hungary. |
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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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