Introducing Transglycosylation Activity into Human Salivary α-Amylase (HSA)

Judit Remenyik, Chandran Ragunath, Narayanan Ramasubbu, Gyöngyi Gyémánt, András Lipták, Lili Kandra

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


(Equation Presented) Synthesis of 4-nitrophenyl 1-thio-β-D-maltoside, maltotrioside, and maltotetraoside in yields up to 60% has been achieved by a Tyr151Met (Y151M) mutant of human salivary α-amylase. Y151M is capable of transferring maltose and maltotriose residues from a maltotetraose donor onto different p-nitrophenyl glycosides. 1H and 13C 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 α(1-4)glycosidic bond, exclusively.

Original languageEnglish (US)
Pages (from-to)4895-4898
Number of pages4
JournalOrganic letters
Issue number25
StatePublished - Dec 11 2003

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry


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