Introducing transglycosylation activity into human salivary alpha-amylase (HSA).
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]
Remenyik
Judit
J
Research Group for Carbohydrates, Hungarian Academy of Sciences and University of Debrecen, P.O. Box 55, 4010 Debrecen, Hungary.
Ragunath
Chandran
C
Ramasubbu
Narayanan
N
Gyémánt
Gyöngyi
G
Lipták
András
A
Kandra
Lili
L
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006031:Glycosylation; D006801:Humans; D008320:Maltose / Q000031:analogs & derivatives / Q000096:biosynthesis; D008969:Molecular Sequence Data; D009154:Mutation; D012463:Saliva / Q000201:enzymology*; D013997:Time Factors; D000516:alpha-Amylases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D008320:Maltose; D000516:alpha-Amylases