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- W2059180348 abstract "Abstract Glycosynthases—retaining glycosidases mutated at their catalytic nucleophile—catalyze the formation of glycosidic bonds from glycosyl fluorides as donor sugars and various glycosides as acceptor sugars. Here the first glycosynthase derived from a family 35 β‐galactosidase is described. The Glu→Gly mutant of BgaC from Bacillus circulans (BgaC‐E233G) catalyzed regioselective galactosylation at the 3‐position of the sugar acceptors with α‐galactosyl fluoride as the donor. Transfer to 4‐nitophenyl α‐ D ‐ N ‐acetyl‐glucosaminide and α‐ D ‐ N ‐acetylgalactosaminide yielded 4‐nitophenyl α‐lacto‐ N ‐biose and α‐galacto‐ N ‐biose, respectively, in high yields (up to 98 %). Kinetic analysis revealed that the high affinity of the acceptors contributed mostly to the BgaC‐E233G‐catalyzed transglycosylation. BgaC‐E233G showed no activity with β‐(1,3)‐linked disaccharides as acceptors, thus suggesting that this enzyme can be used in “one‐pot synthesis” of LNB‐ or GNB‐containing glycans." @default.
- W2059180348 created "2016-06-24" @default.
- W2059180348 creator A5007025306 @default.
- W2059180348 creator A5043301712 @default.
- W2059180348 date "2014-01-23" @default.
- W2059180348 modified "2023-10-16" @default.
- W2059180348 title "Characterization of a Galactosynthase Derived from<i>Bacillus circulans</i>β-Galactosidase: Facile Synthesis of<scp>D</scp>-Lacto- and<scp>D</scp>-Galacto-<i>N</i>-bioside" @default.
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- W2059180348 doi "https://doi.org/10.1002/cbic.201300699" @default.
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