The structural basis of oligosaccharide binding by rice BGlu1 beta-glucosidase.

@article{Chuenchor2011TheSB,
  title={The structural basis of oligosaccharide binding by rice BGlu1 beta-glucosidase.},
  author={Watchalee Chuenchor and Salila Pengthaisong and Robert C Robinson and Jirundon Yuvaniyama and Jisnuson Svasti and James R. Ketudat Cairns},
  journal={Journal of structural biology},
  year={2011},
  volume={173 1},
  pages={169-79}
}
Rice BGlu1 β-glucosidase is an oligosaccharide exoglucosidase that binds to six β-(1→4)-linked glucosyl residues in its active site cleft. Here, we demonstrate that a BGlu1 E176Q active site mutant can be effectively rescued by small nucleophiles, such as acetate, azide and ascorbate, for hydrolysis of aryl glycosides in a pH-independent manner above pH5, consistent with the role of E176 as the catalytic acid-base. Cellotriose, cellotetraose, cellopentaose, cellohexaose and laminaribiose are… CONTINUE READING

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