期刊
CHEMBIOCHEM
卷 16, 期 5, 页码 854-860出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201500004
关键词
binding mode; glycosides; rational design; regiospecificity; terpenoids
资金
- National Research Foundation (NRF) from Minisry of Science, ICT and Future Planing [2014-004198]
- Brain Korea 21 - Ministry of Education
Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types of cancer. Sugar-hydrolyzing enzymes with high substrate specificity would be far more efficient than other methods for the synthesis of such specialty triterpenoids, but they are yet to be developed. Here we present a strategy to rationally design a -glycosidase with high regiospecificity for triterpenoids. A -glycosidase with broad substrate specificity was isolated, and its crystal structure was determined at 2.0 angstrom resolution. Based on the product profiles and substrate docking simulations, we modeled the substrate binding modes of the enzyme. From the model, the substrate binding cleft of the enzyme was redesigned in a manner that preferentially hydrolyzes glycans at specific glycosylation sites of triterpenoids. The designed mutants were shown to produce a variety of specialty triterpenoids with high purity.
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