Rational design of a beta-glycosidase with high regiospecificity for triterpenoid tailoring

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Title
Rational design of a beta-glycosidase with high regiospecificity for triterpenoid tailoring
Author(s)
S J Park; J M Choi; H H Kyeong; Song-Gun Kim; H S Kim
Bibliographic Citation
Chembiochem, vol. 16, no. 5, pp. 854-860
Publication Year
2015
Abstract
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 β-glycosidase with high regiospecificity for triterpenoids. A β-glycosidase with broad substrate specificity was isolated, and its crystal structure was determined at 2.0 A 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.
Keyword
binding modeglycosidesrational designregiospecificityterpenoids
ISSN
1439-4227
Publisher
Wiley
DOI
http://dx.doi.org/10.1002/cbic.201500004
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Biological Resource Center > 1. Journal Articles
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