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Structure, mechanism and engineering of plant natural product glycosyltransferases
Author(s) -
Wang Xiaoqiang
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.09.042
Subject(s) - glycosylation , glycosyltransferase , natural product , chemistry , mechanism (biology) , biochemistry , substrate (aquarium) , chemical biology , protein engineering , substrate specificity , enzyme , biology , ecology , philosophy , epistemology
Glycosylation is a key mechanism in determining chemical complexity and diversity of plant natural products, and influencing their chemical properties and bioactivities. Uridine diphosphate glycosyltransferases (UGTs) are the central players in these glycosylation processes for decorating natural products with sugars. Crystal structures of plant UGTs have revealed their exquisite architectures and provided the structural basis for understanding their catalytic mechanism and substrate specificity. Structure‐based UGT engineering can alter substrate specificity; compromise or enhance catalytic efficiency; and confer reversibility to the glycosylation reaction. This review highlights the structural insights on plant UGTs and successes in glycosylation engineering.