FEBS Letters
Volume 583, Issue 20 , Pages 3303-3309, 20 October 2009

Structure, mechanism and engineering of plant natural product glycosyltransferases

Edited by Ulf-Ingo Flügge

Plant Biology Division, Samuel Roberts Noble Foundation, 2510 Sam Noble Parkway, Ardmore, OK 73401, United States

Received 17 August 2009; received in revised form 24 September 2009; accepted 25 September 2009. published online 30 September 2009.

Abstract 

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.

Abbreviations: UDP, uridine diphosphate, GT, glycosyltransferase, UGT, uridine diphosphate glycosyltransferase

Keywords: Glycosylation, Deglycosylation, Glycosyltransferase, Plant natural product, Enzyme engineering

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PII: S0014-5793(09)00742-X

doi:10.1016/j.febslet.2009.09.042

FEBS Letters
Volume 583, Issue 20 , Pages 3303-3309, 20 October 2009