Structure, mechanism and engineering of plant natural product glycosyltransferases.
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.
Wang
Xiaoqiang
X
Plant Biology Division, Samuel Roberts Noble Foundation, 2510 Sam Noble Parkway, Ardmore, OK 73401, United States. xwang@noble.org
D000595:Amino Acid Sequence; D000818:Animals; D001688:Biological Products / Q000737:chemistry / Q000235:genetics; D018360:Crystallography, X-Ray; D006031:Glycosylation; D016695:Glycosyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010944:Plants / Q000737:chemistry / Q000378:metabolism; D015202:Protein Engineering; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D001688:Biological Products; D016695:Glycosyltransferases