Crystal structures of plant uridine diphosphate-dependent glycosyltransferases.
- Author:
Heshu LÜ
;
Feiyan XUE
;
Chunmei LIU
;
Mingfeng YANG
;
Lanqing MA
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Glycosylation;
Glycosyltransferases;
chemistry;
Phylogeny;
Plant Proteins;
chemistry;
Plants;
enzymology;
Protein Structure, Tertiary;
Substrate Specificity;
Uridine Diphosphate;
chemistry
- From:
Chinese Journal of Biotechnology
2014;30(6):838-847
- CountryChina
- Language:Chinese
-
Abstract:
Glycosyltransferases (GTs) catalyze the transfer of a sugar residue of an activated sugar donor to an acceptor molecule. Many families 1 GTs utilize an uridine diphosphate (UDP) activated sugar as donor in the glycosylation reaction, and most of these belong to a group of GTs referred to as the UGTs. The relationship between the degree of amino acid sequence identity and substrate specificity of the plant UGTs is highly complicated, and the prediction of substrate specificity based on phylogenetic analyses need to be improved by more biochemical characterization. This review summarizes the three dimensional structures of plant UGTs published in the Protein Data Bank (PDB), including the detailed substrate interactions with the sugar and receptor binding pockets and mutational analyses of some critical amino acids. It will be helpful for biochemical characterization the substrate specificity of the individual UGT, and lay the foundation for the enzymatic and genetic manipulation of plant UGTs in the future.
