Download MendeleyMolecular and Structural Characterization of a Promiscuous C-Glycosyltransferase from Trollius chinensis.
He, J.B., Zhao, P., Hu, Z.M., Liu, S., Kuang, Y., Zhang, M., Li, B., Yun, C.H., Qiao, X., Ye, M.(2019) Angew Chem Int Ed Engl 58: 11513-11520
- PubMed: 31163097
- DOI: https://doi.org/10.1002/anie.201905505
- Primary Citation of Related Structures:
6JTD - PubMed Abstract:
Herein, the catalytic promiscuity of TcCGT1, a new C-glycosyltransferase (CGT) from the medicinal plant Trollius chinensis is explored. TcCGT1 could efficiently and regio-specifically catalyze the 8-C-glycosylation of 36 flavones and other flavonoids and could also catalyze the O-glycosylation of diverse phenolics. The crystal structure of TcCGT1 in complex with uridine diphosphate was determined at 1.85 Å resolution. Molecular docking revealed a new model for the catalytic mechanism of TcCGT1, which is initiated by the spontaneous deprotonation of the substrate. The spacious binding pocket explains the substrate promiscuity, and the binding pose of the substrate determines C- or O-glycosylation activity. Site-directed mutagenesis at two residues (I94E and G284K) switched C- to O-glycosylation. TcCGT1 is the first plant CGT with a crystal structure and the first flavone 8-C-glycosyltransferase described. This provides a basis for designing efficient glycosylation biocatalysts.
Organizational Affiliation:
State Key Laboratory of Natural and Biomimetic Drugs & Key Laboratory of Molecular Cardiovascular Sciences of Ministry of Education, School of Pharmaceutical Sciences, Peking University, 38 Xueyuan Road, Beijing, 100191, China.
