Functional characterization of a C -glycosyltransferase from Pueraria lobata with dual-substrate selectivity.

We report a C -glycosyltransferase PlCGT from Pueraria lobata . PlCGT exhibits efficient C -glycosylation activities toward two types of substrates (isoflavones and phloroglucinol derivatives). Homology modelling reveals that a narrow hydrophobic pocket is responsible for its substrate selectivity. An unusual Asn16-Asp124 dyad in the pocket may mediate the S N 2-like mechanism in C -glycosylation.