Fig. 1: Probing the aglycon acceptor and sugar donor promiscuity of AbCGT. | Nature Communications

Fig. 1: Probing the aglycon acceptor and sugar donor promiscuity of AbCGT.

From: Exploring and applying the substrate promiscuity of a C-glycosyltransferase in the chemo-enzymatic synthesis of bioactive C-glycosides

Fig. 1: Probing the aglycon acceptor and sugar donor promiscuity of AbCGT.

a Percent conversion of each aglycon acceptor with AbCGT. The aglycon acceptors and sugar donors are listed based on the structural scaffolds shown in part b and c. The red, blue, light blue, green, and black columns represent conversion rates of O-, mono-C-, di-C-, S-, and N-glycosylation reactions, respectively. b The structures of the aglycon acceptors and corresponding glycosylated products prepared from the scale-up enzymatic reactions. c The structures of sugar donors used in this work. The sugar donor promiscuity was tested with phloretin (17) as the acceptor. ND not detected. Experiments were performed at pH 7.4 and 30 °C for up to 12 h. Conversion rates represent mean ± SD of three independent replicates (n = 3).

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