Fig. 6: Engineering the catalytic specificity of AbCGT in C-/O-glycosylation. | Nature Communications

Fig. 6: Engineering the catalytic specificity of AbCGT in C-/O-glycosylation.

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

Fig. 6: Engineering the catalytic specificity of AbCGT in C-/O-glycosylation.

a Structure homology modeling of AbCGT. The crystal structure of GgCGT (PDB entry, 6L5R.1) was used as a template for homology modeling. 2-hydroxynaringenin was docked into the putative binding pocket of AbCGT. H19, F89, F90, F194, and V183 are labeled. b Sequence alignment of AbCGT and UGT85H2. The conversed amino acid residues (H19 and V183) in the binding pocket are labeled with red triangles. c Percent conversion of 2-hydroxynaringenin by AbCGT and AbCGT variants. d Exploring the catalytic specificity of variants V183D, V183E and V183P in C-/O-glycosylation. The red, blue columns represent conversion rates of O- and C-glycosylation reactions, respectively. Reactions were performed at pH 7.4 and 30 °C for 12 h. The conversion rates represent mean ± SD of three independent replicates (n = 3).

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