Fig. 6: Key residues for the catalytic activity and specificity of SgUGT94-289-3. | Nature Communications

Fig. 6: Key residues for the catalytic activity and specificity of SgUGT94-289-3.

From: Structural insights into the catalytic selectivity of glycosyltransferase SgUGT94-289-3 towards mogrosides

Fig. 6

a Superposition of M3 and M3E structures. Sugar acceptors are shown in lines. Residues crucial for recognition and binding of sugar acceptors in both pocket 1 and pocket 2 are shown in stick mode. R1-G1 in M3E (green) and R2-G1 in SIA (brown) are filled with green and brown color, respectively. b–e Catalytic activity and specificity of WT and mutated forms of SgUGT94-289-3 after 40 min reaction time. Conversion from M2E to M3 (b), from M3E to SIA (c), from M3 to M4A (d), and from SIA to M5 (e). The activity (%) was measured as substrate consumption (hollow) and the specificity (%) was measured as product yield (solid). b, c represent the case of R1-in substrates, while d, e represent that of R2-in substrates. Data are presented as mean values ± SD (n = 3 biological replicates). The WT enzyme-catalyzed reaction served as the positive control group, while the negative control group consisted of buffer without enzyme or substrates. Source data are provided as a Source Data file.

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