Fig. 6: Investigation of the catalytic specificity and the mechanism for LbUGT1. | Nature Communications

Fig. 6: Investigation of the catalytic specificity and the mechanism for LbUGT1.

From: Functional and structural dissection of glycosyltransferases underlying the glycodiversity of wolfberry-derived bioactive ingredients lycibarbarspermidines

Fig. 6

A Proposed catalytic mechanism for the 4”/3’-O-glycosylation of LbUGT1; B, C The binding mode 1 and binding mode 2 of LbUGT1 with the ligand 1 shown in cyan and UDP-Glc shown in yellow, the hydrogen bond was shown with the purple dash; D, E Time evolutions of the two key distances between the hydroxyl H atom of substrate and the N atom of the catalytic histidine (d1) and between the hydroxyl O atom of substrate and the acetal C atom of UDP-Glc (d2) in the 50 ns MD simulations of wild type LbUGT1 and mutant Y389A in two binding modes shown in B and C, respectively; F Exploring the catalytic specificity of variants of LbUGT1-5. Data represent mean ± SD (n = 3). The source data underlying Fig. 6F are provided in a Source Data file.

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