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Fig. S1. Expression and purification of recombinant UGT74B1 and truncated UGT74B1ΔC. (a) SDS-PAGE analysis of recombinant UGT74B1 and truncated UGT74B1ΔC. Separations of total proteins from uninduced (U) and induced (I) Escherichia coli cells, and of proteins purified under denaturing conditions (P) are shown. (b) SDS-Page analysis of recombinant UGT74B1 purified under native conditions.

Fig. S2. Mass spectra of the phenylacetothiohydroximic acid substrate (PATH) and the dsBGS product of the UGT74B1-catalyzed glucosylation reaction. (a) Mass spectrum of the PATH substrate. [M-H]- (m/z 166), [2M-H]- (m/z 332), [M-H]2-Na+ (m/z 354). (b) Mass spectrum of the dsBGS product peak of a UGT74B1-catalyzed reaction. The collected product peak gives rise to dsBGS (m/z 328), thioglucose (m/z 195), and PATH (m/z 166).

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