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- W4387025467 abstract "Abstract Acetylation contributes to the bioactivity of numerous medicinally important natural products. However, little is known about the acetylation on sugar moieties. Here we report a saponin acetyltransferase from Astragalus membranaceus . AmAT7-3 is discovered through a stepwise gene mining approach and characterized as the xylose C3′/C4′- O -acetyltransferse of astragaloside IV ( 1 ). To elucidate its catalytic mechanism, complex crystal structures of AmAT7-3/ 1 and AmAT7-3 A310G / 1 are obtained, which reveal a large active pocket decided by a specific sequence AADAG. Combining with QM/MM computation, the regiospecificity of AmAT7-3 is determined by sugar positioning modulated by surrounding amino acids including #A310 and #L290. Furthermore, a small mutant library is built using semi-rational design, where variants A310G and A310W are found to catalyze specific C3′- O and C4′- O acetylation, respectively. AmAT7-3 and its variants are also employed to acetylate other bioactive saponins. This work expands the understanding of saponin acetyltransferases, and provide efficient catalytic tools for saponin acetylation." @default.
- W4387025467 created "2023-09-26" @default.
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- W4387025467 date "2023-09-25" @default.
- W4387025467 modified "2023-10-17" @default.
- W4387025467 title "Characterization and structure-based protein engineering of a regiospecific saponin acetyltransferase from Astragalus membranaceus" @default.
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- W4387025467 doi "https://doi.org/10.1038/s41467-023-41599-7" @default.
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