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- W3159073350 abstract "Fsa2 and Phm7 are a unique pair of pericyclases catalyzing [4 + 2] cycloaddition reactions with reverse stereoselectivities in the biosynthesis of equisetin and phomasetin, both of which are potent HIV-1 integrase inhibitors. We here solve the crystal structures of Fsa2 and Phm7, both of which possess unusual “two-β barrel” folds. Different residues are evident between the active sites of Fsa2 and Phm7, and modeling experiments provide key structural information determining the reverse stereoselectivities. These results provide a better understanding of how natural pericyclases control the catalytic stereoselectivities and benefit the protein engineering in future." @default.
- W3159073350 created "2021-05-10" @default.
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- W3159073350 date "2021-05-06" @default.
- W3159073350 modified "2023-10-15" @default.
- W3159073350 title "Crystal Structures of Fsa2 and Phm7 Catalyzing [4 + 2] Cycloaddition Reactions with Reverse Stereoselectivities in Equisetin and Phomasetin Biosynthesis" @default.
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- W3159073350 doi "https://doi.org/10.1021/acsomega.1c01593" @default.
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