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- W2023943027 endingPage "1090" @default.
- W2023943027 startingPage "1079" @default.
- W2023943027 abstract "Prenyltransferases (PTSs) are involved in the biosynthesis of terpenes with diverse functions. Here, a novel PTS from Arabidopsis (Arabidopsis thaliana) is identified as a trans-type polyprenyl pyrophosphate synthase (AtPPPS), which forms a trans-double bond during each homoallylic substrate condensation, rather than a homomeric C10-geranyl pyrophosphate synthase as originally proposed. Biochemical and genetic complementation analyses indicate that AtPPPS synthesizes C25 to C45 medium/long-chain products. Its close relationship to other long-chain PTSs is also uncovered by phylogenetic analysis. A mutant of contiguous surface polar residues was produced by replacing four charged surface amino acids with alanines to facilitate the crystallization of the enzyme. The crystal structures of AtPPPS determined here in apo and ligand-bound forms further reveal an active-site cavity sufficient to accommodate the medium/long-chain products. The two monomers in each dimer adopt different conformations at the entrance of the active site depending on the binding of substrates. Taken together, these results suggest that AtPPPS is endowed with a unique functionality among the known PTSs." @default.
- W2023943027 created "2016-06-24" @default.
- W2023943027 creator A5006129823 @default.
- W2023943027 creator A5016567722 @default.
- W2023943027 creator A5065536494 @default.
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- W2023943027 date "2011-01-10" @default.
- W2023943027 modified "2023-10-12" @default.
- W2023943027 title "Structure and Mechanism of an Arabidopsis Medium/Long-Chain-Length Prenyl Pyrophosphate Synthase " @default.
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- W2023943027 doi "https://doi.org/10.1104/pp.110.168799" @default.
- W2023943027 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3046570" @default.
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- W2023943027 hasPublicationYear "2011" @default.
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