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- W4386504162 abstract "Plant-derived diterpene synthases (PdiTPSs) play a critical role in the formation of structurally and functionally diverse diterpenoids. However, the specificity or promiscuity of PdiTPSs remains unclear. In order to gain more understanding of this, the sequences of 199 functionally characterized PdiTPSs and their corresponding 3D structures were collected and manually corrected. Then, the correlations among sequences, domains, structures and their corresponding products were comprehensively analyzed. However, those features alone was insufficient for ef-fective product-specific classification of PdiTPSs as these methods could not establish a clear mapping between the enzymes and products. Nevertheless, local structural analysis can identify residues that have been experimentally proven to influence product outcomes through mutagenesis, and these residues exhibit conservation in spatial positioning and physicochemical properties. And aromatic residues surrounding the substrate exhibited selectivity towards its chemical structure. Specifically, tryptophan (W) was preferentially located around the linear substrate geranylgeranyl pyrophosphate (GGPP), while phenylalanine (F) and tyrosine (Y) were preferentially located around the initial cyclized diterpene intermediate. This analysis revealed the functional space of residues surrounding the substrate of PdiTPSs, most of which have not been experimentally explored. These findings provide guidance for screening specific residues for mutation studies to change the catalytic products of PdiTPSs." @default.
- W4386504162 created "2023-09-08" @default.
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- W4386504162 date "2023-09-07" @default.
- W4386504162 modified "2023-09-28" @default.
- W4386504162 title "AlphaFold2 Empowers Product Specificity Analysis in Plant-derived Diterpene Synthases" @default.
- W4386504162 doi "https://doi.org/10.20944/preprints202309.0431.v1" @default.
- W4386504162 hasPublicationYear "2023" @default.
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