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- W3161542819 endingPage "2275" @default.
- W3161542819 startingPage "2261" @default.
- W3161542819 abstract "Covering: up to May 2020Oxidosqualene cyclases (OSCs) catalyze one of the most complex polycyclization reactions in nature, using the linear 2,3-oxidosqualene to generate an array of triterpene skeletons in plants. Despite the structural diversity of the products, the protein sequences of plant OSCs are highly conserved, where a few key amino acids could govern the product selectivity. Due to the absence of crystal structures, site-directed mutagenesis and substrate structural modification become key approaches to understand the cyclization mechanism. In this review, 98 mutation sites in 25 plant OSCs have been summarized, and the conserved key residues have been identified by sequence alignment. Structure-function relationships are further discussed. Meanwhile, the substrate selectivity has been summarized to probe the active site cavity of plant OSCs. A total of 77 references are included." @default.
- W3161542819 created "2021-05-24" @default.
- W3161542819 creator A5005296833 @default.
- W3161542819 creator A5042268014 @default.
- W3161542819 creator A5061537073 @default.
- W3161542819 creator A5091186725 @default.
- W3161542819 date "2021-01-01" @default.
- W3161542819 modified "2023-10-17" @default.
- W3161542819 title "Site-directed mutagenesis and substrate compatibility to reveal the structure–function relationships of plant oxidosqualene cyclases" @default.
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- W3161542819 doi "https://doi.org/10.1039/d1np00015b" @default.
- W3161542819 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33988197" @default.
- W3161542819 hasPublicationYear "2021" @default.
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