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Novel triterpene oxidizing activity of Arabidopsis thaliana CYP716A subfamily enzymes
Author(s) -
Yasumoto Shuhei,
Fukushima Ery O.,
Seki Hikaru,
Muranaka Toshiya
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12074
Subject(s) - triterpene , biochemistry , monooxygenase , arabidopsis thaliana , subfamily , biology , enzyme , chemistry , cytochrome p450 , stereochemistry , gene , medicine , alternative medicine , pathology , mutant
Triterpenoids have diverse chemical structures and bioactivities. Cytochrome P450 monooxygenases play a key role in their structural diversification. In higher plants, CYP716A subfamily enzymes are triterpene oxidases. In this study, Arabidopsis thaliana CYP716A1 and CYP716A2 were characterized by heterologously expressing them in simple triterpene‐producing yeast strains. In contrast to the C‐28 oxidative activity of CYP716A1 shown in several CYP716A subfamily enzymes, remarkably, CYP716A2 displayed 22α‐hydroxylation activity against α‐amyrin that has not been previously reported, which produces the cytotoxic triterpenoid, 22α‐hydroxy‐α‐amyrin. Our results contribute to the enrichment of the molecular toolbox that allows for the combinatorial biosynthesis of diverse triterpenoids.