A cellulose synthase-derived enzyme catalyses 3-O-glucuronosylation in saponin biosynthesis

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作者：
Soo Yeon Chung
Hikaru Seki
Yukiko Fujisawa
Yoshikazu Shimoda
Susumu Hiraga
Yuhta Nomura
Kazuki Saito
Masao Ishimoto
Toshiya Muranaka
机构：
[1] Osaka University,Department of Biotechnology, Graduate School of Engineering
[2] RIKEN Center for Sustainable Resource Science,Graduate School of Pharmaceutical Sciences
[3] Institute of Crop Science,undefined
[4] NARO,undefined
[5] Institute of Agrobiological Sciences,undefined
[6] NARO,undefined
[7] Chiba University,undefined
[8] RIKEN Center for Sustainable Resource Science,undefined
来源：
Nature Communications | / 11卷
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摘要：
Triterpenoid saponins are specialised metabolites distributed widely in the plant kingdom that consist of one or more sugar moieties attached to triterpenoid aglycones. Despite the widely accepted view that glycosylation is catalysed by UDP-dependent glycosyltransferase (UGT), the UGT which catalyses the transfer of the conserved glucuronic acid moiety at the C-3 position of glycyrrhizin and various soyasaponins has not been determined. Here, we report that a cellulose synthase superfamily-derived glycosyltransferase (CSyGT) catalyses 3-O-glucuronosylation of triterpenoid aglycones. Gene co-expression analyses of three legume species (Glycyrrhiza uralensis, Glycine max, and Lotus japonicus) reveal the involvement of CSyGTs in saponin biosynthesis, and we characterise CSyGTs in vivo using Saccharomyces cerevisiae. CSyGT mutants of L. japonicus do not accumulate soyasaponin, but the ectopic expression of endoplasmic reticulum membrane–localised CSyGTs in a L. japonicus mutant background successfully complement soyasaponin biosynthesis. Finally, we produced glycyrrhizin de novo in yeast, paving the way for sustainable production of high-value saponins.
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