The biosynthetic pathway of potato solanidanes diverged from that of spirosolanes due to evolution of a dioxygenase
Ryota Akiyama,
Bunta Watanabe,
Masaru Nakayasu,
Hyoung Jae Lee,
Junpei Kato,
Naoyuki Umemoto,
Toshiya Muranaka,
Kazuki Saito,
Yukihiro Sugimoto and
Masaharu Mizutani ()
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Ryota Akiyama: Kobe University
Bunta Watanabe: Kyoto University
Masaru Nakayasu: Kobe University
Hyoung Jae Lee: Kobe University
Junpei Kato: Kobe University
Naoyuki Umemoto: RIKEN Center for Sustainable Resource Science
Toshiya Muranaka: Osaka University
Kazuki Saito: RIKEN Center for Sustainable Resource Science
Yukihiro Sugimoto: Kobe University
Masaharu Mizutani: Kobe University
Nature Communications, 2021, vol. 12, issue 1, 1-10
Abstract:
Abstract Potato (Solanum tuberosum), a worldwide major food crop, produces the toxic, bitter tasting solanidane glycoalkaloids α-solanine and α-chaconine. Controlling levels of glycoalkaloids is an important focus on potato breeding. Tomato (Solanum lycopersicum) contains a bitter spirosolane glycoalkaloid, α-tomatine. These glycoalkaloids are biosynthesized from cholesterol via a partly common pathway, although the mechanisms giving rise to the structural differences between solanidane and spirosolane remained elusive. Here we identify a 2-oxoglutarate dependent dioxygenase, designated as DPS (Dioxygenase for Potato Solanidane synthesis), that is a key enzyme for solanidane glycoalkaloid biosynthesis in potato. DPS catalyzes the ring-rearrangement from spirosolane to solanidane via C-16 hydroxylation. Evolutionary divergence of spirosolane-metabolizing dioxygenases contributes to the emergence of toxic solanidane glycoalkaloids in potato and the chemical diversity in Solanaceae.
Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21546-0
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DOI: 10.1038/s41467-021-21546-0
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