Expanding the “Terpenome”: Diterpene Synthases Accept GGPP-Ether Substrates

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

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  • Leibniz-Institut für Pflanzenbiochemie, Halle (IPB)
  • Uppsala University
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Details

OriginalspracheEnglisch
Seiten (von - bis)6796-6811
Seitenumfang16
FachzeitschriftACS catalysis
Jahrgang15
Ausgabenummer9
Frühes Online-Datum11 Apr. 2025
PublikationsstatusVeröffentlicht - 2 Mai 2025

Abstract

Three geranylgeranyl pyrophosphate derivatives carrying an ether group at different positions within geranylgeranyl pyrophosphate were employed in biotransformations with five diterpene synthases (CotB2, PvHVS, PaFS, Bnd4 and TXS) derived from plants, bacteria and fungi. A total of six new oxygen-containing diterpenoids were isolated and characterized, deepening our knowledge on the substrate promiscuity of diterpene synthases. In addition, the diterpene synthase PvHVS also accepts an ether derivative of farnesyl pyrophosphate and converts it to the same tetrahydrofuran core as found for the analogous extended GGPP substrate. This result further demonstrates that diterpene synthases also exhibit promiscuity toward truncated unnatural substrates.

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Expanding the “Terpenome”: Diterpene Synthases Accept GGPP-Ether Substrates. / Ravkina, Viktoria; Dräger, Gerald; Droste, Jörn et al.
in: ACS catalysis, Jahrgang 15, Nr. 9, 02.05.2025, S. 6796-6811.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Ravkina V, Dräger G, Droste J, Schwörer S, Hassanin A, Davari MD et al. Expanding the “Terpenome”: Diterpene Synthases Accept GGPP-Ether Substrates. ACS catalysis. 2025 Mai 2;15(9):6796-6811. Epub 2025 Apr 11. doi: 10.1021/acscatal.5c00272
Ravkina, Viktoria ; Dräger, Gerald ; Droste, Jörn et al. / Expanding the “Terpenome” : Diterpene Synthases Accept GGPP-Ether Substrates. in: ACS catalysis. 2025 ; Jahrgang 15, Nr. 9. S. 6796-6811.
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T1 - Expanding the “Terpenome”

T2 - Diterpene Synthases Accept GGPP-Ether Substrates

AU - Ravkina, Viktoria

AU - Dräger, Gerald

AU - Droste, Jörn

AU - Schwörer, Svenja

AU - Hassanin, Ahmed

AU - Davari, Mehdi D.

AU - Kirschning, Andreas

N1 - Publisher Copyright: © 2025 The Authors. Published by American Chemical Society.

PY - 2025/5/2

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N2 - Three geranylgeranyl pyrophosphate derivatives carrying an ether group at different positions within geranylgeranyl pyrophosphate were employed in biotransformations with five diterpene synthases (CotB2, PvHVS, PaFS, Bnd4 and TXS) derived from plants, bacteria and fungi. A total of six new oxygen-containing diterpenoids were isolated and characterized, deepening our knowledge on the substrate promiscuity of diterpene synthases. In addition, the diterpene synthase PvHVS also accepts an ether derivative of farnesyl pyrophosphate and converts it to the same tetrahydrofuran core as found for the analogous extended GGPP substrate. This result further demonstrates that diterpene synthases also exhibit promiscuity toward truncated unnatural substrates.

AB - Three geranylgeranyl pyrophosphate derivatives carrying an ether group at different positions within geranylgeranyl pyrophosphate were employed in biotransformations with five diterpene synthases (CotB2, PvHVS, PaFS, Bnd4 and TXS) derived from plants, bacteria and fungi. A total of six new oxygen-containing diterpenoids were isolated and characterized, deepening our knowledge on the substrate promiscuity of diterpene synthases. In addition, the diterpene synthase PvHVS also accepts an ether derivative of farnesyl pyrophosphate and converts it to the same tetrahydrofuran core as found for the analogous extended GGPP substrate. This result further demonstrates that diterpene synthases also exhibit promiscuity toward truncated unnatural substrates.

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KW - diterpene synthases

KW - diterpenoids

KW - farnesyl pyrophosphates

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