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An algal enzyme required for biosynthesis of the most abundant marine carotenoids.

  • Author(s): Dautermann, O
  • Lyska, D
  • Andersen-Ranberg, J
  • Becker, M
  • Fröhlich-Nowoisky, J
  • Gartmann, H
  • Krämer, LC
  • Mayr, K
  • Pieper, D
  • Rij, LM
  • Wipf, HM-L
  • Niyogi, KK
  • Lohr, M
  • et al.
Abstract

Fucoxanthin and its derivatives are the main light-harvesting pigments in the photosynthetic apparatus of many chromalveolate algae and represent the most abundant carotenoids in the world's oceans, thus being major facilitators of marine primary production. A central step in fucoxanthin biosynthesis that has been elusive so far is the conversion of violaxanthin to neoxanthin. Here, we show that in chromalveolates, this reaction is catalyzed by violaxanthin de-epoxidase-like (VDL) proteins and that VDL is also involved in the formation of other light-harvesting carotenoids such as peridinin or vaucheriaxanthin. VDL is closely related to the photoprotective enzyme violaxanthin de-epoxidase that operates in plants and most algae, revealing that in major phyla of marine algae, an ancient gene duplication triggered the evolution of carotenoid functions beyond photoprotection toward light harvesting.

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