Construction of a pathway to C50ε-carotene

Yusuke Otani, Takashi Maoka, Shigeko Kawai-Noma, Kyoichi Saito, Daisuke Umeno*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Substrate tolerance of bacterial cyclases has been demonstrated in various contexts, but little is known about that of plant cyclases. Here, we tested two plant ε-cyclases to convert C50lycopene, which we previously established by rounds of directed evolution. Unlike bacterial β-cyclases, two-end cyclase from lettuce exhibited complete specificity against this molecule, indicating that this enzyme has some mechanism that exerts size-specificity. Arabidopsis one-end cyclase At-y2 showed detectable activity to C50lycopene. Interestingly, we found that it functions as a two-end cyclase in a C50context. Based on this observation, a possible model for substrate discrimination of this enzyme is proposed.

Original languageEnglish
Article numbere0216729
JournalPloS one
Volume14
Issue number5
DOIs
Publication statusPublished - 2019 May
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

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