Construction of a pathway to C50-ε-carotene | Zendy

Yusuke Otani | Zendy; Takashi Maoka | Zendy; Shigeko KawaiNoma | Zendy; Kyoichi Saito | Zendy; Daisuke Umeno | Zendy

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Construction of a pathway to C50-ε-carotene

Author(s) -

Yusuke Otani,

Takashi Maoka,

Shigeko KawaiNoma,

Kyoichi Saito,

Daisuke Umeno

Publication year - 2019

Publication title -

plos one

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.99

H-Index - 332

ISSN - 1932-6203

DOI - 10.1371/journal.pone.0216729

Subject(s) - cyclase , lycopene , context (archaeology) , enzyme , biochemistry , arabidopsis , carotene , substrate specificity , biology , arabidopsis thaliana , chemistry , carotenoid , botany , gene , paleontology , mutant

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 C 50 -lycopene, 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 C 50 -lycopene. Interestingly, we found that it functions as a two-end cyclase in a C 50 context. Based on this observation, a possible model for substrate discrimination of this enzyme is proposed.

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