Open AccessConstruction of a pathway to C50-ε-carotene
Author(s) -
Yusuke Otani,
Takashi Maoka,
Shigeko Kawai-Noma,
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.