TY - JOUR
T1 - Construction of a pathway to C50ε-carotene
AU - Otani, Yusuke
AU - Maoka, Takashi
AU - Kawai-Noma, Shigeko
AU - Saito, Kyoichi
AU - Umeno, Daisuke
N1 - Funding Information:
This work was supported by JSPS KAKENHI Grants 15H04189, 15K14228, and 16K21725, the Hamaguchi Foundation for the Advancement of Biochemistry, the Futaba Electronics Memorial Foundation, and the Shorai Foundation for Science and Technology. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Publisher Copyright:
© 2019 Otani et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
PY - 2019/5
Y1 - 2019/5
N2 - 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.
AB - 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.
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U2 - 10.1371/journal.pone.0216729
DO - 10.1371/journal.pone.0216729
M3 - Article
C2 - 31086389
AN - SCOPUS:85065846427
VL - 14
JO - PLoS One
JF - PLoS One
SN - 1932-6203
IS - 5
M1 - e0216729
ER -