Construction of a pathway to C50-ε-carotene

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 C50-lycopene, which we previously established by rounds of directed evolution. Unlike bacterial β-cyclases, two-end c...

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Bibliographic Details
Published in:PloS one 2019-05, Vol.14 (5), p.e0216729-e0216729
Main Authors: Otani, Yusuke, Maoka, Takashi, Kawai-Noma, Shigeko, Saito, Kyoichi, Umeno, Daisuke
Format: Article
Language:English
Subjects:
Arabidopsis - enzymology
Arabidopsis - genetics
Binding sites
Biology and Life Sciences
Biosynthesis
Biotechnology
Carotene
Carotenoids
Carotenoids - chemistry
Carotenoids - metabolism
Cloning
Directed evolution
E coli
Enzymes
Experiments
Lettuce
Lyases - genetics
Lyases - metabolism
Lycopene
Metabolic Engineering
Physical Sciences
Plasmids
Research and Analysis Methods
Substrate Specificity
Substrates
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Summary: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 C50-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 C50-lycopene. Interestingly, we found that it functions as a two-end cyclase in a C50 context. Based on this observation, a possible model for substrate discrimination of this enzyme is proposed.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0216729