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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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Published in: | PloS one 2019-05, Vol.14 (5), p.e0216729-e0216729 |
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description | 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. |
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Based on this observation, a possible model for substrate discrimination of this enzyme is proposed.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0216729</identifier><identifier>PMID: 31086389</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>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</subject><ispartof>PloS one, 2019-05, Vol.14 (5), p.e0216729-e0216729</ispartof><rights>2019 Otani et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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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 |
title | Construction of a pathway to C50-ε-carotene |
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