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231225s2020 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/eraa353
|2 doi
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|a pubmed24n1043.xml
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|a (DE-627)NLM312967632
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|a (NLM)32720987
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Ding, Guangyu
|e verfasserin
|4 aut
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| 245 |
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|a Origin and functional differentiation of (E)-β-ocimene synthases reflect the expansion of monoterpenes in angiosperms
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|c 2020
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 14.05.2021
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|a Date Revised 14.05.2021
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
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|a The acquisition of new metabolic activities is a major force driving evolution. We explored, from the perspectives of gene family expansion and the evolutionary adaptability of proteins, how new functions have arisen in which terpene synthases diverged. Monoterpenoids are diverse natural compounds that can be divided into cyclic and acyclic skeleton forms according to their chemical structure. We demonstrate, through phylogenetic reconstructions and genome synteny analyses, that the (E)-β-ocimene synthases, which are acyclic monoterpene synthases (mTPSs), appear to have arisen several times in independent lineages during plant evolution. Bioinformatics analyses and classical mutation experiments identified four sites (I388, F420, S446, and F485) playing important roles in the neofunctionalization of mTPSs. Incubation of neryl diphosphate with Salvia officinalis 1,8-cineole synthase (SCS) and mutated proteins show that these four sites obstruct the isomerization of geranyl diphosphate. Quantum mechanical/molecular mechanical molecular dynamics simulations of models of SCS, SCSY420F/I446S, and SCSN338I/Y420F/I446S/L485F with (3R)-linalyl diphosphate suggest that mutations changed the configuration of the intermediate to obtain new activities. These results provide new perspectives on the evolution of mTPSs, explain the convergent evolution of (E)-β-ocimene synthases at the molecular level, and identify key residues to control the specificity of engineered mTPSs
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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| 650 |
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|a (E)-β-ocimene
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| 650 |
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4 |
|a 1,8-cineole
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| 650 |
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|a Ancestral sequence reconstruction
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| 650 |
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|a QM/MM MD
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| 650 |
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|a chemical diversity
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|a convergent evolution
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|a monoterpene cyclization
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| 650 |
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|a Acyclic Monoterpenes
|2 NLM
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| 650 |
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|a Alkenes
|2 NLM
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| 650 |
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|a Monoterpenes
|2 NLM
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| 650 |
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|a beta-ocimene
|2 NLM
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| 650 |
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|a 13877-91-3
|2 NLM
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| 650 |
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|a Alkyl and Aryl Transferases
|2 NLM
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| 650 |
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|a EC 2.5.-
|2 NLM
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| 700 |
1 |
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|a Zhang, Shaoyu
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ma, Bi
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Liang, Jiubo
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Han
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Luo, Yiwei
|e verfasserin
|4 aut
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| 700 |
1 |
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|a He, Ningjia
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 71(2020), 20 vom: 22. Okt., Seite 6571-6586
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
1 |
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|g volume:71
|g year:2020
|g number:20
|g day:22
|g month:10
|g pages:6571-6586
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| 856 |
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|u http://dx.doi.org/10.1093/jxb/eraa353
|3 Volltext
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|d 71
|j 2020
|e 20
|b 22
|c 10
|h 6571-6586
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