Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites

© The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 67(2016), 21 vom: 03. Nov., Seite 5993-6005
1. Verfasser: Bruno, Mark (VerfasserIn)
Weitere Verfasser: Koschmieder, Julian, Wuest, Florian, Schaub, Patrick, Fehling-Kaschek, Mirjam, Timmer, Jens, Beyer, Peter, Al-Babili, Salim
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2016
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Apocarotenoids CCD4 CCD7 carotenoid cleavage dioxygenase carotenoids retrograde signaling Arabidopsis Proteins Xanthophylls mehr... Carotenoids 36-88-4 CCD4 protein, Arabidopsis EC 1.- CCD7 protein, Arabidopsis EC 1.13.11.- Dioxygenases
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100 1 |a Bruno, Mark  |e verfasserin  |4 aut 
245 1 0 |a Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites 
264 1 |c 2016 
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500 |a Date Completed 13.11.2017 
500 |a Date Revised 13.11.2018 
500 |a published: Print-Electronic 
500 |a ErratumIn: J Exp Bot. 2017 Nov 2;68(18):5249. - PMID 29106620 
500 |a Citation Status MEDLINE 
520 |a © The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology. 
520 |a The Arabidopsis carotenoid cleavage dioxygenase 4 (AtCCD4) is a negative regulator of the carotenoid content of seeds and has recently been suggested as a candidate for the generation of retrograde signals that are thought to derive from the cleavage of poly-cis-configured carotene desaturation intermediates. In this work, we investigated the activity of AtCCD4 in vitro and used dynamic modeling to determine its substrate preference. Our results document strict regional specificity for cleavage at the C9-C10 double bond in carotenoids and apocarotenoids, with preference for carotenoid substrates and an obstructing effect on hydroxyl functions, and demonstrate the specificity for all-trans-configured carotenes and xanthophylls. AtCCD4 cleaved substrates with at least one ionone ring and did not convert acyclic carotene desaturation intermediates, independent of their isomeric states. These results do not support a direct involvement of AtCCD4 in generating the supposed regulatory metabolites. In contrast, the strigolactone biosynthetic enzyme AtCCD7 converted 9-cis-configured acyclic carotenes, such as 9-cis-ζ-carotene, 9'-cis-neurosporene, and 9-cis-lycopene, yielding 9-cis-configured products and indicating that AtCCD7, rather than AtCCD4, is the candidate for forming acyclic retrograde signals 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Apocarotenoids 
650 4 |a CCD4 
650 4 |a CCD7 
650 4 |a carotenoid cleavage dioxygenase 
650 4 |a carotenoids 
650 4 |a retrograde signaling 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Xanthophylls  |2 NLM 
650 7 |a Carotenoids  |2 NLM 
650 7 |a 36-88-4  |2 NLM 
650 7 |a CCD4 protein, Arabidopsis  |2 NLM 
650 7 |a EC 1.-  |2 NLM 
650 7 |a CCD7 protein, Arabidopsis  |2 NLM 
650 7 |a EC 1.13.11.-  |2 NLM 
650 7 |a Dioxygenases  |2 NLM 
650 7 |a EC 1.13.11.-  |2 NLM 
700 1 |a Koschmieder, Julian  |e verfasserin  |4 aut 
700 1 |a Wuest, Florian  |e verfasserin  |4 aut 
700 1 |a Schaub, Patrick  |e verfasserin  |4 aut 
700 1 |a Fehling-Kaschek, Mirjam  |e verfasserin  |4 aut 
700 1 |a Timmer, Jens  |e verfasserin  |4 aut 
700 1 |a Beyer, Peter  |e verfasserin  |4 aut 
700 1 |a Al-Babili, Salim  |e verfasserin  |4 aut 
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