On the substrate- and stereospecificity of the plant carotenoid cleavage dioxygenase 7

Handle URI:
http://hdl.handle.net/10754/563521
Title:
On the substrate- and stereospecificity of the plant carotenoid cleavage dioxygenase 7
Authors:
Bruno, Mark; Hofmann, Manuel; Vermathen, Martina; Alder, Adrian; Beyer, Peter D.; Al-Babili, Salim ( 0000-0003-4823-2882 )
Abstract:
Strigolactones are phytohormones synthesized from carotenoids via a stereospecific pathway involving the carotenoid cleavage dioxygenases 7 (CCD7) and 8. CCD7 cleaves 9-cis-β-carotene to form a supposedly 9-cis-configured β-apo-10′-carotenal. CCD8 converts this intermediate through a combination of yet undetermined reactions into the strigolactone-like compound carlactone. Here, we investigated the substrate and stereo-specificity of the Arabidopsis and pea CCD7 and determined the stereo-configuration of the β-apo-10′-carotenal intermediate by using Nuclear Magnetic Resonance Spectroscopy. Our data unequivocally demonstrate the 9-cis-configuration of the intermediate. Both CCD7s cleave different 9-cis-carotenoids, yielding hydroxylated 9-cis-apo-10′-carotenals that may lead to hydroxylated carlactones, but show highest affinity for 9-cis-β-carotene. © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Center for Desert Agriculture; Bioscience Program
Publisher:
Wiley-Blackwell
Journal:
FEBS Letters
Issue Date:
May-2014
DOI:
10.1016/j.febslet.2014.03.041
PubMed ID:
24685691
Type:
Article
ISSN:
00145793
Sponsors:
This work was supported by the German Research Foundation (DFG) Grant AL 892/1-4 and by the EU (METAPRO; FP7 KBBE-2009-3-1-01).
Appears in Collections:
Articles; Bioscience Program; Center for Desert Agriculture; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorBruno, Marken
dc.contributor.authorHofmann, Manuelen
dc.contributor.authorVermathen, Martinaen
dc.contributor.authorAlder, Adrianen
dc.contributor.authorBeyer, Peter D.en
dc.contributor.authorAl-Babili, Salimen
dc.date.accessioned2015-08-03T11:53:33Zen
dc.date.available2015-08-03T11:53:33Zen
dc.date.issued2014-05en
dc.identifier.issn00145793en
dc.identifier.pmid24685691en
dc.identifier.doi10.1016/j.febslet.2014.03.041en
dc.identifier.urihttp://hdl.handle.net/10754/563521en
dc.description.abstractStrigolactones are phytohormones synthesized from carotenoids via a stereospecific pathway involving the carotenoid cleavage dioxygenases 7 (CCD7) and 8. CCD7 cleaves 9-cis-β-carotene to form a supposedly 9-cis-configured β-apo-10′-carotenal. CCD8 converts this intermediate through a combination of yet undetermined reactions into the strigolactone-like compound carlactone. Here, we investigated the substrate and stereo-specificity of the Arabidopsis and pea CCD7 and determined the stereo-configuration of the β-apo-10′-carotenal intermediate by using Nuclear Magnetic Resonance Spectroscopy. Our data unequivocally demonstrate the 9-cis-configuration of the intermediate. Both CCD7s cleave different 9-cis-carotenoids, yielding hydroxylated 9-cis-apo-10′-carotenals that may lead to hydroxylated carlactones, but show highest affinity for 9-cis-β-carotene. © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.en
dc.description.sponsorshipThis work was supported by the German Research Foundation (DFG) Grant AL 892/1-4 and by the EU (METAPRO; FP7 KBBE-2009-3-1-01).en
dc.publisherWiley-Blackwellen
dc.subjectApocarotenoiden
dc.subjectCarlactoneen
dc.subjectCarotenoiden
dc.subjectCarotenoid cleavage dioxygenaseen
dc.subjectStrigolactoneen
dc.titleOn the substrate- and stereospecificity of the plant carotenoid cleavage dioxygenase 7en
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentCenter for Desert Agricultureen
dc.contributor.departmentBioscience Programen
dc.identifier.journalFEBS Lettersen
dc.contributor.institutionAlbert-Ludwigs University of Freiburg, Faculty of Biology, Schaenzlestr. 1, D-79104 Freiburg, Germanyen
dc.contributor.institutionDepartment of Chemistry and Biochemistry, University of Bern, 3012 Bern, Switzerlanden
kaust.authorAl-Babili, Salimen

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