Tomato carotenoid cleavage dioxygenases 1A and 1B: Relaxed double bond specificity leads to a plenitude of dialdehydes, mono-apocarotenoids and isoprenoid volatiles

Handle URI:
http://hdl.handle.net/10754/334629
Title:
Tomato carotenoid cleavage dioxygenases 1A and 1B: Relaxed double bond specificity leads to a plenitude of dialdehydes, mono-apocarotenoids and isoprenoid volatiles
Authors:
Ilg, Andrea; Bruno, Mark; Beyer, Peter; Al-Babili, Salim ( 0000-0003-4823-2882 )
Abstract:
The biosynthetic processes leading to many of the isoprenoid volatiles released by tomato fruits are still unknown, though previous reports suggested a clear correlation with the carotenoids contained within the fruit. In this study, we investigated the activity of the tomato (Solanum lycopersicum) carotenoid cleavage dioxygenase (SlCCD1B), which is highly expressed in fruits, and of its homolog SlCCD1A. Using in vitro assays performed with purified recombinant enzymes and by analyzing products formed by the two enzymes in carotene-accumulating Escherichia coli strains, we demonstrate that SlCCD1A and, to a larger extent, SlCCD1B, have a very relaxed specificity for both substrate and cleavage site, mediating the oxidative cleavage of cis- and all-. trans-carotenoids as well as of different apocarotenoids at many more double bonds than previously reported. This activity gives rise to a plenitude of volatiles, mono-apocarotenoids and dialdehyde products, including cis-pseudoionone, neral, geranial, and farnesylacetone. Our results provide a direct evidence for a carotenoid origin of these compounds and point to CCD1s as the enzymes catalyzing the formation of the vast majority of tomato isoprenoid volatiles, many of which are aroma constituents. © 2014 The Authors.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Center for Desert Agriculture
Citation:
Ilg A, Bruno M, Beyer P, Al-Babili S (2014) Tomato carotenoid cleavage dioxygenases 1A and 1B: Relaxed double bond specificity leads to a plenitude of dialdehydes, mono-apocarotenoids and isoprenoid volatiles. FEBS Open Bio 4: 584-593. doi:10.1016/j.fob.2014.06.005.
Publisher:
Wiley-Blackwell
Journal:
FEBS Open Bio
Issue Date:
25-Jun-2014
DOI:
10.1016/j.fob.2014.06.005
PubMed ID:
25057464
PubMed Central ID:
PMC4096678
Type:
Article
ISSN:
22115463
Appears in Collections:
Articles; Center for Desert Agriculture; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorIlg, Andreaen
dc.contributor.authorBruno, Marken
dc.contributor.authorBeyer, Peteren
dc.contributor.authorAl-Babili, Salimen
dc.date.accessioned2014-11-11T14:32:44Z-
dc.date.available2014-11-11T14:32:44Z-
dc.date.issued2014-06-25en
dc.identifier.citationIlg A, Bruno M, Beyer P, Al-Babili S (2014) Tomato carotenoid cleavage dioxygenases 1A and 1B: Relaxed double bond specificity leads to a plenitude of dialdehydes, mono-apocarotenoids and isoprenoid volatiles. FEBS Open Bio 4: 584-593. doi:10.1016/j.fob.2014.06.005.en
dc.identifier.issn22115463en
dc.identifier.pmid25057464en
dc.identifier.doi10.1016/j.fob.2014.06.005en
dc.identifier.urihttp://hdl.handle.net/10754/334629en
dc.description.abstractThe biosynthetic processes leading to many of the isoprenoid volatiles released by tomato fruits are still unknown, though previous reports suggested a clear correlation with the carotenoids contained within the fruit. In this study, we investigated the activity of the tomato (Solanum lycopersicum) carotenoid cleavage dioxygenase (SlCCD1B), which is highly expressed in fruits, and of its homolog SlCCD1A. Using in vitro assays performed with purified recombinant enzymes and by analyzing products formed by the two enzymes in carotene-accumulating Escherichia coli strains, we demonstrate that SlCCD1A and, to a larger extent, SlCCD1B, have a very relaxed specificity for both substrate and cleavage site, mediating the oxidative cleavage of cis- and all-. trans-carotenoids as well as of different apocarotenoids at many more double bonds than previously reported. This activity gives rise to a plenitude of volatiles, mono-apocarotenoids and dialdehyde products, including cis-pseudoionone, neral, geranial, and farnesylacetone. Our results provide a direct evidence for a carotenoid origin of these compounds and point to CCD1s as the enzymes catalyzing the formation of the vast majority of tomato isoprenoid volatiles, many of which are aroma constituents. © 2014 The Authors.en
dc.language.isoenen
dc.publisherWiley-Blackwellen
dc.rightsThis is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).en
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/en
dc.titleTomato carotenoid cleavage dioxygenases 1A and 1B: Relaxed double bond specificity leads to a plenitude of dialdehydes, mono-apocarotenoids and isoprenoid volatilesen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentCenter for Desert Agricultureen
dc.identifier.journalFEBS Open Bioen
dc.identifier.pmcidPMC4096678en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionAlbert-Ludwigs University of Freiburg, Faculty of Biology, Schaenzlestr. 1, D-79104 Freiburg, Germanyen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorAl-Babili, Salimen
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