Tomato carotenoid cleavage dioxygenases 1A and 1B: Relaxed double bond specificity leads to a plenitude of dialdehydes, mono-apocarotenoids and isoprenoid volatiles
Article - Full Text
Supplemental File 1
Supplemental File 2
Supplemental File 3
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Desert Agriculture Initiative
Plant Science Program
Online Publication Date2014-06-25
Print Publication Date2014-01-01
Permanent link to this recordhttp://hdl.handle.net/10754/334629
MetadataShow full item record
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.
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.
JournalFEBS Open Bio
PubMed Central IDPMC4096678
The following license files are associated with this item:
Except where otherwise noted, this item's license is described as This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).
- Characterization of the rice carotenoid cleavage dioxygenase 1 reveals a novel route for geranial biosynthesis.
- Authors: Ilg A, Beyer P, Al-Babili S
- Issue date: 2009 Feb
- Apocarotenoids: A New Carotenoid-Derived Pathway.
- Authors: Beltran JC, Stange C
- Issue date: 2016
- The tomato carotenoid cleavage dioxygenase 1 genes contribute to the formation of the flavor volatiles beta-ionone, pseudoionone, and geranylacetone.
- Authors: Simkin AJ, Schwartz SH, Auldridge M, Taylor MG, Klee HJ
- Issue date: 2004 Dec
- The carotenoid cleavage dioxygenase 1 enzyme has broad substrate specificity, cleaving multiple carotenoids at two different bond positions.
- Authors: Vogel JT, Tan BC, McCarty DR, Klee HJ
- Issue date: 2008 Apr 25
- Analysis of apocarotenoid volatiles during the development of Ficus carica fruits and characterization of carotenoid cleavage dioxygenase genes.
- Authors: Nawade B, Shaltiel-Harpaz L, Yahyaa M, Bosamia TC, Kabaha A, Kedoshim R, Zohar M, Isaacson T, Ibdah M
- Issue date: 2020 Jan