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(7E,7'E,9Z,9'E)-7',8'-dihydro-psi,psi-carotene + O2
zeta-apo-10'-carotenal + beta-ionone
-
-
-
?
(7E,7'E,9Z,9'E)-lycopene + O2
zeta-apo-10'-carotenal + beta-ionone
-
-
-
?
9'-cis-cryptoxanthin + O2
?
-
-
-
?
9'-cis-neurosporene + O2
9'-cis-apo-10'-neurosporenal + ?
-
-
-
-
?
9'-cis-neurosporene + O2
zeta-apo-10'-carotenal + beta-ionone
low activity
-
-
?
9-cis-beta-carotene + 02
9-cis-beta-apo-10'-carotenal + beta-ionone
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
9-cis-cryptoxanthin + O2
?
-
-
-
?
9-cis-lutein + O2
9-cis-3-hydroxy-epsilon-apo-10'-carotenal + 3-hydroxy-beta-ionone
9-cis-lutein + O2
9-cis-3-hydroxy-epsilon-apo-10'-carotenal + ?
9-cis-lycopene + O2
9-cis-apo-10'-lycopenal + ?
-
-
-
-
?
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + ?
9-cis-zeta-carotene + O2
9-cis-zeta-apo-10'-carotenal + ?
-
-
-
-
?
9-cis-zeta-carotene + O2
9-cis-zeta-apo-10'-carotenal + beta-ionone
-
-
-
?
beta-carotene + O2
10'-apo-beta-carotenal + beta-ionone
-
-
-
?
beta-carotene + O2
7-cis-8'-apo-beta-carotenal + beta-cyclocitral
-
-
-
-
?
beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
isoform CCD1 prefers to cleave the 9, 10 position of beta-carotene
-
-
?
additional information
?
-
9-cis-beta-carotene + 02
9-cis-beta-apo-10'-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + 02
9-cis-beta-apo-10'-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + 02
9-cis-beta-apo-10'-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
AtCCD7 preferentially cleaves 9-cis-beta-carotene
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-lutein + O2
9-cis-3-hydroxy-epsilon-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
?
9-cis-lutein + O2
9-cis-3-hydroxy-epsilon-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
-
?
9-cis-lutein + O2
9-cis-3-hydroxy-epsilon-apo-10'-carotenal + ?
-
-
-
-
?
9-cis-lutein + O2
9-cis-3-hydroxy-epsilon-apo-10'-carotenal + ?
-
-
-
-
?
9-cis-lutein + O2
9-cis-3-hydroxy-epsilon-apo-10'-carotenal + ?
-
-
-
-
?
9-cis-lutein + O2
9-cis-3-hydroxy-epsilon-apo-10'-carotenal + ?
-
-
-
-
?
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
?
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
-
?
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + ?
-
-
-
-
?
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + ?
-
-
-
-
?
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + ?
-
-
-
-
?
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + ?
-
-
-
-
?
additional information
?
-
no substrate: lycopene, lutein, zeaxanthin, violaxanthin, or neoxanthin
-
-
?
additional information
?
-
substrate- and stereospecificity of Arabidopsis thaliana carotenoid cleavage dioxygenase 7, overview
-
-
?
additional information
?
-
AtCCD7 cleaves asymmetrically at the 9, 10, and 9', 10' bonds
-
-
?
additional information
?
-
enzyme CCD7 cleaves different 9-cis-carotenoids, yielding hydroxylated 9-cis-apo-10'-carotenals that may lead to hydroxylated carlactones, but show highest affinity for 9-cis-beta-carotene. The enzyme has a higher affinity to 9-cis-beta-carotene than to 9-cis-zeaxanthin, but converts the latter with higher rate. No detectable conversion of 9-cis-violaxanthin, all-trans-lutein, -zeaxanthin or -cryptoxanthin
-
-
?
additional information
?
-
enzyme substrate specificity, dynamic modeling, overview. No activity with the tri-cis-configured PDS or ZDS intermediates and products, i.e. 9,15-di-cis-phytofluene, 9,15,9'-tri-cis-zeta-carotene, 7,9,9'-tri-cis-neurosporene, and 7,9,9',7-tetra-cis-lycopene, as well as with non-canonical isomers of phytofluene (9-cis, 15-cis, all-trans). 9-cis-Lycopene is a poor substrate, and all-trans-lycopene is no substrate. AtCCD7 shows specificity for cleavage of the trans-configured C9-C10 double bond
-
-
?
additional information
?
-
-
the enzyme does not act on 9-cis-violaxanthin
-
-
-
additional information
?
-
-
substrate- and stereospecificity of Pisum sativum carotenoid cleavage dioxygenase 7, overview
-
-
?
additional information
?
-
-
enzyme CCD7 cleaves different 9-cis-carotenoids, yielding hydroxylated 9-cis-apo-10'-carotenals that may lead to hydroxylated carlactones, but show highest affinity for 9-cis-beta-carotene. The enzyme has a higher affinity to 9-cis-beta-carotene than to 9-cis-zeaxanthin, but converts the latter with higher rate. No detectable conversion of 9-cis-violaxanthin, all-trans-lutein, -zeaxanthin or -cryptoxanthin
-
-
?
additional information
?
-
recombinant ZmCCD7 is able to efficiently catalyze metabolism of linear and cyclic carotenoids in Escherichia coli, and generates bionone by cleaving beta-carotene at the 9,10 (9',10') position. The recombinant enzyme in Escherichia coli catalyzes convertion of individual carotenoids including phytoene, lycopene, delta-carotene, ecarotene, beta-carotene, and zeaxanthin
-
-
?
additional information
?
-
-
recombinant ZmCCD7 is able to efficiently catalyze metabolism of linear and cyclic carotenoids in Escherichia coli, and generates bionone by cleaving beta-carotene at the 9,10 (9',10') position. The recombinant enzyme in Escherichia coli catalyzes convertion of individual carotenoids including phytoene, lycopene, delta-carotene, ecarotene, beta-carotene, and zeaxanthin
-
-
?
additional information
?
-
recombinant ZmCCD7 is able to efficiently catalyze metabolism of linear and cyclic carotenoids in Escherichia coli, and generates bionone by cleaving beta-carotene at the 9,10 (9',10') position. The recombinant enzyme in Escherichia coli catalyzes convertion of individual carotenoids including phytoene, lycopene, delta-carotene, ecarotene, beta-carotene, and zeaxanthin
-
-
?
additional information
?
-
-
recombinant ZpCCD7 is able to efficiently catalyze metabolism of linear and cyclic carotenoids in Escherichia coli, and generates bionone by cleaving beta-carotene at the 9,10 (9',10') position. The recombinant enzyme in Escherichia coli catalyzes convertion of individual carotenoids including phytoene, lycopene, delta-carotene, ecarotene, beta-carotene, and zeaxanthin
-
-
?
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9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
additional information
?
-
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-beta-carotene + O2
9-cis-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
?
9-cis-zeaxanthin + O2
9-cis-3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
-
?
additional information
?
-
substrate- and stereospecificity of Arabidopsis thaliana carotenoid cleavage dioxygenase 7, overview
-
-
?
additional information
?
-
-
substrate- and stereospecificity of Pisum sativum carotenoid cleavage dioxygenase 7, overview
-
-
?
additional information
?
-
recombinant ZmCCD7 is able to efficiently catalyze metabolism of linear and cyclic carotenoids in Escherichia coli, and generates bionone by cleaving beta-carotene at the 9,10 (9',10') position. The recombinant enzyme in Escherichia coli catalyzes convertion of individual carotenoids including phytoene, lycopene, delta-carotene, ecarotene, beta-carotene, and zeaxanthin
-
-
?
additional information
?
-
-
recombinant ZmCCD7 is able to efficiently catalyze metabolism of linear and cyclic carotenoids in Escherichia coli, and generates bionone by cleaving beta-carotene at the 9,10 (9',10') position. The recombinant enzyme in Escherichia coli catalyzes convertion of individual carotenoids including phytoene, lycopene, delta-carotene, ecarotene, beta-carotene, and zeaxanthin
-
-
?
additional information
?
-
recombinant ZmCCD7 is able to efficiently catalyze metabolism of linear and cyclic carotenoids in Escherichia coli, and generates bionone by cleaving beta-carotene at the 9,10 (9',10') position. The recombinant enzyme in Escherichia coli catalyzes convertion of individual carotenoids including phytoene, lycopene, delta-carotene, ecarotene, beta-carotene, and zeaxanthin
-
-
?
additional information
?
-
-
recombinant ZpCCD7 is able to efficiently catalyze metabolism of linear and cyclic carotenoids in Escherichia coli, and generates bionone by cleaving beta-carotene at the 9,10 (9',10') position. The recombinant enzyme in Escherichia coli catalyzes convertion of individual carotenoids including phytoene, lycopene, delta-carotene, ecarotene, beta-carotene, and zeaxanthin
-
-
?
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metabolism
biosynthesis of strigolactones requires the action of two CCD enzymes, CCD7 and CCD8 (EC 1.13.11.70), which act sequentially on 9-cis-beta-carotene, strigolactone biosynthesis pathway from all-trans-beta-carotene to ent-2'-epi-5-deoxystrigol
evolution
occurrence of duplication in CCD4 genes that evolved into two new genes CCD7 and CCD8, EC 1.13.11.70. The site-specific profile and coefficient of type-I functional divergences reveals critical amino acid residues, leading to subgroup-specific functional evolution after their phylogenetic diversification
evolution
Zea mays ZmCCD7 and Zea mays subsp. parviglumis ZpCCD7 have the same coding sequence, indicating negative selection of the CCD7 gene over domestication from Zea mays subsp. parviglumis to Zea mays. ZmCCD7/ZpCCD7 encodes a carotenoid cleavage dioxygenase mediating strigolactone biosynthesis in maize and its ancestor
evolution
-
Zea mays ZmCCD7 and Zea mays subsp. parviglumis ZpCCD7 have the same coding sequence, indicating negative selection of the CCD7 gene over domestication from Zea mays subsp. parviglumis to Zea mays. ZmCCD7/ZpCCD7 encodes a carotenoid cleavage dioxygenase mediating strigolactone biosynthesis in maize and its ancestor
evolution
-
Zea mays ZmCCD7 and Zea mays subsp. parviglumis ZpCCD7 have the same coding sequence, indicating negative selection of the CCD7 gene over domestication from Zea mays subsp. parviglumis to Zea mays. ZmCCD7/ZpCCD7 encodes a carotenoid cleavage dioxygenase mediating strigolactone biosynthesis in maize and its ancestor
-
malfunction
-
tomato plants expressing a SlCCD7 antisense construct display greatly increased branching. A metabolomic screen is conducted. With the exception of a reduction of stem amino acid content in the transgenic lines, no major changes are observed. Targeted analysis of the same plants reveal significantly decreased levels of strigolactone. There are no significant changes in root carotenoids, indicating that relatively little substrate is required to produce the bioactive strigolactones. The germination rate of Orobanche ramosa seeds is reduced by up to 90% on application of extract from the SlCCD7 antisense lines, compared with the wild type. Upon mycorrhizal colonization, C13 cyclohexenone and C14 mycorradicin apocarotenoid levels are greatly reduced in the roots of the antisense lines, implicating SlCCD7 in their biosynthesis
malfunction
-
gene silencing of CCD7 in Phelipanche aegyptiaca by tobacco rattle virus system retards the parasite development on the host. Transient knockdown of PaCCD7 inhibits tubercle development and the infestation process in host plants. The number of parasite tubercles attached to the roots of host plants treated with TRV:PaCCD7, TRV:PaCCD8, or a mixture of TRV:PaCCD7 and TRV:PaCCD8 is significantly reduced by 95% as compared to control plants
malfunction
suppression of shoot branching in the Arabidopsis thaliana Col-0 ccd7 max3 mutant by transformation of ZmCCD7/ZpCCD7. Knockout or knockdown of these CCD7 results in numerous shoot branches by blocking or reducing strigolactone production
malfunction
-
suppression of shoot branching in the Arabidopsis thaliana Col-0 ccd7 max3 mutant by transformation of ZmCCD7/ZpCCD7. Knockout or knockdown of these CCD7 results in numerous shoot branches by blocking or reducing strigolactone production
malfunction
-
suppression of shoot branching in the Arabidopsis thaliana Col-0 ccd7 max3 mutant by transformation of ZmCCD7/ZpCCD7. Knockout or knockdown of these CCD7 results in numerous shoot branches by blocking or reducing strigolactone production
-
physiological function
coexpression of the enzyme, CCD7, and all-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase CCD8, EC 1.13.11.70, in Escherichia coli results in production of 13-apo-beta-carotenone. The sequential cleavages of beta-carotene by CCD7 and CCD8 are likely the initial steps in the synthesis of a carotenoid-derived signaling molecule that is necessary for the regulation lateral branching
physiological function
loss-of-function mutants exhibit a significant decrease in petiole length and are highly branched. The axillary buds, which are typically delayed in growth in wild-type plants, grow out to produce leaves and inflorescences. The mutant plant have smaller rosette diameters due to a decrease in the lengths of petioles and leaf blades compared with wild-type plants. The phenotypes contribute to the bushy appearance of the mutants. The double mutant, additionally lacking 10'-apo-beta-carotenal 13,14-cleaving dioxygenase activity, EC 1.13.11.70, is phenotypically indistinguishable from either single mutant, indicating an interaction consistent with both genes functioning in the same pathway. Both classes of plants show a slight increase in inflorescence number compared with wild type
physiological function
biosynthesis of strigolactones requires the action of two CCD enzymes, CCD7 and CCD8 (EC 1.13.11.70), which act sequentially on 9-cis-beta-carotene
physiological function
CCD7 enzymes are highly stereospecific, cleaving only 9-cis-configured substrates, such as 9-cis-beta-carotene. The strigolactone biosynthetic enzyme AtCCD7 converts 9-cis-configured acyclic carotenes, such as 9-cis-zeta-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 that are thought to derive from the cleavage of poly-cis-configured carotene desaturation intermediates
physiological function
-
important role of the strigolactone associated gene PaCCD7 in the parasite life cycle, and roles of CCD7 and CCD8 enzymes in the biosynthesis of strigolactones
physiological function
strigolactones are apocarotenoids generated via all-trans-beta-carotene isomerization, sequential oxidative cleavage of 9-cis-beta-carotene by two carotenoid cleavage dioxygenases (CCD7 and CCD8)
physiological function
-
strigolactones are apocarotenoids generated via all-trans-beta-carotene isomerization, sequential oxidative cleavage of 9-cis-beta-carotene by two carotenoid cleavage dioxygenases (CCD7 and CCD8)
physiological function
-
strigolactones are phytohormones synthesized from carotenoids via a stereospecific pathway involving the carotenoid cleavage dioxygenases 7 (CCD7) and 8. CCD7 cleaves 9-cis-beta-carotene to form a supposedly 9-cis-configured beta-apo-10'-carotenal
physiological function
strigolactones are phytohormones synthesized from carotenoids via a stereospecific pathway involving the carotenoid cleavage dioxygenases 7 (CCD7) and 8. CCD7 cleaves 9-cis-beta-carotene to form a supposedly 9-cis-configured beta-apo-10'-carotenal
physiological function
two carotenoid cleavage dioxygenases, CCD7 and CCD8, are involved in strigolactones biosynthesis. Involvement of the branching enzymes CCD7 and CCD8 in the control of bud sprouting and apical dominance. CsCCD7 and CsCCD8 expression show some overlapping, although they are not identical
physiological function
-
the enzyme plays an important role in the development of branches and inhibits the growth of axillary buds by up-regulating its downstream gene, BRC1
physiological function
-
strigolactones are apocarotenoids generated via all-trans-beta-carotene isomerization, sequential oxidative cleavage of 9-cis-beta-carotene by two carotenoid cleavage dioxygenases (CCD7 and CCD8)
-
additional information
in silico analysis, structure homology modeling, molecular modeling, dynamic simulation and structure comparisons of Arabidopsis thaliana carotenoid cleavage dioxygenases, overview
additional information
the biochemical basis of the shoot branching phenotype is not due to inhibition of enzyme CCD7, but of enzyme CCD8, EC 1.13.11.70
additional information
-
the biochemical basis of the shoot branching phenotype is not due to inhibition of enzyme CCD7, but of enzyme CCD8, EC 1.13.11.70
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Schwartz, S.H.; Qin, X.; Loewen, M.C.
The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching
J. Biol. Chem.
279
46940-46945
2004
Arabidopsis thaliana (Q7XJM2)
brenda
Ledger, S.E.; Janssen, B.J.; Karunairetnam, S.; Wang, T.; Snowden, K.C.
Modified CAROTENOID CLEAVAGE DIOXYGENASE8 expression correlates with altered branching in kiwifruit (Actinidia chinensis)
New Phytol.
188
803-813
2010
Actinidia chinensis (E3T3A3)
brenda
Auldridge, M.E.; Block, A.; Vogel, J.T.; Dabney-Smith, C.; Mila, I.; Bouzayen, M.; Magallanes-Lundback, M.; DellaPenna, D.; McCarty, D.R.; Klee, H.J.
Characterization of three members of the Arabidopsis carotenoid cleavage dioxygenase family demonstrates the divergent roles of this multifunctional enzyme family
Plant J.
45
982-993
2006
Arabidopsis thaliana (Q7XJM2)
brenda
Alder, A.; Jamil, M.; Marzorati, M.; Bruno, M.; Vermathen, M.; Bigler, P.; Ghisla, S.; Bouwmeester, H.; Beyer, P.; Al-Babili, S.
The path from beta-carotene to carlactone, a strigolactone-like plant hormone
Science
335
1348-1351
2012
Arabidopsis thaliana, Oryza sativa, Pisum sativum
brenda
Vogel, J.T.; Walter, M.H.; Giavalisco, P.; Lytovchenko, A.; Kohlen, W.; Charnikhova, T.; Simkin, A.J.; Goulet, C.; Strack, D.; Bouwmeester, H.J.; Fernie, A.R.; Klee, H.J.
SlCCD7 controls strigolactone biosynthesis, shoot branching and mycorrhiza-induced apocarotenoid formation in tomato
Plant J.
61
300-311
2010
Phelipanche ramosa
brenda
Rubio-Moraga, A.; Ahrazem, O.; Perez-Clemente, R.M.; Gomez-Cadenas, A.; Yoneyama, K.; Lopez-Raez, J.A.; Molina, R.V.; Gomez-Gomez, L.
Apical dominance in saffron and the involvement of the branching enzymes CCD7 and CCD8 in the control of bud sprouting
BMC Plant Biol.
14
171
2014
Crocus sativus (A0A075IEG5)
brenda
Harrison, P.J.; Newgas, S.A.; Descombes, F.; Shepherd, S.A.; Thompson, A.J.; Bugg, T.D.
Biochemical characterization and selective inhibition of beta-carotene cis-trans isomerase D27 and carotenoid cleavage dioxygenase CCD8 on the strigolactone biosynthetic pathway
FEBS J.
282
3986-4000
2015
Arabidopsis thaliana (Q7XJM2), Arabidopsis thaliana
brenda
Bruno, M.; Hofmann, M.; Vermathen, M.; Alder, A.; Beyer, P.; Al-Babili, S.
On the substrate- and stereospecificity of the plant carotenoid cleavage dioxygenase 7
FEBS Lett.
588
1802-1807
2014
Pisum sativum, Arabidopsis thaliana (Q7XJM2)
brenda
Priya, R.; Sneha, P.; Rivera Madrid, R.; Doss, C.G.P.; Singh, P.; Siva, R.
Molecular modeling and dynamic simulation of Arabidopsis thaliana carotenoid cleavage dioxygenase gene a comparison with Bixa orellana and Crocus sativus
J. Cell. Biochem.
118
2712-2721
2017
Arabidopsis thaliana (Q7XJM2)
brenda
Bruno, M.; Koschmieder, J.; Wuest, F.; Schaub, P.; Fehling-Kaschek, M.; Timmer, J.; Beyer, P.; Al-Babili, S.
Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites
J. Exp. Bot.
67
5993-6005
2016
Arabidopsis thaliana (Q7XJM2)
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From carotenoids to strigolactones
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