Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.13.11.69 - carlactone synthase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8VY26

for references in articles please use BRENDA:EC1.13.11.69
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Requires Fe2+. The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza. Also catalyses EC 1.13.11.70, all-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase, but 10-fold slower.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q8VY26
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
slccd8, carotenoid cleavage dioxygenase 8, psccd8, ccd8b, carlactone synthase, more axillary branching 4, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carotenoid cleavage dioxygenase
-
carotenoid cleavage dioxygenase 8
-
MORE AXILLARY BRANCHING 4
-
carotenoid cleavage dioxygenase 8
-
-
NCED8
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
9-cis-10'-apo-beta-carotenal + 2 O2 = carlactone + (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal
show the reaction diagram
acid-base catalysis in the CCD8 catalytic cycle and existence of an essential cysteine residue in the CCD8 active site, two-step kinetic mechanism
SYSTEMATIC NAME
IUBMB Comments
9-cis-10'-apo-beta-carotenal:O2 oxidoreductase (14,15-cleaving, carlactone-forming)
Requires Fe2+. The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza. Also catalyses EC 1.13.11.70, all-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase, but 10-fold slower.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
9-cis-10'-apo-beta-carotenal + 2 O2
carlactone + (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal
show the reaction diagram
9-cis-beta-apo-10'-carotenal + O2
carlactone + omega-OH-(4-CH3)heptanal
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
9-cis-10'-apo-beta-carotenal + 2 O2
carlactone + (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal
show the reaction diagram
-
-
-
?
9-cis-beta-apo-10'-carotenal + O2
carlactone + omega-OH-(4-CH3)heptanal
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E)-3-(3,4-dimethoxyphenyl)-N-hydroxyprop-2-enamide
over 95% inhibition at 0.1 mM
(2E)-N-benzyl-N-hydroxy-3,7-dimethylocta-2,6-dienamide
52% inhibition at 0.1 mM
(2E)-N-hydroxy-3-(4-methoxyphenyl)prop-2-enamide
over 95% inhibition at 0.1 mM
(2E,4E)-N-benzyl-N-hydroxy-5,9-dimethyldeca-2,4,8-trienamide
47% inhibition at 0.1 mM
(2E,4E)-N-hydroxy-3-methyl-5-(2,6,6-trimethylcyclohex-1-en-1-yl)penta-2,4-dienamide
over 95% inhibition at 0.1 mM
2-(2H-1,3-benzodioxol-5-yl)-N-[(4-fluorophenyl)methyl]-N-hydroxyacetamide
over 95% inhibition at 0.1 mM
2-(3,4-dimethoxyphenyl)-N-[(4-fluorophenyl)methyl]-N-hydroxyacetamide
over 95% inhibition at 0.1 mM
3-(3,4-dimethoxyphenyl)-N-hydroxy-N-octylpropanamide
over 95% inhibition at 0.1 mM
3-(3,4-dimethoxyphenyl)-N-hydroxypropanamide
78% inhibition at 0.1 mM
3-amino-N-benzyl-N-hydroxybenzamide
over 95% inhibition at 0.1 mM
abamine
over 95% inhibition at 0.1 mM
N-benzyl-2-(3,4-dimethoxyphenyl)-N-hydroxyacetamide
over 95% inhibition at 0.1 mM
N-benzyl-3-chloro-N-hydroxybenzamide
over 95% inhibition at 0.1 mM
N-benzyl-N-hydroxy-2-(4-hydroxyphenyl)acetamide
over 95% inhibition at 0.1 mM
N-benzyl-N-hydroxy-3,4-dimethoxybenzamide
over 95% inhibition at 0.1 mM
N-benzyl-N-hydroxy-3-(4-methoxyphenyl)propanamide
over 95% inhibition at 0.1 mM
N-benzyl-N-hydroxy-4-methoxybenzamide
over 95% inhibition at 0.1 mM
N-hydroxy-3-(4-methoxyphenyl)-N-octylpropanamide
over 95% inhibition at 0.1 mM
N-hydroxy-3-(4-methoxyphenyl)propanamide
over 95% inhibition at 0.1 mM
N-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-N-hydroxy-2-(4-methoxyphenyl)acetamide
70% inhibition at 0.1 mM
N-[(4-fluorophenyl)methyl]-N-hydroxy-2-(4-hydroxyphenyl)acetamide
over 95% inhibition at 0.1 mM
N-[(4-fluorophenyl)methyl]-N-hydroxy-2-(4-methoxyphenyl)acetamide
over 95% inhibition at 0.1 mM
N-[(4-fluorophenyl)methyl]-N-hydroxy-3,4-dimethoxybenzamide
over 95% inhibition at 0.1 mM
N-[(4-fluorophenyl)methyl]-N-hydroxy-3-(4-methoxyphenyl)propanamide
over 95% inhibition at 0.1 mM
N-[(4-fluorophenyl)methyl]-N-hydroxy-4-methoxybenzamide
over 95% inhibition at 0.1 mM
N1-[(4-fluorophenyl)methyl]-N1-hydroxy-N4-[(4-methoxyphenyl)methyl]butanediamide
-
sodium 3-[hydroxy[(4-methoxyphenyl)acetyl]amino]propanoate
47% inhibition at 0.1 mM
sodium 3-[hydroxy[(naphthalen-2-yl)acetyl]amino]propanoate
92% inhibition at 0.1 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
two-step kinetic mechanism, pre-steady-state kinetic analysis
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
activity range, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
expression of gene is widely distributed, but at low level
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the biochemical basis of the shoot branching phenotype is due to inhibition of enzyme CCD8
metabolism
biosynthesis of strigolactones requires the action of two CCD enzymes, CCD7 (EC 1.13.11.68) and CCD8, which act sequentially on 9-cis-beta-carotene, strigolactone biosynthesis pathway from all-trans-beta-carotene to ent-2'-epi-5-deoxystrigol, overview
physiological function
physiological function
-
coexpression of the enzyme, CCD8, and carotenoid-9',10'-cleaving dioxygenase CCD7, EC 1.13.11.71, 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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CCD8_ARATH
570
0
63957
Swiss-Prot
Chloroplast (Reliability: 5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
coexpression of the enzyme, CCD8, and carotenoid-9',10'-cleaving dioxygenase CCD7, EC 1.13.11.71, 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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged AtCCD8 lacking the first 168 bp from Escherichia coli strain BL21 by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ccd8, recombinant expression of N-terminally His6-tagged AtCCD8 lacking the first 168 bp, corresponding to a chloroplast transit peptide, in Escherichia coli strain BL21
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme is upregulated in the root eleongation zone following 24 h auxin treatment, and hypocotyl, and this is not required for the inhibition of shoot branching
expression is induced by auxin
gene is repressed by low phosphate stress
in early interaction stages, Rhizophagus sp. activates the Arabidopsis gene CCD8. A significant increase in CCD8 transcript abundance is observed in roots of Arabidopsis within 24 h after transfer of the seedlings onto the mycorrhizal mycelium of Rhizophagus sp.
no evidence is found for auxin-induced upregulation of enzyme expression in nodal tissue
the mycelium of Fusarium and Trichoderma do not significantly affect CCD8 transcript abundance compared with control plants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jiang, L.; Jian, H.; Qian, J.; Sun, Z.; Wei, Z.; Chen, X.; Cao, S.
MAX4 gene is involved in the regulation of low inorganic phosphate stress responses in Arabidopsis thaliana
Acta Physiol. Plant.
33
867-875
2011
Arabidopsis thaliana (Q8VY26)
-
Manually annotated by BRENDA team
Sorefan, K.; Booker, J.; Haurogne, K.; Goussot, M.; Bainbridge, K.; Foo, E.; Chatfield, S.; Ward, S.; Beveridge, C.; Rameau, C.; Leyser, O.
MAX4 and RMS1 are orthologous dioxygenase-like genes that regulate shoot branching in Arabidopsis and pea
Genes Dev.
17
1469-1474
2003
Arabidopsis thaliana (Q8VY26)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Bainbridge, K.; Sorefan, K.; Ward, S.; Leyser, O.
Hormonally controlled expression of the Arabidopsis MAX4 shoot branching regulatory gene
Plant J.
44
569-580
2005
Arabidopsis thaliana (Q8VY26)
Manually annotated by BRENDA team
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 (Q8VY26)
Manually annotated by BRENDA team
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 (Q8VY26), Pisum sativum
Manually annotated by BRENDA team
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 (Q8VY26)
Manually annotated by BRENDA team
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 (Q8VY26)
Manually annotated by BRENDA team
Jia, K.; Baz, L.; Al-Babili, S.
From carotenoids to strigolactones
J. Exp. Bot.
69
2189-2204
2018
Arabidopsis thaliana
Manually annotated by BRENDA team
Fernandez, I.; Cosme, M.; Stringlis, I.; Yu, K.; de Jonge, R.; van Wees, S.; Pozo, M.; Pieterse, C.; van der Heijden, M.
Molecular dialogue between arbuscular mycorrhizal fungi and the nonhost plant Arabidopsis thaliana switches from initial detection to antagonism
New Phytol.
223
867-881
2019
Arabidopsis thaliana (Q8VY26)
Manually annotated by BRENDA team
Batra, R.; Agarwal, P.; Tyagi, S.; Saini, D.K.; Kumar, V.; Kumar, A.; Kumar, S.; Balyan, H.S.; Pandey, R.; Gupta, P.K.
A study of CCD8 genes/proteins in seven monocots and eight dicots
PLoS ONE
14
e0213531
2019
Aegilops tauschii, Arabidopsis thaliana (Q8VY26), Brachypodium distachyon, Glycine max (A0A2H4GW71), Medicago truncatula (G7J3F4), Oryza sativa Japonica Group (Q8LIY8), Populus trichocarpa, Prunus persica, Solanum lycopersicum, Sorghum bicolor (C5XK17), Theobroma cacao (A0A061GRL5), Triticum aestivum, Triticum urartu, Vitis vinifera, Zea mays (C4PJN4)
Manually annotated by BRENDA team