Information on EC 1.13.11.70 - all-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.70
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RECOMMENDED NAME
GeneOntology No.
all-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
all-trans-10'-apo-beta-carotenal + O2 = 13-apo-beta-carotenone + (2E,4E,6E)-4-methylocta-2,4,6-trienedial
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
carotenoid cleavage
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SYSTEMATIC NAME
IUBMB Comments
all-trans-10'-apo-beta-carotenal:O2 oxidoreductase (13,14-cleaving)
Requires Fe2+. The enzyme from the plant Arabidopsis thaliana also catalyses EC 1.13.11.69, carlactone synthase, 10-fold faster.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
CCD8a and CCD8b
A0A075IBX5, A0A075IGQ2
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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occurrence of duplication in CCD4 genes that evolved into two new genes CCD7, EC 1.13.11.68, and CCD8. 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
malfunction
metabolism
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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
additional information
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in silico analysis, structure homology modeling, molecular modeling, dynamic simulation and structure comparisons of Arabidopsis thaliana carotenoid cleavage dioxygenases, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
all-trans-10'-apo-beta-carotenal + O2
13-apo-beta-carotenone + (2E,4E,6E)-4-methylocta-2,4,6-trienedial
show the reaction diagram
all-trans-10'-apo-beta-carotenal + O2
13-apo-beta-carotenone + ?
show the reaction diagram
all-trans-10'-apo-beta-carotenol + O2
13-apo-beta-carotenone + ?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
all-trans-10'-apo-beta-carotenal + O2
13-apo-beta-carotenone + (2E,4E,6E)-4-methylocta-2,4,6-trienedial
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E)-3-(3,4-dimethoxyphenyl)-N-hydroxyprop-2-enamide
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over 95% inhibition at 0.1 mM
(2E)-N-benzyl-N-hydroxy-3,7-dimethylocta-2,6-dienamide
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52% inhibition at 0.1 mM
(2E)-N-hydroxy-3-(4-methoxyphenyl)prop-2-enamide
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over 95% inhibition at 0.1 mM
(2E,4E)-N-benzyl-N-hydroxy-5,9-dimethyldeca-2,4,8-trienamide
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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
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over 95% inhibition at 0.1 mM
2-(2H-1,3-benzodioxol-5-yl)-N-[(4-fluorophenyl)methyl]-N-hydroxyacetamide
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over 95% inhibition at 0.1 mM
2-(3,4-dimethoxyphenyl)-N-[(4-fluorophenyl)methyl]-N-hydroxyacetamide
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over 95% inhibition at 0.1 mM
3-(3,4-dimethoxyphenyl)-N-hydroxy-N-octylpropanamide
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over 95% inhibition at 0.1 mM
3-(3,4-dimethoxyphenyl)-N-hydroxypropanamide
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78% inhibition at 0.1 mM
3-amino-N-benzyl-N-hydroxybenzamide
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over 95% inhibition at 0.1 mM
abamine
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over 95% inhibition at 0.1 mM
N-benzyl-2-(3,4-dimethoxyphenyl)-N-hydroxyacetamide
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over 95% inhibition at 0.1 mM
N-benzyl-3-chloro-N-hydroxybenzamide
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over 95% inhibition at 0.1 mM
N-benzyl-N-hydroxy-2-(4-hydroxyphenyl)acetamide
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over 95% inhibition at 0.1 mM
N-benzyl-N-hydroxy-3,4-dimethoxybenzamide
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over 95% inhibition at 0.1 mM
N-benzyl-N-hydroxy-3-(4-methoxyphenyl)propanamide
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over 95% inhibition at 0.1 mM
N-benzyl-N-hydroxy-4-methoxybenzamide
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over 95% inhibition at 0.1 mM
N-hydroxy-3-(4-methoxyphenyl)-N-octylpropanamide
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over 95% inhibition at 0.1 mM
N-hydroxy-3-(4-methoxyphenyl)propanamide
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over 95% inhibition at 0.1 mM
N-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-N-hydroxy-2-(4-methoxyphenyl)acetamide
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70% inhibition at 0.1 mM
N-[(4-fluorophenyl)methyl]-N-hydroxy-2-(4-hydroxyphenyl)acetamide
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over 95% inhibition at 0.1 mM
N-[(4-fluorophenyl)methyl]-N-hydroxy-2-(4-methoxyphenyl)acetamide
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over 95% inhibition at 0.1 mM
N-[(4-fluorophenyl)methyl]-N-hydroxy-3,4-dimethoxybenzamide
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over 95% inhibition at 0.1 mM
N-[(4-fluorophenyl)methyl]-N-hydroxy-3-(4-methoxyphenyl)propanamide
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over 95% inhibition at 0.1 mM
N-[(4-fluorophenyl)methyl]-N-hydroxy-4-methoxybenzamide
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over 95% inhibition at 0.1 mM
N1-[(4-fluorophenyl)methyl]-N1-hydroxy-N4-[(4-methoxyphenyl)methyl]butanediamide
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sodium 3-[hydroxy[(4-methoxyphenyl)acetyl]amino]propanoate
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47% inhibition at 0.1 mM
sodium 3-[hydroxy[(naphthalen-2-yl)acetyl]amino]propanoate
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92% inhibition at 0.1 mM
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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two-step kinetic mechanism, pre-steady-state kinetic analysis
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
A0A075IBX5; A0A075IGQ2;
axillary and apical bud
Manually annotated by BRENDA team
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high expression level of CCD8
Manually annotated by BRENDA team
A0A075IBX5; A0A075IGQ2;
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Manually annotated by BRENDA team
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low expression level of CCD8
Manually annotated by BRENDA team
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moderate expression level of CCD8
Manually annotated by BRENDA team
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highest expression level of CCD8
Manually annotated by BRENDA team
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged AtCCD8 lacking the first 168 bp from Escherichia coli strain BL21 by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene ccd8, quantitative real-time and RT-PCR enzyme expression analysis
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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
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gene ccd8, sequence comparisons
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
decapitation dramatically reduces the high CsCCD8 expression levels in quiescent axillary buds
A0A075IBX5; A0A075IGQ2;
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
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expression is induced by auxin
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gene is repressed by low phosphate stress
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no evidence is found for auxin-induced upregulation of enzyme expression in nodal tissue
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information