1.13.11.71: carotenoid-9',10'-cleaving dioxygenase
This is an abbreviated version!
For detailed information about carotenoid-9',10'-cleaving dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.71
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1.13.11.71
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retinoids
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lutein
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grey
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all-trans-retinal
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zeaxanthin
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15,15'-monooxygenase
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lycopene
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oviparous
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ornamental
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hamilton
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captive
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vitellogenesis
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loach
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queen
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strigolactone
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synthesis
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csf1r
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junglefowl
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agriculture
- 1.13.11.71
-
retinoids
- lutein
-
grey
- all-trans-retinal
- zeaxanthin
-
15,15'-monooxygenase
- lycopene
-
oviparous
-
ornamental
- hamilton
-
captive
-
vitellogenesis
- loach
-
queen
- strigolactone
- synthesis
- csf1r
- junglefowl
- agriculture
Reaction
Synonyms
BC-9',10'-oxygenase, Bcdo2, BCO2, beta,beta-carotene 9',10'-dioxygenase 2, beta,beta-carotene 9',10'-oxygenase, beta,beta-carotene-9',10'-dioxygenase, beta,beta-carotene-9',10'-dioxygenase 2, beta,beta-carotene-9,10-oxygenase 2, beta-carotene 9',10' oxygenase, beta-carotene 9',10'-oxygenase, beta-carotene-9',10'-oxygenase, beta-carotene-9,10'-oxygenase, CCD1, CCD4b, CCD7, LjCCD7, ScBCO2, xanthophyll cleavage enzyme
ECTree
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Engineering
Engineering on EC 1.13.11.71 - carotenoid-9',10'-cleaving dioxygenase
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additional information
enzyme is able to complement a CCD7/max3 mutation in Arabidopsis thaliana
additional information
a truncated enzyme protein of 587 amino acids lacking the N-terminal targeting sequence is also able to catalyze the 910 cleavage of beta-carotene. 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
additional information
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a polymorphism at the beta,beta-carotene 15,15'-monooxygenase 1 (BCMO1, EC 1.13.11.63) locus affects the response to dietary beta-carotene and the expression level of enzyme BCDO2, two fully linked BCMO1 SNPs are identified within the proximal promoter of the BCMO1 gene at -678 and -621 upstream from the ATG codon corresponding to the substitution of two adenines (A/A) by two guanines (G/G) and defined two haplotypes, AN57A and GN57G, which segregate within chicken lines
additional information
GKAA represents an extension of human BCO2 exon 3 caused by use of an alternate donor splice site. Deletion of GKAA between P125 and M127 and replacement of A126 by T are expected to induce a substantial change in structure in this area, but no significant difference is found at their enzymatic cleavage domains, as all four key histidine residues are conserved. Simple deletion of GKAA cannot convert human BCO2 into an active carotenoid cleavage enzyme. Also replacing the N-terminal 197 amino acids of human BCO2a with the N-terminal 150 amino acids of mouse BCO2 or substitution of a wide range of amino acid residues of human BCO2 with the corresponding residues of mouse BCO2 cannot restore human BCO2's cleavage activity. Combined deletion of GKAA from human BCO2 with several key amino acid substitutions selected from the mouse BCO2 sequence still cannot rescue human BCO2's function
additional information
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GKAA represents an extension of human BCO2 exon 3 caused by use of an alternate donor splice site. Deletion of GKAA between P125 and M127 and replacement of A126 by T are expected to induce a substantial change in structure in this area, but no significant difference is found at their enzymatic cleavage domains, as all four key histidine residues are conserved. Simple deletion of GKAA cannot convert human BCO2 into an active carotenoid cleavage enzyme. Also replacing the N-terminal 197 amino acids of human BCO2a with the N-terminal 150 amino acids of mouse BCO2 or substitution of a wide range of amino acid residues of human BCO2 with the corresponding residues of mouse BCO2 cannot restore human BCO2's cleavage activity. Combined deletion of GKAA from human BCO2 with several key amino acid substitutions selected from the mouse BCO2 sequence still cannot rescue human BCO2's function
additional information
insertion of GKAA into mouse BCO2, in analogy to the inactive human enzyme, inactivates the mutant mouse enzyme, demonstrating that the GKAA insertion alone is sufficient to inactivate mouse BCO2
additional information
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insertion of GKAA into mouse BCO2, in analogy to the inactive human enzyme, inactivates the mutant mouse enzyme, demonstrating that the GKAA insertion alone is sufficient to inactivate mouse BCO2
additional information
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insertion of GKAA into mouse BCO2, in analogy to the inactive human enzyme, inactivates the mutant mouse enzyme, demonstrating that the GKAA insertion alone is sufficient to inactivate mouse BCO2
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