1.13.11.63: beta-carotene 15,15'-dioxygenase
This is an abbreviated version!
For detailed information about beta-carotene 15,15'-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.63
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1.13.11.63
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beta-cyclodextrin
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cyclodextrins
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gamma-cds
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guest
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alpha-cd
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enantiomer
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selector
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host-guest
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dissolution
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enantioseparation
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gamma-cyclodextrins
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supramolecular
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racemic
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diagram
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voltage
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encapsulation
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surfactant
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electrolyte
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roesy
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micellar
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uv-vis
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infrared
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hydroxypropyl-beta-cyclodextrin
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electrokinetic
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enantioselectivity
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alpha-cyclodextrin
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spectrofluorimetric
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diagnostics
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adamantane
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knead
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synthesis
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glucanotransferase
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deltag
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permethylated
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fused-silica
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medicine
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adamantyl
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provitamin
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photophysical
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borate
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diffractometry
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cgtases
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overhauser
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hydroxypropylated
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photodegradation
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analysis
- 1.13.11.63
- beta-cyclodextrin
- cyclodextrins
-
gamma-cds
-
guest
-
alpha-cd
-
enantiomer
-
selector
-
host-guest
-
dissolution
-
enantioseparation
- gamma-cyclodextrins
-
supramolecular
-
racemic
-
diagram
-
voltage
-
encapsulation
- surfactant
-
electrolyte
-
roesy
-
micellar
-
uv-vis
-
infrared
- hydroxypropyl-beta-cyclodextrin
-
electrokinetic
-
enantioselectivity
- alpha-cyclodextrin
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spectrofluorimetric
- diagnostics
- adamantane
-
knead
- synthesis
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glucanotransferase
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deltag
-
permethylated
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fused-silica
- medicine
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adamantyl
-
provitamin
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photophysical
- borate
-
diffractometry
- cgtases
-
overhauser
-
hydroxypropylated
-
photodegradation
- analysis
Reaction
Synonyms
BC-15,15'-oxygenase, BCM, BCMO, Bcmo1, Bcmo2, BCO, BCO1, BCO2, Bcox, beta,beta-carotene 15,15'-mono-oxygenase 1, beta,beta-carotene 15,15'-monooxygenase, beta,beta-carotene 15,15'-monooxygenase 1, beta,beta-carotene 15,15'-monooxygenase-1, beta,beta-carotene 15,15-monooxygenase 1, beta,beta-carotene-15,15'-monooxygenase, beta,beta-carotene-15,15'-oxygenase, beta-carotene 15,15' oxygenase, beta-carotene 15,15'-dioxygenase, beta-carotene 15,15'-monooxygenase, beta-carotene 15,15'-monooxygenase 1, beta-carotene 15,15'-oxygenase, beta-carotene 15,15-monooxygenase, beta-carotene dioxygenase 1, beta-carotene oxygenase 2, beta-carotene-15,15'-dioxygenase, beta-carotene-15,15'-monooxygenase, beta-carotene-15,15'-oxygenase, beta-carotene-15,15'-oxygenase-1, beta-carotene-15,15'-oxygenase-2, beta-CD, betaCDIOX, betaCO, BLH, brp/blh-family beta-carotene monooxygenase, brpA, carotenoid oxygenase, Ci-BCO, CMO1, EC 1.13.11.21, EC 1.14.99.36, NinaB
ECTree
1.13.11.63 beta-carotene 15,15'-dioxygenaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.13.11.63 - beta-carotene 15,15'-dioxygenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
13-cis-beta-carotene + O2
retinal
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11.4% of the activity with all-trans-beta-carotene
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-
?
alpha-carotene + ?
11-cis-retinal + all-trans-retinal + all-trans-alpha-retinal
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32.7% 11-cis-retinal + 17.3% all-trans-retinal + 50.0% all-trans-alpha-retinal
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?
alpha-carotene + O2
retinal
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8.2% of the activity with all-trans-beta-carotene
-
-
?
alpha-carotene + O2
retinal + alpha-retinal
one molecule retinal is formed
-
-
?
beta-apo-4'-carotenal + O2
retinal + ?
one molecule retinal is formed
-
-
?
beta-carotene + ?
11-cis-retinal + all-trans-retinal
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41.2% 11-cis-retinal + 58.8% all-trans-retinal
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?
beta-carotene + O2
11-cis-retinal + 13-cis-retinal + all-trans-retinal
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-
-
?
cryptoxanthin + O2
11-cis-retinal + all-trans-retinal + 11-cis-3-hydroxy-retinal + all-trans-3-hydroxy-retinal
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4.2% 11-cis-retinal + 45.8% all-trans-retinal + 35.1% 11-cis-3-hydroxy-retinal + 14.9% all-trans-3-hydroxy-retinal
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?
gamma-carotene + O2
retinal + acycloretinal
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one molecule retinal is formed
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?
lutein + O2
11-cis-3-hydroxy-retinal + all-trans-3-hydroxy-retinal + all-trans-3-hydroxy-alpha-retinal
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39.9% 11-cis-3-hydroxy-retinal + 10.1% all-trans-3-hydroxy-retinal + 47.7% all-trans-3-hydroxy-alpha-retinal
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?
beta-apo-10'-carotenol + O2
?
beta-apo-10'-carotenol is the major long-chain beta-apocarotenoid in mouse liver
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-
?
beta-apo-8'-carotenal + O2
retinal + ?
one molecule retinal is formed
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-
?
beta-carotene + O2
2 all-trans-retinal
BCMO1 cleaves at the central 15,15' position of the polyene chain producing two molecules of retinal
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-
?
beta-carotene + O2
2 all-trans-retinal
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BCMO1 cleaves at the central 15,15' position of the polyene chain producing two molecules of retinal
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-
?
beta-carotene + O2
2 all-trans-retinal
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BCMO1 cleaves at the central 15,15' position of the polyene chain producing two molecules of retinal
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-
?
beta-carotene + O2
2 all-trans-retinal
BCMO1 cleaves at the central 15,15' position of the polyene chain producing two molecules of retinal
-
-
?
beta-carotene + O2
2 all-trans-retinal
BCMO1 cleaves at the central 15,15' position of the polyene chain producing two molecules of retinal
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-
?
beta-carotene + O2
2 all-trans-retinal
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-
-
?
beta-carotene + O2
2 all-trans-retinal
BCMO1 cleaves at the central 15,15' position of the polyene chain producing two molecules of retinal
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-
?
beta-carotene + O2
2 all-trans-retinal
BCMO1 cleaves at the central 15,15' position of the polyene chain producing two molecules of retinal
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-
?
beta-carotene + O2
2 all-trans-retinal
BCMO1 cleaves at the central 15,15' position of the polyene chain producing two molecules of retinal
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-
?
beta-carotene + O2
2 all-trans-retinal
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-
-
?
beta-carotene + O2
2 all-trans-retinal
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the oxygen atom of retinal originates from molecular oxygen
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?
beta-carotene + O2
2 retinal
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tyrosine Y235 and Y326 in mouse BCMO1 fix the position of the substrate on the two sides of the 15,15'-double bond most likely due to a mechanism implicating cation pi-stabilization
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-
?
beta-carotene + O2
all-trans-retinal
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BCMO1 is a key enzyme in the pathway of retinoid synthesis from carotenoids, regulation of BCMO1 activity, overview
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-
?
beta-carotene + O2
all-trans-retinal
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BCMO1 is a key enzyme in the pathway of retinoid synthesis from carotenoids, and is responsible for metabolically limiting the amount of intact beta-carotene that can be absorbed by mice from their diet, regulation of BCMO1 activity, overview
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?
beta-carotene + O2
retinal
the enzyme is essential for pattern formation and differentation during zebrafish embryogenesis
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-
?
beta-carotene + O2
retinal
key enzyme in the metabolism of beta,beta-carotene to vitamin A
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-
?
beta-carotene + O2
retinal
the enzyme catalyzes the first step in the synthesis of vitamin A from dietary carotenoids. May also play a role in peripheral vitamin A synthesis from plasma-borne provitamin A carotenoids
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-
?
beta-carotene + O2
retinal
enzyme plays an important role in retinoid synthesis. BCDO may also be a candidate gene for retinal degenerative disease
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-
?
beta-carotene + O2
retinal
crucial enzyme in development and metabolism that governs the de novo entry of vitamin A from plant-derived precursors, enzyme may play a critical role in gastrulation
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-
?
beta-carotene + O2
retinal
enzyme may play a critical role in gastrulation
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-
?
beta-carotene + O2
retinal
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conversion of the plant product beta-carotene into a product necessary for the growth and life of the animal organism
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?
beta-carotene + O2
retinal
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the enzyme is responsible for providing vertebrates with vitamin A by catalyzing oxidative cleavage of beta-carotene at its central double bond to two molecules of retinal in intestinal cells
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-
?
beta-cryptoxanthin + O2
retinal + (3R)-3-hydroxyretinal
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-
-
?
zeaxanthin + O2
(3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
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-
-
-
?
zeaxanthin + O2
(3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
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41.5% 11-cis-3-hydroxy-retinal + 58.5% all-trans-3-hydroxy-retinal
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?
additional information
?
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substrate specificity for BCMO1, overview. BCMO1 requires at least one unsubstituted beta-ionone ring for the cleavage of carotenoid substrates, but also the presence and position of methyl groups on the polyene chain are important. Therefore, activity is limited mainly to alpha- and beta-carotene, beta-apo-carotenals and beta-cryptoxanthin. Specificity of BCMO1 towards substrates decreases in the order: beta-carotene, beta-cryptoxanthin, beta-apo-8'-carotenal, beta-apo-4'-carotenal, alpha-carotene, gamma-carotene
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-
?
additional information
?
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substrate specificity for BCMO1, overview
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-
?
additional information
?
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substrate specificity for BCMO1, overview. BCMO1 requires at least one unsubstituted beta-ionone ring for the cleavage of carotenoid substrates, but also the presence and position of methyl groups on the polyene chain are important. Therefore, activity is limited mainly to alpha- and beta-carotene, beta-apo-carotenals and beta-cryptoxanthin. Specificity of BCMO1 towards substrates decreases in the order: beta-carotene, beta-cryptoxanthin, beta-apo-8'-carotenal, beta-apo-4'-carotenal, alpha-carotene, gamma-carotene
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-
?
additional information
?
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catalyses the first step in the conversion of dietary provitamin A carotenoids to vitamin A in the small intestine
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-
?
additional information
?
-
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catalyses the first step in the conversion of dietary provitamin A carotenoids to vitamin A in the small intestine
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-
?
additional information
?
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BCMO is also active with alpha-carotene, beta-apo-8'-carotenal, and beta-apo-4'-carotenal. The hydrophobicity of residue 108 specifically affects the affinity of beta-carotene 15,15'-monooxygenase for substrates with two ionone rings. Residue 108 may be related to the indirect interaction with the second ionone ring of the substrates with two ionone rings, comparison with apo-carotenoid 15,15'-oxygenase, EC 1.14.99.41, overview
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-
?
additional information
?
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-
BCMO is also active with alpha-carotene, beta-apo-8'-carotenal, and beta-apo-4'-carotenal. The hydrophobicity of residue 108 specifically affects the affinity of beta-carotene 15,15'-monooxygenase for substrates with two ionone rings. Residue 108 may be related to the indirect interaction with the second ionone ring of the substrates with two ionone rings, comparison with apo-carotenoid 15,15'-oxygenase, EC 1.14.99.41, overview
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-
?
additional information
?
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shorter beta-apocarotenals, i.e. beta-apo-10-carotenal, beta-apo-12'-carotenal, and beta-apo-14'-carotenal, do not show Michaelis-Menten behavior under the conditions tested. No activity with lutein, zeaxanthin, and 9-cis-beta-carotene. Purified recombinant BCO1 cleaves beta-carotene solely at the central 15-15' bond
-
-
?
additional information
?
-
substrate specificity for BCMO1, overview. BCMO1 requires at least one unsubstituted beta-ionone ring for the cleavage of carotenoid substrates, but also the presence and position of methyl groups on the polyene chain are important. Therefore, activity is limited mainly to alpha- and beta-carotene, beta-apo-carotenals and beta-cryptoxanthin
-
-
?
additional information
?
-
-
substrate specificity for BCMO1, overview. BCMO1 requires at least one unsubstituted beta-ionone ring for the cleavage of carotenoid substrates, but also the presence and position of methyl groups on the polyene chain are important. Therefore, activity is limited mainly to alpha- and beta-carotene, beta-apo-carotenals and beta-cryptoxanthin
-
-
?
additional information
?
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25-hydroxycholesterol is a secondary autoxidation product derived from 3beta-hydroxy-cholest-5-ene-25-hydroperoxide, a hydroperoxide identified in air-aged cholesterol
-
-
?
additional information
?
-
substrate specificity for BCMO1, overview. BCMO1 requires at least one unsubstituted beta-ionone ring for the cleavage of carotenoid substrates, but also the presence and position of methyl groups on the polyene chain are important. Therefore, activity is limited mainly to alpha- and beta-carotene, beta-apo-carotenals and beta-cryptoxanthin
-
-
?
additional information
?
-
symmetric cleavage by BCO1 yields retinoids, i.e. beta-15'-apocarotenoids, C20
-
-
?
additional information
?
-
-
substrate specificity for BCMO1, overview
-
-
?
additional information
?
-
substrate specificity for BCMO1, overview. BCMO1 requires at least one unsubstituted beta-ionone ring for the cleavage of carotenoid substrates, but also the presence and position of methyl groups on the polyene chain are important. Therefore, activity is limited mainly to alpha- and beta-carotene, beta-apo-carotenals and beta-cryptoxanthin. Specificity of BCMO1 towards substrates decreases in the order: beta-carotene, beta-cryptoxanthin, beta-apo-8'-carotenal, beta-apo-4'-carotenal, alpha-carotene, gamma-carotene
-
-
?
additional information
?
-
substrate specificity for BCMO1, overview. BCMO1 requires at least one unsubstituted beta-ionone ring for the cleavage of carotenoid substrates, but also the presence and position of methyl groups on the polyene chain are important. Therefore, activity is limited mainly to alpha- and beta-carotene, beta-apo-carotenals and beta-cryptoxanthin. Specificity of BCMO1 towards substrates decreased in the order: beta-carotene, beta-cryptoxanthin, beta-apo-8'-carotenal, beta-apo-4'-carotenal, alpha-carotene, gamma-carotene
-
-
?
additional information
?
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no substrate: beta-apo-8'-carotenal, beta-apo-12'-carotenal, lutein, zeaxanthin, or lycopene, suggesting that the presence of one unsubstituted-ionone ring in a substrate with a molecular weight greater than C35 seems to be essential for enzyme activity
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-
?
