Information on EC 1.13.11.75 - all-trans-8'-apo-beta-carotenal 15,15'-oxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.75
-
RECOMMENDED NAME
GeneOntology No.
all-trans-8'-apo-beta-carotenal 15,15'-oxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
all-trans-8'-apo-beta-carotenal + O2 = all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
all-trans-8'-apo-beta-carotenal:oxygen 15,15'-oxidoreductase (bond-cleaving)
Contains an Fe2+-4His arrangement. The enzyme is involved in retinal biosynthesis in bacteria [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
-
role of CCD1 as an ACO of C27 apocarotenoid intermediates, following their predicted export from plastid to cytosol
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-3hydroxy-beta-apo-12'-carotenal + O2
(3R)-3-hydroxy-retinal + ?
show the reaction diagram
-
-
-
?
(3R)-3hydroxy-beta-apo-12'-carotenal + O2
(3R)-3-hydroxyretinal + ?
show the reaction diagram
-
-
-
?
(3R)-3hydroxy-beta-apo-8'-carotenal + O2
(3R)-3-hydroxy-retinal + apo-8',15'-apo-carotenedial
show the reaction diagram
-
-
-
?
(3R)-3hydroxy-beta-apo-8'-carotenal + O2
(3R)-3-hydroxyretinal + apo-8',15'-apo-carotenedial
show the reaction diagram
-
-
-
?
(3R)-3hydroxy-beta-apo-8'-carotenol + O2
(3R)-3-hydroxy-retinal + apo-8',15'-apo-carotenedial
show the reaction diagram
-
-
-
?
(3R)-3hydroxy-beta-apo-8'-carotenol + O2
(3R)-3-hydroxyretinal + apo-8',15'-apo-carotenedial
show the reaction diagram
-
-
-
?
3,3'-dihydoxyisorenieratene + O2
?
show the reaction diagram
3-hydroxy-beta-apo-10'-carotenal + O2
?
show the reaction diagram
3% cleavage at C15-C15' double bond, 97% cleavage at the C13-C14 double bond
-
-
?
3-hydroxy-beta-apo-8'-carotenal + O2
?
show the reaction diagram
95% cleavage at C15-C15' double bond, 5% cleavage at the C13-C14 double bond
-
-
?
9'-cis-neoxanthin + O2
?
show the reaction diagram
-
-
-
?
all-trans-(3R)-hydroxy-8'-apo-beta-carotenol + O2
?
show the reaction diagram
-
-
-
?
all-trans-8'-apo-?-carotenal + O2
all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
show the reaction diagram
-
-
-
-
?
all-trans-8'-apo-beta-carotenal + O2
all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
show the reaction diagram
-
-
-
-
?
all-trans-beta-apo-8'-carotenal + O2
all-trans-retinal + apo-8'15'-apo-carotenedial
show the reaction diagram
the cis-isomer is not a substrate
-
-
?
apo-10'-lycopenal + O2
acycloretinal + ?
show the reaction diagram
-
-
-
?
apo-8'-lycopenal + O2
acycloretinal + ?
show the reaction diagram
-
-
-
?
apo-8'-lycopenol + O2
acycloretinal + ?
show the reaction diagram
-
-
-
?
beta-apo-10'-carotenal + O2
?
show the reaction diagram
beta-apo-10'-carotenal + O2
retinal + ?
show the reaction diagram
-
-
-
?
beta-apo-8'-carotenal + O2
?
show the reaction diagram
beta-apo-8'-carotenal + O2
retinal + apo-8',15'-apo-carotenedial
show the reaction diagram
-
-
-
?
beta-apo-8'-carotenol + O2
retinal + apo-8',15'-apo-carotenedial
show the reaction diagram
beta-carotene + O2
retinal + beta-apo-14'-carotenal + beta-apo-13-carotenone
show the reaction diagram
30% cleavage at C13-C14 double bond, 69% cleavage at the C15-C15' double bond
-
-
?
lutein + O2
?
show the reaction diagram
54% cleavage at C15-C15' double bond, 45% cleavage at the C13-C14 double bond
-
-
?
zeaxanthin + O2
?
show the reaction diagram
additional information
?
-
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-8'-apo-?-carotenal + O2
all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the substrate specificity of the enzyme is unique in that it cleaves only all-trans apocarotenoids of different chain lengths, but not C40 beta-carotene to yield all-trans C20 retinal or its derivatives
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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
enzyme contains an Fe2+-4-His arrangement at the axis of a seven-bladed beta-propeller chain fold covered by a dome formed by six large loops. The Fe2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CHAPS
-
slight inhibition
CYMAL-4
-
slight inhibition
-
hexaethylene glycol monooctyl ether
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strongly inhibits ACO activity even at concentrations below its critical micelle concentration
tetraethylene glycol monooctyl ether
-
strongly inhibits ACO activity even at concentrations below its critical micelle concentration
additional information
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the enzyme ACO is inhibited by linear polyoxyethylene detergents, mechanism, overview. ACO crystallization strongly inhibits the apocarotenoid oxygenase activity of the enzyme. PEG 3350 has little influence on enzyme activity up to a concentration of10% w/v
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026
(3R)-3hydroxy-beta-apo-12'-carotenal
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pH 7.0, 27°C
0.0014 - 0.0021
(3R)-3hydroxy-beta-apo-8'-carotenal
0.031
(3R)-3hydroxy-beta-apo-8'-carotenol
-
pH 7.0, 27°C
0.0438
3-hydroxy-beta-apo-10'-carotenal
pH 7.9, 28°C
0.0219
3-hydroxy-beta-apo-8'-carotenal
pH 7.9, 28°C
0.121 - 0.127
all-trans-8'-apo-beta-carotenal
0.0025
all-trans-beta-apo-8'-carotenal
-
pH 7.0, 27°C
0.017 - 0.0294
beta-apo-10'-carotenal
0.00415 - 0.016
beta-apo-8'-carotenal
0.0245 - 0.043
beta-apo-8'-carotenol
additional information
additional information
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steady-state kinetics, Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
764
3-hydroxy-beta-apo-10'-carotenal
pH 7.9, 28°C
1307
3-hydroxy-beta-apo-8'-carotenal
pH 7.9, 28°C
561
beta-apo-10'-carotenal
pH 7.9, 28°C
392
beta-apo-8'-carotenal
pH 7.9, 28°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.47
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purified recombinant enzyme, pH 7.0, 28°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
monotopic membrane protein
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
Synechocystis sp. (strain PCC 6803 / Kazusa);
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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three-dimensional structure analysis
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
three-dimensional structure analysis
-
enzyme contains an Fe2+-4-His arrangement at the axis of a seven-bladed beta-propeller chain fold covered by a dome formed by six large loops. The Fe2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative in one of the crystals. On binding, three consecutive double bonds of this carotenoid change from a straight all-trans to a cranked cis-trans-cis conformation. The remaining trans bond is located at the dioxygen-ligated Fe2+ and cleaved by oxygen
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native enzyme in the absence of apocarotenoid substrate, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 25 mM HEPES-NaOH, pH 7.0, 1 mM dithiothreitol, and 0.8% w/v hexaethylene glycol monooctyl ether or 0.02% w/v Triton X-100, with 0.001 ml of reservoir solution containing 0.1 M BTP-HCl, pH 6.0, 22–23% w/v PEG 3350, 0.2 M NH4Cl, and 1 mM MnCl2, 8°C, 3-4 days, X-ray diffraction structure determination and analysis. ACO crystallization strongly inhibits the apocarotenoid oxygenase activity of the enzyme
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21 by ammonium sulfate fractionation and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree
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expression in Escherichia coli
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gene sll1541, recombinant expression in Escherichia coli strain BL21
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
used as a homology model for 9-cis-epoxycarotenoid dioxygenase, EC 1.13.11.51