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
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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
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UniProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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plant CCD1 enzymes and the NosCCD might have evolved into ACOs without losing their ability to cleave C40 carotenoids
physiological function
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role of CCD1 as an ACO of C27 apocarotenoid intermediates, following their predicted export from plastid to cytosol
additional information
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importance of sequential cleavage reactions of C40 carotenoid precursors, the apocarotenoid cleavage oxygenase, ACO, nature of several carotenoid cleavage oxygenases and the topic of compartmentation. ACO belongs to an outgroup of the CCO enzyme family, but in the mycorrhizal root system suggest CCD1 to preferentially act as an apocarotenoid oxygenase, ACO, in planta cleaving C27 and perhaps other apocarotenoids, enzyme parameters, overview
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-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
?
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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
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+
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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
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, 27C
0.0014 - 0.0021
(3R)-3hydroxy-beta-apo-8'-carotenal
0.031
(3R)-3hydroxy-beta-apo-8'-carotenol
-
pH 7.0, 27C
0.0438
3-hydroxy-beta-apo-10'-carotenal
pH 7.9, 28C
0.0219
3-hydroxy-beta-apo-8'-carotenal
pH 7.9, 28C
0.0025
all-trans-beta-apo-8'-carotenal
-
pH 7.0, 27C
0.017 - 0.0294
beta-apo-10'-carotenal
0.00415 - 0.016
beta-apo-8'-carotenal
0.0245 - 0.043
beta-apo-8'-carotenol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
764
3-hydroxy-beta-apo-10'-carotenal
Mycobacterium tuberculosis
P9WPR5
pH 7.9, 28C
1307
3-hydroxy-beta-apo-8'-carotenal
Mycobacterium tuberculosis
P9WPR5
pH 7.9, 28C
561
beta-apo-10'-carotenal
Mycobacterium tuberculosis
P9WPR5
pH 7.9, 28C
392
beta-apo-8'-carotenal
Mycobacterium tuberculosis
P9WPR5
pH 7.9, 28C
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
ORGANISM
UNIPROT
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
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
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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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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
used as a homology model for 9-cis-epoxycarotenoid dioxygenase, EC 1.13.11.51
Show AA Sequence (122 entries)
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