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Information on EC 1.13.11.75 - all-trans-8'-apo-beta-carotenal 15,15'-oxygenase
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EC Tree
1.13.11.75 all-trans-8'-apo-beta-carotenal 15,15'-oxygenaseIUBMB Comments
Contains an Fe2+-4His arrangement. The enzyme is involved in retinal biosynthesis in bacteria .
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Word Map
- 1.13.11.75
-
apocarotenoids
- oxygenases
- synechocystis
-
non-heme
- stilbene
-
nceds
- zeaxanthin
- strigolactone
-
all-trans-retinyl
- piceatannol
- 4-vinylguaiacol
-
end-groups
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
Synonyms
carotenoid cleavage oxygenase, apocarotenoid oxygenase, apocarotenoid-15-15'-oxygenase, sll1541, apocarotenoid cleavage oxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACO
carotenoid cleavage oxygenase
CCO
EC 1.14.99.41
-
-
formerly
-
additional information
-
ACO belongs to an outgroup of the CCO enzyme family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
all-trans-8'-apo-beta-carotenal + O2 = all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
all-trans-8'-apo-beta-carotenal + O2 = all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
on binding, three consecutive double bonds of the 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
all-trans-8'-apo-beta-carotenal + O2 = all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
the enzyme utilizes a non-heme iron center to oxidatively cleave a carbon-carbon double bond of a carotenoid substrate
all-trans-8'-apo-beta-carotenal + O2 = all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
-
-
-
-
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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].
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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
(3R)-3hydroxy-beta-apo-12'-carotenal + O2
(3R)-3-hydroxy-retinal + ?
-
-
-
?
(3R)-3hydroxy-beta-apo-12'-carotenal + O2
(3R)-3-hydroxyretinal + ?
-
-
-
?
(3R)-3hydroxy-beta-apo-8'-carotenal + O2
(3R)-3-hydroxy-retinal + apo-8',15'-apo-carotenedial
-
-
-
?
(3R)-3hydroxy-beta-apo-8'-carotenal + O2
(3R)-3-hydroxyretinal + apo-8',15'-apo-carotenedial
-
-
-
?
(3R)-3hydroxy-beta-apo-8'-carotenol + O2
(3R)-3-hydroxy-retinal + apo-8',15'-apo-carotenedial
-
-
-
?
(3R)-3hydroxy-beta-apo-8'-carotenol + O2
(3R)-3-hydroxyretinal + apo-8',15'-apo-carotenedial
-
-
-
?
3-hydroxy-beta-apo-10'-carotenal + O2
?
3% cleavage at C15-C15' double bond, 97% cleavage at the C13-C14 double bond
-
-
?
3-hydroxy-beta-apo-8'-carotenal + O2
?
95% cleavage at C15-C15' double bond, 5% cleavage at the C13-C14 double bond
-
-
?
all-trans-(3R)-hydroxy-8'-apo-beta-carotenol + O2
?
-
-
-
?
all-trans-8'-apo-beta-carotenal + O2
all-trans-retinal + 8'-hydroxy-15'-apocarotenal
-
-
-
?
all-trans-8'-apo-beta-carotenol + O2
all-trans-retinal + (2E,4E,6E)-8-hydroxy-2,6-dimethylocta-2,4,6-trienal
-
-
-
?
all-trans-8'-apocarotenol + O2
all-trans-retinal + (2E,4E,6E)-8-hydroxy-2,6-dimethylocta-2,4,6-trienal
-
-
-
?
all-trans-beta-apo-8'-carotenal + O2
all-trans-retinal + apo-8'15'-apo-carotenedial
the cis-isomer is not a substrate
-
-
?
beta-apo-8'-carotenal + O2
retinal + apo-8',15'-apo-carotenedial
-
-
-
?
beta-carotene + O2
retinal + beta-apo-14'-carotenal + beta-apo-13-carotenone
30% cleavage at C13-C14 double bond, 69% cleavage at the C15-C15' double bond
-
-
?
lutein + O2
?
54% cleavage at C15-C15' double bond, 45% cleavage at the C13-C14 double bond
-
-
?
3,3'-dihydoxyisorenieratene + O2
?
54% cleavage at C15-C15' double bond, 45% cleavage at the C13-C14 double bond
-
-
?
3,3'-dihydoxyisorenieratene + O2
?
54% cleavage at C15-C15' double bond, 45% cleavage at the C13-C14 double bond
-
-
?
beta-apo-10'-carotenal + O2
?
79% cleavage at C13-C14 double bond, 20% cleavage at the C15-C15' double bond
-
-
?
beta-apo-10'-carotenal + O2
?
79% cleavage at C13-C14 double bond, 20% cleavage at the C15-C15' double bond
-
-
?
beta-apo-8'-carotenal + O2
?
86% cleavage at C13-C14 double bond, 14% cleavage at the C15-C15' double bond
-
-
?
beta-apo-8'-carotenal + O2
?
86% cleavage at C13-C14 double bond, 14% cleavage at the C15-C15' double bond
-
-
?
beta-apo-8'-carotenol + O2
retinal + apo-8',15'-apo-carotenedial
-
-
-
?
beta-apo-8'-carotenol + O2
retinal + apo-8',15'-apo-carotenedial
-
-
-
?
zeaxanthin + O2
?
83% cleavage at C15-C15' double bond, 17% cleavage at the C13-C14 double bond
-
-
?
zeaxanthin + O2
?
83% cleavage at C15-C15' double bond, 17% cleavage at the C13-C14 double bond
-
-
?
additional information
?
-
MtCCO cleaves the central C15-C15' and an excentric double bond at the C13-C14 position. The preference for each of the cleavage positions is determined by the hydroxylation and the nature of the ionone ring
-
-
?
additional information
?
-
-
MtCCO cleaves the central C15-C15' and an excentric double bond at the C13-C14 position. The preference for each of the cleavage positions is determined by the hydroxylation and the nature of the ionone ring
-
-
?
additional information
?
-
MtCCO cleaves the central C15-C15' and an excentric double bond at the C13-C14 position. The preference for each of the cleavage positions is determined by the hydroxylation and the nature of the ionone ring
-
-
?
additional information
?
-
enzyme exhibits a wide substrate specificity with respect to chain lengths and functional endgroups, converting beta-apo-carotenals, (3R)-3-hydroxy-beta-apocarotenals and the corresponding alcohols into retinal and (3R)-3-hydroxyretinal, respectively. Cleavage occurs at the C15-C15' double bond. No substrates: beta-apo-4'-carotenal, beta-apo-12'-carotenal
-
-
?
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
-
-
?
additional information
?
-
enzyme exhibits wide substrate specificity with respect to chain-lengths and functional end-groups
-
-
?
additional information
?
-
enzyme ACO exclusively produces all-trans-retinal from all-trans-apo-8'-carotenol. ACO cleaves but does not isomerize all-trans-8'-apocarotenol. Raman spectroscopic study, overview. During the entire reaction, spectroscopic signals for 13-cis-retinal or the 13,14'-di-cis-8-apocarotenol intermediate are not detected
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
all-trans-8'-apo-beta-carotenal + O2
all-trans-retinal + 8'-hydroxy-15'-apocarotenal
-
-
-
?
all-trans-8'-apocarotenol + O2
all-trans-retinal + (2E,4E,6E)-8-hydroxy-2,6-dimethylocta-2,4,6-trienal
-
-
-
?
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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
Fe2+
iron can occupy the enzyme metal binding site and is able to support the enzyme's catalytic activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hexaethylene glycol monooctyl ether
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
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
The Mycobacterium tuberculosis ORF Rv0654 encodes a carotenoid oxygenase mediating central and excentric cleavage of conventional and aromatic carotenoids.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics, Michaelis-Menten kinetics
-
0.0021
(3R)-3hydroxy-beta-apo-8'-carotenal
20°C, pH 6.8
0.121
all-trans-8'-apo-beta-carotenal
recombinant enzyme, pH 7.0, 28°C
0.127
all-trans-8'-apo-beta-carotenal
recombinant enzyme, pH 7.0, 28°C, in presence of 0.1 CMC C8E6
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
-
role of CCD1 as an ACO of C27 apocarotenoid intermediates, following their predicted export from plastid to cytosol
additional information
evolution
-
plant CCD1 enzymes and the NosCCD might have evolved into ACOs without losing their ability to cleave C40 carotenoids
evolution
ACO is a classical non-isomerizing member of the carotenoid cleavage enzyme (CCE) family
additional information
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACOX_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
490
0
54286
Swiss-Prot
-
A0A2I0B8N7_9ASPA
615
0
67096
TrEMBL
Chloroplast (Reliability: 4)
A0A1Z5K302_FISSO
540
0
60054
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2I0AZY4_9ASPA
626
0
69594
TrEMBL
Chloroplast (Reliability: 4)
A0A1Q9N9N0_ODILC
Odinarchaeota archaeon (strain LCB_4)
493
0
56708
TrEMBL
-
A0A654LU06_9ARCH
359
0
40821
TrEMBL
-
A0A1Z5J918_FISSO
547
0
60909
TrEMBL
Secretory Pathway (Reliability: 3)
CCO_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
501
0
54944
Swiss-Prot
-
Q8YPB4_NOSS1
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
497
0
55856
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging drop vapor diffusion method, using 0.1 mM Bis-tris propane-HCl, pH 6.0, 18-22% (w/v) sodium polyacrylate 2100, and 0.2 M NaCl
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, 2223% 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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
used as a homology model for 9-cis-epoxycarotenoid dioxygenase, EC 1.13.11.51
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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
-
gene sll1541, recombinant expression in Escherichia coli strain BL21
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boyd, J.; Gai, Y.; Nelson, K.M.; Lukiwski, E.; Talbot, J.; Loewen, M.K.; Owen, S.; Zaharia, L.I.; Cutler, A.J.; Abrams, S.R.; Loewen, M.C.
Sesquiterpene-like inhibitors of a 9-cis-epoxycarotenoid dioxygenase regulating abscisic acid biosynthesis in higher plants
Bioorg. Med. Chem.
17
2902-2912
2009
Synechocystis sp. PCC 6803 (P74334)
brenda
Ruch, S.; Beyer, P.; Ernst, H.; Al-Babili, S.
Retinal biosynthesis in Eubacteria: in vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803
Mol. Microbiol.
55
1015-1024
2005
Synechocystis sp. PCC 6803 (P74334)
brenda
Kloer, D.P.; Ruch, S.; Al-Babili, S.; Beyer, P.; Schulz, G.E.
The structure of a retinal-forming carotenoid oxygenase
Science
308
267-269
2005
Synechocystis sp. PCC 6803 (P74334)
brenda
Scherzinger, D.; Ruch, S.; Kloer, D.P.; Wilde, A.; Al-Babili, S.
Retinal is formed from apo-carotenoids in Nostoc sp. PCC7120: in vitro characterization of an apo-carotenoid oxygenase
Biochem. J.
398
361-369
2006
Nostoc sp. PCC 7120 = FACHB-418 (Q8YPB4)
brenda
Scherzinger, D.; Scheffer, E.; Bar, C.; Ernst, H.; Al-Babili, S.
The Mycobacterium tuberculosis ORF Rv0654 encodes a carotenoid oxygenase mediating central and excentric cleavage of conventional and aromatic carotenoids
FEBS J.
277
4662-4673
2010
Mycobacterium tuberculosis (P9WPR5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPR5)
brenda
Walter, M.H.; Floss, D.S.; Strack, D.
Apocarotenoids: hormones, mycorrhizal metabolites and aroma volatiles
Planta
232
1-17
2010
Synechocystis sp.
brenda
Sui, X.; Kiser, P.D.; Che, T.; Carey, P.R.; Golczak, M.; Shi, W.; von Lintig, J.; Palczewski, K.
Analysis of carotenoid isomerase activity in a prototypical carotenoid cleavage enzyme, apocarotenoid oxygenase (ACO)
J. Biol. Chem.
289
12286-12299
2014
Synechocystis sp. PCC 6803 (P74334)
brenda
Sui, X.; Farquhar, E.R.; Hill, H.E.; von Lintig, J.; Shi, W.; Kiser, P.D.
Preparation and characterization of metal-substituted carotenoid cleavage oxygenases
J. Biol. Inorg. Chem.
23
887-901
2018
Synechocystis sp. PCC 6803 (P74334)
brenda
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