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EC Tree
IUBMB Comments Contains an Fe2+-4His arrangement. The enzyme is involved in retinal biosynthesis in bacteria .
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
carotenoid cleavage oxygenase, apocarotenoid oxygenase, apocarotenoid cleavage oxygenase, apocarotenoid-15-15'-oxygenase,
sll1541 ,
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apo-carotenoid oxygenase
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apocarotenoid cleavage oxygenase
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apocarotenoid oxygenase
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apocarotenoid-15,15'-oxygenase
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apocarotenoid-15-15'-oxygenase
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carotenoid cleavage oxygenase
additional information
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ACO belongs to an outgroup of the CCO enzyme family
ACO
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carotenoid cleavage oxygenase
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carotenoid cleavage oxygenase
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CCO
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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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-
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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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(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
-
-
?
3,3'-dihydoxyisorenieratene + O2
?
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
-
?
9'-cis-neoxanthin + O2
?
-
-
?
all-trans-(3R)-hydroxy-8'-apo-beta-carotenol + O2
?
-
-
?
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
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-
?
all-trans-beta-apo-8'-carotenal + O2
all-trans-retinal + apo-8'15'-apo-carotenedial
the cis-isomer is not a substrate
-
?
apo-10'-lycopenal + O2
acycloretinal + ?
-
-
?
apo-8'-lycopenal + O2
acycloretinal + ?
-
-
?
apo-8'-lycopenol + O2
acycloretinal + ?
-
-
?
beta-apo-10'-carotenal + O2
?
beta-apo-10'-carotenal + O2
retinal + ?
-
-
?
beta-apo-8'-carotenal + O2
?
beta-apo-8'-carotenal + O2
retinal + apo-8',15'-apo-carotenedial
-
-
?
beta-apo-8'-carotenol + 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
-
?
additional information
?
-
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
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?
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
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?
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
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-
?
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
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?
zeaxanthin + O2
?
83% cleavage at C15-C15' double bond, 17% cleavage at the C13-C14 double bond
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?
additional information
?
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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
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?
additional information
?
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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
?
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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
?
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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
?
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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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?
additional information
?
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enzyme exhibits wide substrate specificity with respect to chain-lengths and functional end-groups
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?
additional information
?
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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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?
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all-trans-8'-apocarotenol + O2
all-trans-retinal + (2E,4E,6E)-8-hydroxy-2,6-dimethylocta-2,4,6-trienal
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-
-
?
additional information
?
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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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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
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CYMAL-4
slight inhibition
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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0.0026
(3R)-3hydroxy-beta-apo-12'-carotenal
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
steady-state kinetics, Michaelis-Menten kinetics
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0.0014
(3R)-3hydroxy-beta-apo-8'-carotenal
pH 7.0, 27°C
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
0.017
beta-apo-10'-carotenal
20°C, pH 6.8
0.0294
beta-apo-10'-carotenal
pH 7.9, 28°C
0.00415
beta-apo-8'-carotenal
pH 7.9, 28°C
0.016
beta-apo-8'-carotenal
20°C, pH 6.8
0.0245
beta-apo-8'-carotenol
20°C, pH 6.8
0.043
beta-apo-8'-carotenol
pH 7.0, 27°C
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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
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0.47
purified recombinant enzyme, pH 7.0, 28°C
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UniProt
brenda
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UniProt
brenda
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UniProt
brenda
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brenda
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UniProt
brenda
strain PCC 6803
UniProt
brenda
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brenda
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brenda
monotopic membrane protein
brenda
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physiological function
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role of CCD1 as an ACO of C27 apocarotenoid intermediates, following their predicted export from plastid to cytosol
evolution
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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
active site structure, overview
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
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ACOX_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
490
0
54286
Swiss-Prot
-
A0A1Q9N9N0_ODILC
Odinarchaeota archaeon (strain LCB_4)
493
0
56708
TrEMBL
-
A0A1Z5K302_FISSO
540
0
60054
TrEMBL
Secretory Pathway (Reliability: 4 )
A0A654LU06_9ARCH
359
0
40821
TrEMBL
-
A0A2I0B8N7_9ASPA
615
0
67096
TrEMBL
Chloroplast (Reliability: 4 )
A0A2I0AZY4_9ASPA
626
0
69594
TrEMBL
Chloroplast (Reliability: 4 )
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
-
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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)
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)
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additional information
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three-dimensional structure analysis
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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
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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additional information
used as a homology model for 9-cis-epoxycarotenoid dioxygenase, EC 1.13.11.51
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recombinant enzyme from Escherichia coli strain BL21 by ammonium sulfate fractionation and gel filtration
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DNA and amino acid sequence determination and analysis, phylogenetic tree
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expression in Escherichia coli
gene sll1541, recombinant expression in Escherichia coli strain BL21
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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
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1.13.11.75 all-trans-8'-apo-beta-carotenal 15,15'-oxygenase
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