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Literature summary extracted from

  • 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) (2014), J. Biol. Chem., 289, 12286-12299 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.75 gene sll1541, recombinant expression in Escherichia coli strain BL21 Synechocystis sp. PCC 6803

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.75 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 Synechocystis sp. PCC 6803

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.75 CHAPS slight inhibition Synechocystis sp. PCC 6803
1.13.11.75 CYMAL-4 slight inhibition Synechocystis sp. PCC 6803
1.13.11.75 hexaethylene glycol monooctyl ether strongly inhibits ACO activity even at concentrations below its critical micelle concentration Synechocystis sp. PCC 6803
1.13.11.75 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 Synechocystis sp. PCC 6803
1.13.11.75 tetraethylene glycol monooctyl ether strongly inhibits ACO activity even at concentrations below its critical micelle concentration Synechocystis sp. PCC 6803

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.75 additional information
-
additional information steady-state kinetics, Michaelis-Menten kinetics Synechocystis sp. PCC 6803
1.13.11.75 0.121
-
all-trans-8'-apo-beta-carotenal recombinant enzyme, pH 7.0, 28°C Synechocystis sp. PCC 6803
1.13.11.75 0.127
-
all-trans-8'-apo-beta-carotenal recombinant enzyme, pH 7.0, 28°C, in presence of 0.1 CMC C8E6 Synechocystis sp. PCC 6803

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.75 all-trans-8'-apocarotenol + O2 Synechocystis sp. PCC 6803
-
all-trans-retinal + (2E,4E,6E)-8-hydroxy-2,6-dimethylocta-2,4,6-trienal
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.75 Synechocystis sp. PCC 6803 P74334
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.75 recombinant enzyme from Escherichia coli strain BL21 by ammonium sulfate fractionation and gel filtration Synechocystis sp. PCC 6803

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.75 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 Synechocystis sp. PCC 6803

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.13.11.75 0.47
-
purified recombinant enzyme, pH 7.0, 28°C Synechocystis sp. PCC 6803

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.75 all-trans-8'-apo-beta-carotenol + O2
-
Synechocystis sp. PCC 6803 all-trans-retinal + (2E,4E,6E)-8-hydroxy-2,6-dimethylocta-2,4,6-trienal
-
?
1.13.11.75 all-trans-8'-apocarotenol + O2
-
Synechocystis sp. PCC 6803 all-trans-retinal + (2E,4E,6E)-8-hydroxy-2,6-dimethylocta-2,4,6-trienal
-
?
1.13.11.75 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 Synechocystis sp. PCC 6803 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.75 ACO
-
Synechocystis sp. PCC 6803
1.13.11.75 apocarotenoid oxygenase
-
Synechocystis sp. PCC 6803
1.13.11.75 sll1541
-
Synechocystis sp. PCC 6803

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.75 28
-
assay at Synechocystis sp. PCC 6803

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.75 7
-
assay at Synechocystis sp. PCC 6803

General Information

EC Number General Information Comment Organism
1.13.11.75 evolution ACO is a classical non-isomerizing member of the carotenoid cleavage enzyme (CCE) family Synechocystis sp. PCC 6803
1.13.11.75 additional information active site structure, overview Synechocystis sp. PCC 6803