EC Number | Cloned (Comment) | Organism |
---|---|---|
1.13.11.75 | gene sll1541, recombinant expression in Escherichia coli strain BL21 | Synechocystis sp. PCC 6803 |
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, 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 | Synechocystis sp. PCC 6803 |
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 |
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 |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.75 | Synechocystis sp. PCC 6803 | P74334 | - |
- |
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 |
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 |
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 |
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 | ? | - |
? |
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 |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.13.11.75 | 28 | - |
assay at | Synechocystis sp. PCC 6803 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.13.11.75 | 7 | - |
assay at | Synechocystis sp. PCC 6803 |
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 |