1.13.11.75: all-trans-8'-apo-beta-carotenal 15,15'-oxygenase

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For detailed information about all-trans-8'-apo-beta-carotenal 15,15'-oxygenase, go to the full flat file.

Reaction

Synonyms

ACO, apo-carotenoid oxygenase, apocarotenoid cleavage oxygenase, apocarotenoid oxygenase, apocarotenoid-15,15'-oxygenase, apocarotenoid-15-15'-oxygenase, carotenoid cleavage oxygenase, CCO, Diox1, EC 1.14.99.41, More, sll1541

ECTree

     1 Oxidoreductases

         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

             1.13.11 With incorporation of two atoms of oxygen

                1.13.11.75 all-trans-8'-apo-beta-carotenal 15,15'-oxygenase

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Results	in table
9	AA Sequence
4	Cloned(Commentary)
4	Crystallization (Commentary)
5	General Information
5	Inhibitors
16	KM Value [mM]
3	Localization
4	Metals/Ions
3	Natural Substrates/ Products (Substrates)
9	Organism
39	PDB ID
2	pH Optimum
1	Protein Variants
1	Purification (Commentary)
3	Reaction
9	Reference
1	Specific Activity [micromol/min/mg]
37	Substrates and Products (Substrate)
2	Subunits
19	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
4	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.13.11.75 - all-trans-8'-apo-beta-carotenal 15,15'-oxygenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

three-dimensional structure analysis

Synechocystis sp.

-

716649

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

Synechocystis sp. PCC 6803

P74334

706756

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

Synechocystis sp. PCC 6803

P74334

765090

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

P74334

745295