1.13.11.75: all-trans-8'-apo-beta-carotenal 15,15'-oxygenase
This is an abbreviated version!
For detailed information about all-trans-8'-apo-beta-carotenal 15,15'-oxygenase, go to the full flat file.
Word Map on EC 1.13.11.75
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1.13.11.75
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apocarotenoids
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oxygenases
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synechocystis
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non-heme
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stilbene
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nceds
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zeaxanthin
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strigolactone
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all-trans-retinyl
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piceatannol
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4-vinylguaiacol
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end-groups
- 1.13.11.75
-
apocarotenoids
- oxygenases
- synechocystis
-
non-heme
- stilbene
-
nceds
- zeaxanthin
- strigolactone
-
all-trans-retinyl
- piceatannol
- 4-vinylguaiacol
-
end-groups
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
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Crystallization
Crystallization on EC 1.13.11.75 - all-trans-8'-apo-beta-carotenal 15,15'-oxygenase
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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
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