Literature summary for 1.13.11.75 extracted from

Kloer, D.P.; Ruch, S.; Al-Babili, S.; Beyer, P.; Schulz, G.E.
The structure of a retinal-forming carotenoid oxygenase (2005), Science, 308, 267-269.

Search for more literature for 1.13.11.75

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Synechocystis sp. PCC 6803

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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	Synechocystis sp. PCC 6803

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp. PCC 6803	P74334	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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	Synechocystis sp. PCC 6803	a

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Release 2023.1 (January 2023)