Structural highlights
Function
ACOX_SYNY3 Cleaves a number of carotenals and carotenols in the all-trans configuration at the 15-15' double bond producing retinal or retinol, respectively. Also shows activity toward lycopenals and the corresponding alcohols. Does not cleave beta-carotene or lycopene.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Enzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and 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 changed 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.
The structure of a retinal-forming carotenoid oxygenase.,Kloer DP, Ruch S, Al-Babili S, Beyer P, Schulz GE Science. 2005 Apr 8;308(5719):267-9. PMID:15821095[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kloer DP, Ruch S, Al-Babili S, Beyer P, Schulz GE. The structure of a retinal-forming carotenoid oxygenase. Science. 2005 Apr 8;308(5719):267-9. PMID:15821095 doi:308/5719/267
