Carotenoid oxygenase
| Retinal pigment epithelial membrane protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
The Structure of a Retinal-Forming Carotenoid Oxygenase.
|
|||||||||
| Identifiers | |||||||||
| Symbol | RPE65 | ||||||||
| Pfam | PF03055 | ||||||||
| InterPro | IPR004294 | ||||||||
| SCOP | 2biw | ||||||||
| SUPERFAMILY | 2biw | ||||||||
| OPM superfamily | 111 | ||||||||
| OPM protein | 2biw | ||||||||
|
|||||||||
| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
Carotenoid oxygenases are a family of enzymes involved in the cleavage of carotenoids to produce, for example, retinol, commonly known as vitamin A. This family includes a receptor which is abundantly expressed in retinal pigment epithelium, and binds plasma retinal binding protein.
Carotenoids such as beta-carotene, lycopene, lutein and beta-cryptoxanthine are produced in plants and certain bacteria, algae and fungi, where they function as accessory photosynthetic pigments and as scavengers of oxygen radicals for photoprotection. They are also essential dietary nutrients in animals. Carotenoid oxygenases cleave a variety of carotenoids into a range of biologically important products, including apocarotenoids in plants that function as hormones, pigments, flavours, floral scents and defence compounds, and retinoids in animals that function as vitamins, visual pigments and signalling molecules. Examples of carotenoid oxygenases include:
This article incorporates text from the public domain Pfam and InterPro IPR004294
...
Wikipedia