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Carotenoid oxygenase
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. Additional recommended knowledgeCarotenoids 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[1]. Examples of carotenoid oxygenases include:
Human proteins containing this domainBCDO2; BCMO1; RPE65; References
This article includes text from the public domain Pfam and InterPro IPR004294 Categories: Carotenoids | Photosynthesis | Enzymes | Protein domains | Protein families | Peripheral membrane proteins |
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This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Carotenoid_oxygenase". A list of authors is available in Wikipedia. |