Abstract 2204 A Conserved α-Helix in β-Carotene-Oxygenase-2 Substantially Modulates Enzyme Activity

In vertebrates, carotenoids serve important functions in vision, cell differentiation, immunity, metabolism, and development. To become biologically active these lipids are enzymatically converted by carotenoid cleavage dioxygenases (CCDs) like β-Carotene-Oxygenase-2 (BCO2). CCDs catalyze a reaction at the lipid water interface and convert carotenoid substrates into more polar apocarotenoids. Structural and biochemical studies have identified the active site and elucidated the general mechanism of carotenoid binding and cleavage of murine BCO2 (mBCO2), which occurs within a broadly specific substrate-binding tunnel.