Cholesterol binding to the carotenoid binding site in Strawberry Dioxygenase

Alok Jha; Ramasare Prasad

Volume : VI, Issue : II, February - 2016

Cholesterol binding to the carotenoid binding site in Strawberry Dioxygenase

Alok Jha, Ramasare Prasad

Abstract :

The 2–oxoglutarate (2–OG) dependent dioxygenases have an absolute requirement for Fe (II) and catalyze a variety of two electron oxidations, including hydroxylation, desaturation and oxidative ring closure reactions. Here, we report a novel α–epoxycholesterol binding to the 9–cis–epoxycarotenoid binding site of dioxygenase in strawberry. The structure model suggests an unusual mode of α–epoxycholesterol binding in the 9–cis–epoxycarotenoid binding pocket that explains the possible location and mechanism for α–epoxycholesterol or lipid oxidation while transferring oxidized lipid in the low density lipoprotein (LDL) and high density lipoprotein (HDL) from chylomicron and chylomicron remnants (CM/CR). The structure can sufficiently produce a measureable improvement by supporting theories pertaining to the oxidation of lipids by dioxygenase. We anticipate that the dioxygenase–9–cis–epoxycarotenoid and α–epoxycholesterol structure complex model will aid to the development of cholesterol lowering drugs and in understanding the mechanism of dietary lipid oxidation.