Identification of Isolevuglandin-CYP27A1 adducts in human retina. Cadaveric retinal sample was mixed with purified recombinant 15N-CYP27A1 modified with authentic isolevuglandin E2, hydrolyzed, and analyzed by multiple reaction monitoring. Transitions arising from endogenous isoLG-adducts were observed at identical retention times as those arising from the isoLGE2 modified 15N-CYP27A1 used as internal standard.
Retinal Pathology in CYP27A1 KO Mice As Revealed by Optical Coherence Tomography and
Plasticity of the CYP46A1 Active Site as Revealed by X-Ray Crystallography. Almost every amino acid residue in the active site of CYP46A1 can readjust its position to better fit the inhibitor molecule, thus explaining the unusual ability of this cholesterol-metabolizing P450 to bind pharmaceuticals of different size and shape.
Structural Basis For Three-step Sequential Catalysis by the Cytochrome P450 11A1 that Catalyzes the Conversion of Cholesterol to Pregnenolone. The network of structural water molecules (in violet) at the entrance to the CYP11A1 active site (contoured in green) allows the "soft" recognition of the hydroxyl group of the first reaction intermediate, 22R-hydroxycholesterol (in yellow) and enables sterol shuttling between the active site entrance and the heme group (in red), the site of catalysis. The protein backbone is represented as a gray ribbon.