1007221-00-2Relevant academic research and scientific papers
Stereospecificity of retinol saturase: Absolute configuration, synthesis, and biological evaluation of dihydroretinoids
Moise, Alexander R.,Dominguez, Marta,Alvarez, Susana,Alvarez, Rosana,Schupp, Michael,Cristancho, Ana G.,Kiser, Philip D.,De Lera, Angel R.,Lazar, Mitchell A.,Palczewski, Krzysztof
, p. 1154 - 1155 (2008/10/09)
Retinol saturase carries out a stereospecific saturation of the C13-C14 double bond of all-trans-retinol to generate (13R)-all-trans-13,14-dihydroretinol. This compound is found in cells expressing mouse or zebrafish retinol saturase and in the livers of mice fed retinyl palmitate. All-trans-13,14-dihydroretinol is oxidized in vivo to all-trans-13,14-dihydroretinoic acid, a highly selective agonist of the retinoic acid receptor. The naturally occurring (13R)-all-trans-13,14-dihydroretinoic acid is a weaker agonist than the (13S) enantiomer, indicating enantioselective recognition by the ligand-binding pocket of this receptor. Consequently the (13S) enantiomer, acting through the retinoic acid receptor, also inhibits adipose differentiation more potently than the (13R) enantiomer. Copyright
