title: From the configurational preference of dihydroceramide desaturase-1 towards Δ6-unsaturated substrates to the discovery of a new inhibitor.
abstract: Dihydroceramide desaturase 1 (Des1) catalyzes the last step of ceramide synthesis de novo, thus regulating the physiologically relevant balance between dihydrosphingolipids and sphingolipids. Here we report on the configurational preference of Des1 towards isomeric Δ6-unsaturated dihydroceramide analogs and the discovery of a potent Des1 inhibitor.
authors.affiliation: Spanish National Research Council (CSIC), Institute of Advanced Chemistry of Catalonia (IQAC-CSIC), Research Unit on Bioactive Molecules (RUBAM), Department of Biomedicinal Chemistry, Jordi Girona 18-26, 08034-Barcelona, Spain. gemma.fabrias@iqac.csic.es delgado@rubam.net.
authors.forename: Ana
authors.initials: A
authors.lastname: Pou
authors.forename: José-Luís
authors.initials: JL
authors.lastname: Abad
authors.forename: Yadira F
authors.initials: YF
authors.lastname: Ordóñez
authors.forename: Maria
authors.initials: M
authors.lastname: Garrido
authors.forename: Josefina
authors.initials: J
authors.lastname: Casas
authors.forename: Gemma
authors.initials: G
authors.lastname: Fabriàs
authors.forename: Antonio
authors.initials: A
authors.lastname: Delgado
mesh_terms: D045744:Cell Line, Tumor; D002518:Ceramides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D057930:Click Chemistry; D057075:Enzyme Assays; D044943:Fatty Acid Desaturases / Q000037:antagonists & inhibitors* / Q000737:chemistry; D006801:Humans; D007536:Isomerism; D007700:Kinetics; D013379:Substrate Specificity
chemical_list: D002518:Ceramides; D044943:Fatty Acid Desaturases; C106615:DEGS1 protein, human