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.