Abstract 1489 Exploring the activity of short-chain dehydrogenases/reductases SDR16C5 and SDR16C6 in fatty aldehyde biosynthetic pathway using liquid chromatography/mass spectrometry

PURPOSE: It has been reported that the short chain dehydrogenase/reductase family 16C member 5 (SDR16C5) is an essential enzyme of all-trans-retinoic acid (RA) biosynthetic pathway which is critical for vision and embryogenesis, among other processes. The enzyme was demonstrated to catalyze the NAD+-dependent oxidation of retinol (RAlc) to retinaldehyde (RAld) in Reaction 1: RAlc → RAld. However, based on the known broad substrate specificity of SDRs, we have hypothesized that SDR16C5/C6 may be involved in another type of reactions, specifically oxidation of very long chain saturated and unsaturated fatty alcohols (FAlc) into fatty aldehydes (FAld) in Meibomian glands.