Retinol dehydrogenase 16 (RDH16)

Retinol dehydrogenase 16 (RDH16) is an NAD+-dependent enzyme in the short-chain dehydrogenase/reductase (SDR) family that catalyzes the oxidation of all-trans-, 9-cis-, 11-cis-, and 13-cis-retinol to their respective retinaldehyde forms, playing a central role in cellular retinoic acid biosynthesis and broader vitamin A metabolism[3][5]. It shows preference for retinol bound to cellular retinol-binding protein (CRBP) and is primarily located in the endoplasmic reticulum of various tissues, especially skin and liver[3][4]. RDH16 is implicated in steroid metabolism and has been identified as a tumor suppressor in hepatocellular carcinoma, where downregulation correlates with tumor progression and poor prognosis[2]. Beyond cancer, its family role is critical in visual cycle biochemistry, although RDH16 itself is not the main enzyme in the retina. It is currently regarded as a prospective drug target for modulating retinoid pathways and influencing cell proliferation[2][5].

Other names

Retinol dehydrogenase 16 (all-trans and 13-cis)Retinol dehydrogenase 16 (all-trans)RDH16RoDH4RODH4SDR9C8hRDH-EHuman epidermal retinol dehydrogenaseMicrosomal NAD+-dependent retinol dehydrogenase 4Short chain dehydrogenase/reductase family 9C member 8Sterol/retinol dehydrogenaseRODH-4

Enzyme inhibition (by competitive small molecule inhibitors like certain retinoids)[1]; Modulation of enzyme expression to alter retinoic acid synthesis and fatty acid metabolism (e.g., upregulation reduces cancer proliferation)[2]