SPTLC1 Inhibitors

SPTLC1 inhibitors encompass a range of compounds that target the serine palmitoyltransferase complex, either directly or indirectly, to modulate sphingolipid biosynthesis. These inhibitors can be classified based on their mode of action and the specific part of the sphingolipid biosynthesis pathway they influence. While some compounds like Myriocin and ISP-1 act directly on SPTLC1 or its complex, others, such as Fumonisin B1 and SAF, target downstream enzymes like ceramide synthase, indirectly influencing the function of SPTLC1.

The chemical diversity of these inhibitors is notable, ranging from natural products like Myriocin to synthetic compounds like Fenretinide. Their modes of action are equally varied: some, like L-Cycloserine, are substrate analogs that compete with natural substrates of SPTLC1, while others, such as C75 and Cerulenin, inhibit enzymes involved in fatty acid metabolism, thereby affecting the availability of substrates necessary for SPTLC1 function. This diversity underscores the complex interplay between different metabolic pathways and how modulation of one enzyme can have cascading effects on related pathways.