Serine palmitoyltransferase long chain base subunit 3 (SPTLC3)

Serine palmitoyltransferase long chain base subunit 3 (SPTLC3) is a component of the serine palmitoyltransferase (SPT) enzyme complex, which catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and an acyl-CoA substrate. SPTLC3 is homologous to the canonical SPTLC2 subunit but is functionally distinct, enabling the enzyme complex to utilize shorter acyl-CoA substrates, leading to the generation of a range of sphingoid base species—including C14 and C16 sphingoid bases and methyl-branched long-chain bases—especially in tissues where SPTLC3 is highly expressed (e.g., certain brain regions and liver)[2][3]. Alterations in SPTLC3 activity or expression have been associated with dysregulated sphingolipid metabolism and implicated in metabolic, neurodegenerative, and cancer pathophysiology. SPTLC3 is a target for experimental drugs such as myriocin, which act via direct active site inhibition[1][4].

Other names

Serine palmitoyltransferase 3SPTLC3C20orf38SPTLC2LLCB2bLCB 3SPT 3FLJ11112hLCB2blong chain base biosynthesis protein 2blong chain base biosynthesis protein 3serine-palmitoyl-CoA transferase 3dJ718P11dJ718P11.1

Competitive inhibition of the serine palmitoyltransferase active site (by myriocin and analogs)[1]