This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is palmitoyl-CoA:L-serine C-palmitoyltransferase (decarboxylating). Other names in common use include serine palmitoyltransferase, SPT, 3-oxosphinganine synthetase, and acyl-CoA:serine C-2 acyltransferase decarboxylating. This enzyme participates in sphingolipid metabolism. It employs one cofactor, pyridoxal phosphate.
This enzyme is expressed in a large number of species from bacteria to humans. The bacterial enzyme is a water soluble homodimer whereas in eukaryotes the enzyme is a heterodimer which is anchored to the endoplasmic reticulum. Humans and other mammals express three paralogous subunits SPTLC1, SPTLC2, and SPTLC3. It was originally proposed that the functional human enzyme is a heterodimer between a SPTLC1 subunit and a second subunit which is either SPTLC2 or SPTLC3. However more recent data suggest that the enzyme may exist as a larger complex, possibly an octamer, comprising all three subunits.
^ abPDB2JG2; Yard BA, Carter LG, Johnson KA, Overton IM, Dorward M, Liu H, McMahon SA, Oke M, Puech D, Barton GJ, Naismith JH, Campopiano DJ (July 2007). "The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis". J. Mol. Biol.370 (5): 870–86. doi:10.1016/j.jmb.2007.04.086. PMID17559874.
^ abIkushiro H, Hayashi H, Kagamiyama H (April 2003). "Bacterial serine palmitoyltransferase: a water-soluble homodimeric prototype of the eukaryotic enzyme". Biochim. Biophys. Acta1647 (1-2): 116–20. doi:10.1016/S1570-9639(03)00074-8. PMID12686119.
^Hornemann T, Richard S, Rütti MF, Wei Y, von Eckardstein A (December 2006). "Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase". J. Biol. Chem.281 (49): 37275–81. doi:10.1074/jbc.M608066200. PMID17023427.