Serine C-palmitoyltransferase

In enzymology, a serine C-palmitoyltransferase is an enzyme that catalyzes the chemical reaction


 * palmitoyl-CoA + L-serine $$\rightleftharpoons$$ CoA + 3-dehydro-D-sphinganine + CO2

Thus, the two substrates of this enzyme are palmitoyl-CoA and L-serine, whereas its 3 products are CoA, 3-dehydro-D-sphinganine, and CO2.

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.

Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and.