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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.
Species distribution
This enzyme is expressed in a large number of species from bacteria to humans. The bacterial enzyme is a water-soluble homodimer[2] whereas in eukaryotes the enzyme is a heterodimer which is anchored to the endoplasmic reticulum.[3] 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.[6] However more recent data suggest that the enzyme may exist as a larger complex, possibly an octamer, comprising all three subunits.[7]
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2JG2 and 2JGT.[1]
References
^ abPDB: 2JG2; 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^ abIkushiro H, Hayashi H, Kagamiyama H (April 2003). "Bacterial serine palmitoyltransferase: a water-soluble homodimeric prototype of the eukaryotic enzyme". Biochim. Biophys. Acta. 1647 (1–2): 116–20. doi:10.1016/S1570-9639(03)00074-8. PMID12686119.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^ abcHanada K (June 2003). "Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism". Biochim. Biophys. Acta. 1632 (1–3): 16–30. doi:10.1016/S1388-1981(03)00059-3. PMID12782147.
^Stoffel W, LeKim D, Sticht G (May 1968). "Biosynthesis of dihydrosphingosine in vitro". Hoppe-Seyler's Z. Physiol. Chem. 349 (5): 664–70. doi:10.1515/bchm2.1968.349.1.664. PMID4386961.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^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.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
