SPTLC complexes transfer acyl-CoA onto serine
L-Ser + acyl-CoA + H+ → CoA-SH + CO2 + 3-ketosphingoid
- Reactome
- R-HSA-428127
- Compartment
- cytosol · endoplasmic reticulum membrane
- Rhea
- None recorded
Inputs
- L-SerCHEBI:33384, C3H7NO3, cytosol
- acyl-CoACHEBI:58342, C22H31N7O17P3SR, cytosol
- H+CHEBI:15378, H, cytosol
Outputs
- CoA-SHCHEBI:57287, C21H32N7O16P3S, cytosol
- CO2CHEBI:16526, CO2, cytosol
- 3-ketosphingoidCHEBI:84411, C3H7NO2R, endoplasmic reticulum membrane
Catalysed by
- serine C-palmitoyltransferase activity of SPTLC complexes [endoplasmic reticulum membrane]EC 2.3.1.50
Literature
- Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase J Biol Chem, 2006
- Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis Eur J Biochem, 1997
- Is the mammalian serine palmitoyltransferase a high-molecular-mass complex? Biochem J, 2007
- Purification of the serine palmitoyltransferase complex responsible for sphingoid base synthesis by using affinity peptide chromatography techniques J Biol Chem, 2000
- Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities Proc. Natl. Acad. Sci. U.S.A., 2009
- Orm family proteins mediate sphingolipid homeostasis Nature, 2010