Serine C-palmitoyltransferase

serine C-palmitoyltransferase
Identifiers
EC no.2.3.1.50
CAS no.62213-50-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
Serine palmitoyltransferase
Crystallographic structure of serine palmitoyltransferase from S. paucimobilis. The cofactor PLP is visible in the center.[1]
Identifiers
SymbolSPT1
PDB2JG2
UniProtQ93UV0
Other data
EC number2.3.1.50
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StructuresSwiss-model
DomainsInterPro
serine palmitoyltransferase, long chain base subunit 1
Identifiers
SymbolSPTLC1
Alt. symbolsHSN1
NCBI gene10558
HGNC11277
OMIM605712
RefSeqNM_006415
UniProtO15269
Other data
EC number2.3.1.50
LocusChr. 9 q22.31
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StructuresSwiss-model
DomainsInterPro
serine palmitoyltransferase, long chain base subunit 2
Identifiers
SymbolSPTLC2
NCBI gene9517
HGNC11278
OMIM605713
RefSeqNM_004863
UniProtO15270
Other data
EC number2.3.1.50
LocusChr. 14 q24.3
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StructuresSwiss-model
DomainsInterPro
serine palmitoyltransferase, long chain base subunit 3
Identifiers
SymbolSPTLC3
Alt. symbolsC20orf38, SPTLC2L
NCBI gene55304
HGNC16253
OMIM611120
RefSeqNM_018327
UniProtQ9NUV7
Other data
EC number2.3.1.50
LocusChr. 20 p12.1
Search for
StructuresSwiss-model
DomainsInterPro

In enzymology, a serine C-palmitoyltransferase (EC 2.3.1.50) is an enzyme that catalyzes the chemical reaction:[2][3]

palmitoyl-CoA + L-serine 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.[4][5] This reaction is a key step in the biosynthesis of sphingosine which is a precursor of many other sphingolipids.[3]

This enzyme participates in sphingolipid metabolism. It employs one cofactor, pyridoxal phosphate.

  1. ^ 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". Journal of Molecular Biology. 370 (5): 870–86. doi:10.1016/j.jmb.2007.04.086. PMID 17559874. S2CID 7140511.
  2. ^ Ikushiro H, Hayashi H, Kagamiyama H (April 2003). "Bacterial serine palmitoyltransferase: a water-soluble homodimeric prototype of the eukaryotic enzyme". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1647 (1–2): 116–20. doi:10.1016/S1570-9639(03)00074-8. PMID 12686119.
  3. ^ a b Hanada K (June 2003). "Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1632 (1–3): 16–30. doi:10.1016/S1388-1981(03)00059-3. PMID 12782147.
  4. ^ Brady RN, Di Mari SJ, Snell EE (January 1969). "Biosynthesis of sphingolipid bases. 3. Isolation and characterization of ketonic intermediates in the synthesis of sphingosine and dihydrosphingosine by cell-free extracts of Hansenula ciferri". The Journal of Biological Chemistry. 244 (2): 491–6. doi:10.1016/S0021-9258(18)94455-8. PMID 4388074.
  5. ^ Stoffel W, LeKim D, Sticht G (May 1968). "Biosynthesis of dihydrosphingosine in vitro". Hoppe-Seyler's Zeitschrift für Physiologische Chemie. 349 (5): 664–70. doi:10.1515/bchm2.1968.349.1.664. PMID 4386961.