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Proteins/UNIPROT:O15270
Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference. Crucial for adipogenesis (By similarity)..
Function from UniProtKB (O15270), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
3 rows
131 statements
131 statements · 8 reference databases · Subject: SPTLC2 · Sources: Bgee, gene ontology, Hetionet, Human-GEM, Reactome, Rhea, UniProt, WikiPathways
3 reactions
proton+palmitoyl-CoA+L-seryl residue3-oxosphinganine+carbon dioxide+CHEBI:1146900
Catalysed by SPTLC1 & SPTLC2 & SPTLC3
Reaction pageLeft to rightBalancedEC 2.3.1.50cytosol
Human-GEM MAR00738CC BY 4.0Reference data
8 names
Resolves to: SPTLC2
Reaction pageLeft to rightBalanced
Rhea RHEA:14761CC BY 4.0Reference data
octadecanoyl-CoA+L-seryl residue+hydron3-oxoeicosasphinganine+carbon dioxide+coenzyme A(4-)
Catalysed by SPTLC1 or SPTLC2 or SPTLC3
Reaction pageLeft to rightBalanced
Rhea RHEA:33683CC BY 4.0Reference data