Serine palmitoyltransferase

From Proteopedia

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Template:STRUCTURE 3a2b

Function

Serine palmitoyltransferase (SPT) catalyzes the conversion of palmitoyl-CoA and serine to CoA and dehydro-sphinganine. This reaction is part of sphingosine biosynthesis. Pyridoxal phosphate (PLP) is a cofactor in the reaction. The prokaryotic SPT is a soluble homodimer while the eukaryotic one is heterodimeric and is anchored in the endoplasmic reticulum^[1].

3D structures of serine palmitoyltransferase

Updated on 25-August-2016

2jg2 – PpSPT + aldimine – Pseudomonas paucimobilis
2jgt – PpSPT
2w8j - SpSPT + aldimine – Sphingomonas paucimobilis
2w8t, 2w8u, 2w8v, 2w8w - SpSPT (mutant) + aldimine
4bmk - SpSPT (mutant) + myriocin + PLP
2xbn – SpSPT + pyridoxamine phosphate
3a2b – SPT + pyridoxal phosphate + serine – Sphingobacterium multivorum
2x8u - SwSPT + pyridoxal derivative – Sphingomonas wittichii

References

1. ↑ Hanada K. Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Biochim Biophys Acta. 2003 Jun 10;1632(1-3):16-30. PMID:12782147