The Structure of Serine Palmitoyltransferase; Gateway to Sphingolipid Biosynthesis

• Published in: Journal of molecular biology Vol. 370; no. 5; pp. 870 - 886
• Main Authors: Yard, Beverley A., Carter, Lester G., Johnson, Kenneth A., Overton, Ian M., Dorward, Mark, Liu, Huanting, McMahon, Stephen A., Oke, Muse, Puech, Daphné, Barton, Geoffrey J., Naismith, James H., Campopiano, Dominic J.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 27.07.2007
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - physiology; Binding Sites; bioinformatics; Computational Biology; Dimerization; hereditary sensory and autonomic neuropathy type I; Holoenzymes - chemistry; Humans; Models, Molecular; Molecular Sequence Data; Mutation; Protein Conformation; Protein Subunits - chemistry; Protein Subunits - genetics; Protein Subunits - physiology; Serine C-Palmitoyltransferase - chemistry; Serine C-Palmitoyltransferase - genetics; Serine C-Palmitoyltransferase - physiology; serine palmitoyltransferase; sphingolipids; Sphingolipids - biosynthesis; Sphingomonas - enzymology; Sphingomonas paucimobilis; X-ray crystallography; hereditary sensory and autonomic neuropathy type I; GSL; ALAS; HSAN1; AOS; sphingolipids; LCB; RMSD; serine palmitoyltransferase; AONS; LPS; X-ray crystallography; CoA; KBL; PLP; SPT; bioinformatics; KDS

Sphingolipid biosynthesis commences with the condensation of L-serine and palmitoyl-CoA to produce 3-ketodihydrosphingosine (KDS). This reaction is catalysed by the PLP-dependent enzyme serine palmitoyltransferase (SPT; EC 2.3.1.50), which is a membrane-bound heterodimer (SPT1/SPT2) in eukaryotes su...