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Article

The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis.

Journal of molecular biology - 27 Jul 2007

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

Abstract excerpt

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 such as humans and yeast and a cytoplasmic homodimer in the Gram-negative bacterium Sphingomonas paucimobilis....

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Identifiers

PMID: 17559874
DOI: 10.1016/j.jmb.2007.04.086

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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