Cloning and characterization of a cDNA encoding serine palmitoyltransferase in Arabidopsis thaliana.

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Tamura K, Nishiura H, Mori J, Imai H

Cloning and characterization of a cDNA encoding serine palmitoyltransferase in Arabidopsis thaliana.

Biochem Soc Trans. 2000 Dec;28(6):745-7.

PubMed ID

11171191 [ View in PubMed

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Abstract

The first and committed step in de novo sphingolipid synthesis is catalysed by serine palmitoyltransferase (EC 2.3.1.50), which condenses serine and palmitoyl-CoA to form 3-ketosphinganine in a pyridoxal-5'-phosphate-dependent reaction. We have isolated and characterized a cDNA clone from Arabidopsis thaliana that is homologous to yeast and mammalian LCB2. For a functional identification, the A. thaliana homologous cDNA was expressed in Escherichia coli, which resulted in significant production of new sphinganine in E. coli cells.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Pyridoxal phosphate	Serine palmitoyltransferase 2	Protein	Humans	Unknown	Cofactor	Details