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Updated: Jun 4, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
Mechanistic enzymology of serine palmitoyltransferase
Hiroko Ikushiro1, Hideyuki Hayashi
1Department of Biochemistry, Faculty of Medicine, Osaka Medical College, 2-7 Daigakumachi, Takatsuki 569-8686, Japan.
Abstract:
Serine palmitoyltransferase, which is one of the α-oxamine synthase family enzymes, catalyzes the condensation reaction of L-serine and palmitoyl-CoA to form 3-ketodihydrosphingosine, the first and rate-determining step of the sphingolipid biosynthesis. As with other α-oxamine synthase family enzymes, the catalytic reaction is composed of multiple elementary steps, and the mechanism to control these steps to avoid side reactions has been the subject of intensive research in recent years. Combined spectroscopic, kinetic, and structural studies have revealed the finely controlled stereochemical mechanism, in which the His residue conserved among the α-oxamine synthase family enzymes plays a central and critical role. This article is part of a Special Issue entitled: Pyridoxal Phosphate Enzymology.
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