Mechanistic enzymology of serine palmitoyltransferase

作者: Hiroko Ikushiro , Hideyuki Hayashi

DOI: 10.1016/J.BBAPAP.2011.02.005

关键词: Serine C-palmitoyltransferaseCondensation reactionEnzymeATP synthaseBiochemistryResidue (chemistry)StereochemistryPyridoxal phosphatePyridoxal 5-PhosphateSphingolipid biosynthesisChemistry

摘要: Serine palmitoyltransferase, which is one of the α-oxamine synthase family enzymes, catalyzes condensation reaction L-serine and palmitoyl-CoA to form 3-ketodihydrosphingosine, first rate-determining step sphingolipid biosynthesis. As with other catalytic composed multiple elementary steps, mechanism control these steps avoid side reactions has been subject intensive research in recent years. Combined spectroscopic, kinetic, structural studies have revealed finely controlled stereochemical mechanism, His residue conserved among enzymes plays a central critical role. This article part Special Issue entitled: Pyridoxal Phosphate Enzymology.

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