作者: Hiroko Ikushiro , Hideyuki Hayashi
DOI: 10.1016/J.BBAPAP.2011.02.005
关键词: Serine C-palmitoyltransferase 、 Condensation reaction 、 Enzyme 、 ATP synthase 、 Biochemistry 、 Residue (chemistry) 、 Stereochemistry 、 Pyridoxal phosphate 、 Pyridoxal 5-Phosphate 、 Sphingolipid biosynthesis 、 Chemistry
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.