title: Mechanistic enzymology of serine palmitoyltransferase.
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.
authors.affiliation: Department of Biochemistry, Faculty of Medicine, Osaka Medical College, 2-7 Daigakumachi, Takatsuki 569-8686, Japan.
authors.forename: Hiroko
authors.initials: H
authors.lastname: Ikushiro
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Hayashi
mesh_terms: D002264:Carboxylic Acids / Q000378:metabolism; D008958:Models, Molecular; D011522:Protons; D051102:Serine C-Palmitoyltransferase / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D002264:Carboxylic Acids; D011522:Protons; D051102:Serine C-Palmitoyltransferase