title: Data on the phosphorylation state of the catalytic serine of enzymes in the α-D-phosphohexomutase superfamily.
abstract: Most enzymes in the α-D-phosphohexomutase superfamily catalyze the reversible conversion of 1- to 6-phosphosugars. They play important roles in carbohydrate and sugar nucleotide metabolism, and participate in the biosynthesis of polysaccharides, glycolipids, and other exoproducts. Mutations in genes encoding these enzymes are associated with inherited metabolic diseases in humans, including glycogen storage disease and congenital disorders of glycosylation. Enzymes in the superfamily share a highly conserved active site serine that participates in the multi-step phosphoryl transfer reaction. Here we provide data on the effects of various phosphosugar ligands on the phosphorylation of this serine, as monitored by electrospray ionization mass spectrometry (ESI-MS) data on the intact proteins. We also show data on the longevity of the phospho-enzyme under various solution conditions in one member of the superfamily fromPseudomonas aeruginosa, and present inhibition data for several ligands. These data should be useful for the production of homogeneous samples of phosphorylated or unphosphorylated proteins, which are essential for biophysical characterization of these enzymes.
authors.affiliation: Departments of Biochemistry and Chemistry, University of Missouri-Columbia, Columbia, MO 65211, United States.
authors.forename: Yingying
authors.initials: Y
authors.lastname: Lee
authors.affiliation: Department of Internal Medicine, Wake Forest University Health Sciences, Winston-Salem, NC, USA.
authors.forename: Cristina
authors.initials: C
authors.lastname: Furdui
authors.affiliation: Departments of Biochemistry and Chemistry, University of Missouri-Columbia, Columbia, MO 65211, United States.
authors.forename: Lesa J
authors.initials: LJ
authors.lastname: Beamer
keywords: Active site; Enzymes; Mass spectrometry; Phosphorylation