Lee Yingying, Furdui Cristina, Beamer Lesa J
Departments of Biochemistry and Chemistry, University of Missouri-Columbia, Columbia, MO 65211, United States.
Department of Internal Medicine, Wake Forest University Health Sciences, Winston-Salem, NC, USA.
Data Brief. 2016 Dec 15;10:398-405. doi: 10.1016/j.dib.2016.12.017. eCollection 2017 Feb.
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 from , 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.
α-D-磷酸己糖变位酶超家族中的大多数酶催化1-磷酸糖与6-磷酸糖之间的可逆转化。它们在碳水化合物和糖核苷酸代谢中发挥重要作用，并参与多糖、糖脂及其他外产物的生物合成。编码这些酶的基因突变与人类遗传性代谢疾病相关，包括糖原贮积病和先天性糖基化障碍。该超家族中的酶共享一个高度保守的活性位点丝氨酸，其参与多步磷酸基转移反应。在此，我们提供了各种磷酸糖配体对该丝氨酸磷酸化作用影响的数据，这些数据通过完整蛋白质的电喷雾电离质谱（ESI-MS）监测获得。我们还展示了来自该超家族一个成员的磷酸化酶在各种溶液条件下的寿命数据，并给出了几种配体的抑制数据。这些数据对于制备磷酸化或未磷酸化蛋白质的均一样品应是有用的，而这些样品对于这些酶的生物物理特性表征至关重要。
