alpha-2,3-Sialyltransferase (PmST2)

MBP-PmST2-His6 (2 mM acceptor; 0-60 min) exhibits higher α2-3-sialyltransferase activity toward LacβPro-triazole-C14 than toward LacβPro2AA under the tested conditions^[1].
MBP-PmST2-His6 (2 mM acceptor; 15 min) maintains α2-3-sialyltransferase activity across pH 4.5-10.0 with an optimal pH of 6.0, and shows slightly narrower optimal pH range (5.0-8.0) when using LacβPro-triazole-C14 as the acceptor^[1].
MBP-PmST2-His6 (2 mM LacβPro-triazole-C14; 15 min) α2-3-sialyltransferase activity is not significantly affected by divalent metal ions (MnCl₂, MgCl₂), the chelating reagent EDTA, or the reducing reagent 2-mercaptoethanol at concentrations up to 20 mM, 20 mM, 10 mM, and 10 mM, respectively^[1].
MBP-PmST2-His6 (14 μM; 10 min) has 7-fold stronger binding to LacβPro-triazole-C14 (K_M = 4.1 mM) than to LacβPro2AA (K_M = 28 mM), 1.5-fold higher turnover number with LacβPro-triazole-C14 (k_cat = 12 min^-1) than with LacβPro2AA (k_cat = 7.9 min^-1), and 10-fold higher catalytic efficiency (k_cat/K_M) with LacβPro-triazole-C14 than with LacβPro2AA^[1].
MBP-PmST2-His6 (2 mM acceptor; 10 min) exhibits the highest α2-3-sialyltransferase activity toward LacβPro-triazole-C14 (36.1% conversion) among tested acceptors, with lower activity toward β1-4-linked galactosides, β-galactosylmonosaccharide lipid, and minimal activity toward β1-3-linked galactosides^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.