The enzyme Ots A（trehalose-P synthase） plays a critical role in the biosynthesis of trehalose, which is a nonreducing disaccharide that plays important functions in many organisms. By using light scattering techniqu...The enzyme Ots A（trehalose-P synthase） plays a critical role in the biosynthesis of trehalose, which is a nonreducing disaccharide that plays important functions in many organisms. By using light scattering technique, we discovered that Ots A in Arthrobacter strain A3 polymerized in the presence of divalent metal ions（Mg2＋ or Ca2＋）, and the kinetics of the assembly was dependent on their concentrations. We identified potential compounds that can affect the kinetics of the polymerization, particularly, heparin, which acts as a very promising inhibitor of the polymerization. The Ots A assembly turns out to be a very delicate process that is finely regulated by p H. Ots A may be in the polymerized form at physiological pH in vivo, suggesting a more complicated mechanism of the enzyme. These unique properties of Ots A provide novel insights into the molecular mechanism of the biosynthesis of trehalose.展开更多
基金Supported by the National Natural Science Foundation of China(21305056)the Open Fund of State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics(T151402)
文摘The enzyme Ots A（trehalose-P synthase） plays a critical role in the biosynthesis of trehalose, which is a nonreducing disaccharide that plays important functions in many organisms. By using light scattering technique, we discovered that Ots A in Arthrobacter strain A3 polymerized in the presence of divalent metal ions（Mg2＋ or Ca2＋）, and the kinetics of the assembly was dependent on their concentrations. We identified potential compounds that can affect the kinetics of the polymerization, particularly, heparin, which acts as a very promising inhibitor of the polymerization. The Ots A assembly turns out to be a very delicate process that is finely regulated by p H. Ots A may be in the polymerized form at physiological pH in vivo, suggesting a more complicated mechanism of the enzyme. These unique properties of Ots A provide novel insights into the molecular mechanism of the biosynthesis of trehalose.
