| Abstract: | 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(Mg~(2+) or Ca~(2+)), 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. |
