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Wan Fang
CNKI
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Wuhan University
Latest Article
Mg2+-Triggered and pH-Tuned in vitro Assembly of Trehalose-6-Phosphate Synthase
Time:2018-9-18  
ZHANG Shanshan, YANG Fan, ZHANG Yuping, LIU Zaiman, YU Linghui, CHEN Ximing, XIAO Jianxi
1. College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou 730000, Gansu, China; 2. School of Chemical and Biological Engineering, Lanzhou Jiaotong University, Lanzhou 730070, Gansu, China; 3. School of Stomatology, Lanzhou University, Lanzhou 730000, Gansu, China; 4. Key Laboratory of Desert & Desertification, Cold & Arid Regions Environmental & Engineering Research Institute, Chinese Academy of Sciences, Lanzhou 730000, Gansu, China
Abstract:
The enzyme OtsA (trehalose-P synthase) plays a critical role in the biosynthesis of trehalose, which is a nonreducing disac-charide that plays important functions in many organisms. By using light scattering technique, we discovered that OtsA 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 OtsA assembly turns out to be a very delicate process that is finely regulated by pH. OtsA may be in the polymerized form at physiological pH in vivo, suggesting a more complicated mechanism of the enzyme. These unique properties of OtsA provide novel insights into the molecular mechanism of the biosynthesis of trehalose.
Key words:OtsA(trehalose-P synthase); trehalose; polymerization; light scattering
CLC number: O 657.93
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