The Ring-Opening Mechanism of GlcN6P Catalyzed by SmuNagB: A QM/MM Molecular Dynamics Study

• 作 者: YuanZhao[1]NanhaoChen[2]RuiboWu[2]ZexingCao[1]
• 机 构: State Key Laboratory of Physical Chemistry of Solid Surfaces and Fujian Provincial Key Laboratory of
• 出 处: International Conference on Theoretical and High Performance
• 发表日期: 2013年期

　　The glucosamine 6-phosphate deaminase (NagB) can catalyze the conversion of D-glucosamine 6-phosphate (GlcN6P) into D-fructose 6-phosphate (F6P) and ammonia.The reaction is the final specific step which can decide the metabolic fate of GlcNAc.Herein, the ring-opening mechanism of GlcN6P catalyzed by NagB of Streptococcus mutans has been first studied by ab initio quantum mechanics and molecular mechanics (QM/MM) molecular dynamics simulation with umbrella sampling, and the different protonation catalytic pathways have been determined by free energy reaction profile.Moreover, the characters of lid motif have been also explored.