Structural and mechanistic investigation of 3-deoxy-D-manno-octulosonate-8-phosphate synthase by solid-state REDOR NMR

Results demonstrate that the enzyme binds phosphoenolpyruvate and arabinose-5-phosphate via arginine and lysine residues by different mechanisms. Data reveal that the active site residues for phosphoenolpyruvate are structurally rigid residues lysine-138 and arginine-168 wheras arginine 63, which binds to arabinose-5-phosphate is flexible.