Magnitude and Origin of the Enhanced Basicity of the Catalytic Glutamate of Triosephosphate Isomerase

Lignende værker

• Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase
  af: Zhai, Xiang, et al.
  Udgivet: (2018)
• Mechanism for Activation of Triosephosphate Isomerase by Phosphite Dianion: The Role of a Ligand-Driven Conformational Change
  af: Malabanan, M. Merced, et al.
  Udgivet: (2011)
• Structure–Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase
  af: Richard, John P., et al.
  Udgivet: (2016)
• Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion
  af: Zhai, Xiang, et al.
  Udgivet: (2013)
• Mechanism for Activation of Triosephosphate Isomerase by Phosphite Dianion: The Role of a Hydrophobic Clamp
  af: Malabanan, M. Merced, et al.
  Udgivet: (2012)