Orotidine 5′-Monophosphate Decarboxylase: Transition State Stabilization from Remote Protein-Phosphodianion Interactions

Eitemau Tebyg

• Enzyme Architecture: Deconstruction of the Enzyme-Activating Phosphodianion Interactions of Orotidine 5′-Monophosphate Decarboxylase
  gan: Goldman, Lawrence M., et al.
  Cyhoeddwyd: (2014)
• Conformational Changes in Orotidine 5′-Monophosphate Decarboxylase: “Remote” Residues that Stabilize the Active Conformation()
  gan: Wood, B. McKay, et al.
  Cyhoeddwyd: (2010)
• Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5′-Monophosphate Decarboxylase
  gan: Goryanova, Bogdana, et al.
  Cyhoeddwyd: (2015)
• Role of a Guanidinium Cation-Phosphodianion Pair in Stabilizing the Vinyl Carbanion Intermediate of Orotidine 5'-Phosphate Decarboxylase-Catalyzed Reactions.()
  gan: Goryanova, Bogdana, et al.
  Cyhoeddwyd: (2013)
• Dissecting the Total Transition State Stabilization Provided by Amino Acid Side-Chains at Orotidine 5′-Monophosphate Decarboxylase: A Two-Part Substrate Approach
  gan: Barnett, Shonoi A., et al.
  Cyhoeddwyd: (2008)