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

Benzer Materyaller

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