Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5′-Monophosphate Decarboxylase

Eitemau Tebyg

• Enzyme Architecture: Deconstruction of the Enzyme-Activating Phosphodianion Interactions of Orotidine 5′-Monophosphate Decarboxylase
  gan: Goldman, Lawrence M., et al.
  Cyhoeddwyd: (2014)
• Orotidine 5′-Monophosphate Decarboxylase: Probing the Limits of the Possible for Enzyme Catalysis
  gan: Richard, John P., et al.
  Cyhoeddwyd: (2018)
• Catalysis by Orotidine 5′-Monophosphate Decarboxylase: Effect of 5-Fluoro and 4′-Substituents on the Decarboxylation of Two-Part Substrates()
  gan: Goryanova, Bogdana, et al.
  Cyhoeddwyd: (2013)
• Enzyme Architecture: Breaking Down the Catalytic Cage that Activates Orotidine 5′-Monophosphate Decarboxylase for Catalysis
  gan: Reyes, Archie C., et al.
  Cyhoeddwyd: (2018)
• Conformational Changes in Orotidine 5’-Monophosphate Decarboxylase: A Structure-Based Explanation for How the 5’-Phosphate Group Activates the Enzyme
  gan: Desai, Bijoy J., et al.
  Cyhoeddwyd: (2012)