An Examination of the Relationship between Active Site Loop Size and Thermodynamic Activation Parameters for Orotidine 5′-Monophosphate Decarboxylase from Mesophilic and Thermophilic Organisms

Samankaltaisia teoksia

• Mechanism of the Orotidine 5’-Monophosphate Decarboxylase-Catalyzed Reaction: Effect of Solvent Viscosity on Kinetic Constants
  Tekijä: Wood, B. McKay, et al.
  Julkaistu: (2009)
• Product Deuterium Isotope Effect for Orotidine 5'-Monophosphate Decarboxylase: Evidence for the Existence of a Short-Lived Carbanion Intermediate
  Tekijä: Toth, Krisztina, et al.
  Julkaistu: (2007)
• Conformational Changes in Orotidine 5′-Monophosphate Decarboxylase: “Remote” Residues that Stabilize the Active Conformation()
  Tekijä: Wood, B. McKay, et al.
  Julkaistu: (2010)
• Enzyme Architecture: Deconstruction of the Enzyme-Activating Phosphodianion Interactions of Orotidine 5′-Monophosphate Decarboxylase
  Tekijä: Goldman, Lawrence M., et al.
  Julkaistu: (2014)
• Product Deuterium Isotope Effects for Orotidine 5'-Monophosphate Decarboxylase: Effect of Changing Substrate and Enzyme Structure on the Partitioning of the Vinyl Carbanion Reaction Intermediate
  Tekijä: Toth, Krisztina, et al.
  Julkaistu: (2010)