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

Keyphrases

• 5-fluorouridine 11%
• 5′-monophosphate 100%
• Conformational Change 100%
• Decarboxylation 50%
• Enzyme Active Site 5%
• Enzyme Catalysis 5%
• Equilibrium Constant 100%
• Hydrogen Bonds (H-bonds) 5%
• Kcat 33%
• Kinetic Data 5%
• Kinetic Parameters 11%
• Mutant Enzyme 5%
• Orotidine 27%
• Orotidine 5′-monophosphate Decarboxylase 100%
• Phenolic Groups 5%
• Phenyl Group 5%
• Physiological Substrates 5%
• Product Release 11%
• Protein Cage 5%
• Protein Release 5%
• Rate Limiting 5%
• Rate-determining Step 11%
• Side Chain 5%
• Substrate Binding 11%
• Transition State 5%
• Tyrosyl 5%

Biochemistry, Genetics and Molecular Biology

• Carboxy-Lyases 100%
• Catalytic Efficiency 33%
• Conformational Change 100%
• Decarboxylation 100%
• Enzyme 100%
• Enzyme Active Site 11%
• Equilibrium Constant 100%
• Kinetic Parameter 22%
• Turnover Number 33%
• Wild Type 11%