Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase

Keyphrases

• Kinetic Analysis 100%
• Active Sites 100%
• Substrate Binding 100%
• Kcat 100%
• Protonation 100%
• Benzoylformate 100%
• Mandelate 100%
• Benzoylformate Decarboxylase 100%
• Thiamine Diphosphate 100%
• ThDP 100%
• Thiamine Diphosphate-dependent Enzymes 100%
• Order of Magnitude 50%
• Side Chain 50%
• Hydroxyl Group 50%
• Kinetic Study 50%
• Steady-state Kinetics 50%
• Competitive Inhibitor 50%
• Imidazole 50%
• Stopped Flow 50%
• Product Release 50%
• Hydroxyl 50%
• Magnitude Effect 50%
• Deprotonation 50%
• Carboxylate Group 50%
• Decarboxylation 50%
• Alternative Substrates 50%
• Enzyme Binding 50%
• Active Site mutant 50%
• Kinetic Resolution 50%
• Enamines 50%
• Catalytic Parameters 50%
• Carbonyl Group 50%
• Hydrogen Bond (H-bond) 50%
• Flow Experiments 50%

Chemistry

• Catalysis 100%
• Kinetic Method 100%
• Thiamine 100%
• Kcat 66%
• Km 66%
• (R)-Mandelate 66%
• protonation 66%
• Nitrogen 33%
• Chemical Kinetics Characteristics 33%
• Hydrogen Bonding 33%
• Hydroxyl Group 33%
• Kinetic Study 33%
• Deprotonation 33%
• Hydroxyl 33%
• Inhibition Constant (Ki) 33%
• Decarboxylation 33%
• Carbonyl Group 33%
• Imidazole 33%
• Enamine 33%
• Cofactor 33%
• Carboxylic Acid 33%
• Serine 33%
• Stopped-Flow 33%

Biochemistry, Genetics and Molecular Biology

• Active Site 100%
• Enzyme 100%
• Carboxy-Lyases 100%
• Thiamine Pyrophosphate 100%
• Turnover Number 66%
• Protonation 66%
• Wild Type 33%
• Hydrogen Bond 33%
• Steady State 33%
• Deprotonation 33%
• Decarboxylation 33%
• Enzyme Binding 33%
• Competitive Inhibition 33%
• Serine 33%