Impact on Catalysis of Secondary Structural Manipulation of the αC-Helix of Escherichia coli Dihydrofolate Reductase

Keyphrases

• Binary Complexes 33%
• C-terminus 33%
• Catalytic Processes 33%
• Conformational Change 33%
• Debinding 33%
• Dislocation 33%
• Enzyme-catalyzed Reaction 33%
• Escherichia Coli Dihydrofolate Reductase 100%
• Fold Increase 66%
• Hairpin Structure 33%
• Hairpin Turn 33%
• Helix 66%
• Hydride Transfer 33%
• Kcat 33%
• Kinetic Parameters 33%
• Koff 33%
• Lactobacillus Casei 66%
• Mutagenesis 33%
• Mutant Enzyme 66%
• Mutant Protein 33%
• Nicotinamide Adenine Dinucleotide Phosphate (NADPH) 100%
• Product Release 33%
• Reaction Rate 33%
• Secondary Structural Elements 100%
• State Reaction 33%
• Steady State 33%
• Substrate-induced 33%
• Synergism 33%
• Ternary Complex 33%
• Tetrahydrofolate 100%
• Triple mutation 33%

Biochemistry, Genetics and Molecular Biology

• C-Terminus 25%
• Conformational Change 25%
• Dihydrofolate Reductase 100%
• Dissociation Rate Constant 25%
• Enzyme 100%
• Enzyme Mechanism 25%
• Escherichia coli 100%
• Kinetic Parameter 25%
• Lactobacillus casei 25%
• Mutagenesis 25%
• Mutant Protein 25%
• Steady State 25%
• Ternary Complex 25%
• Tetrahydrofolic Acid 75%
• Turnover Number 25%
• Wild Type 100%

Chemistry

• Catalysis 20%
• Dihydrofolates 100%
• Enzymatic Reaction 20%
• Kcat 20%
• NADPH 60%
• Pharmacokinetics 20%
• Tetrahydrofolate 60%
• Tetrahydrofolic Acid 60%