Kinetic Mechanism of Adenine Nucleotide Binding to and Hydrolysis by the Escherichia coli Rep Monomer. 2. Application of a Kinetic Competition Approach

Medicine & Life Sciences

• Adenine Nucleotides 100%
• Hydrolysis 74%
• Adenosine Triphosphate 62%
• Kinetics 57%
• Escherichia coli 56%
• Adenylyl Imidodiphosphate 32%
• Nucleotides 30%
• Anions 22%
• Fluorescence 21%
• Adenosine Diphosphate 21%
• Adenosine Monophosphate 17%
• Magnesium Chloride 14%
• 2'-O-(N-methylanthraniloyl)ATP 12%
• 3'-O-(N-methylanthraniloyl) ATP 11%
• Cations 10%
• Adenosine 10%
• Phosphates 9%
• DNA Helicases 7%
• Competitive Binding 6%
• Escherichia coli Proteins 6%
• triphosphoric acid 6%
• DNA 5%
• Sulfates 5%
• Tryptophan 5%
• Glycerol 5%
• DNA Replication 5%
• Biochemistry 4%
• Salts 4%
• Binding Sites 4%
• Proteins 1%

Chemical Compounds

• Adenine 74%
• Nucleotide 65%
• Hydrolysis 49%
• Monomer 47%
• ADP 30%
• Application 25%
• Rate Constant 19%
• Anion 16%
• Fluorescence 16%
• Adenosine 13%
• Adenosine Phosphate 12%
• Triphosphate(5-) 8%
• Inorganic Phosphate 8%
• Cation 8%
• Homodimer 8%
• Degradation Rate 7%
• Tryptophan 6%
• Biochemistry 6%
• Fluorescence Intensity 6%
• Glycerol 6%
• Protein 6%
• Kd 5%
• Sulfate 5%
• Binding Site 5%
• Phosphate 4%
• Reduction 3%
• Mixture 3%
• pH Value 3%