Specificity and Versatility of Substrate Binding Sites in Four Catalytic Domains of Human N-Terminal Acetyltransferases

Medicine & Life Sciences

• N-Terminal Acetyltransferases 100%
• Substrate Specificity 59%
• Catalytic Domain 48%
• Binding Sites 41%
• Tyrosine 37%
• Hydrogen Bonding 32%
• Acetylation 28%
• Eukaryota 27%
• Enzymes 22%
• X-Rays 20%
• Structural Models 15%
• Molecular Dynamics Simulation 14%
• Alanine 13%
• Computer Simulation 12%
• Proteolysis 12%
• Ligands 9%
• Amino Acids 9%
• Peptides 8%
• Proteins 4%

Agriculture & Biology

• acetyltransferases 65%
• active sites 50%
• binding sites 45%
• tyrosine 36%
• acetylation 29%
• substrate specificity 26%
• hydrogen 24%
• X-radiation 23%
• eukaryotic cells 23%
• molecular dynamics 17%
• enzyme substrates 15%
• protein subunits 13%
• alanine 12%
• ligands 12%
• enzymes 12%
• peptides 9%
• proteins 9%
• degradation 8%
• mutants 7%
• amino acids 7%

Chemical Compounds

• Tyrosine 49%
• Binding Site 37%
• Simulation 33%
• Hydrogen Bond 21%
• X-Ray 21%
• Alanine 17%
• Protein 14%
• Molecular Dynamics 13%
• Modification 9%
• Time 6%
• Acid 6%