Structural origins for the loss of catalytic activities of bifunctional human LTA4H revealed through molecular dynamics simulations

Medicine & Life Sciences

• Aminopeptidases 35%
• Anti-Inflammatory Agents 19%
• Arachidonic Acid 26%
• Catalysis 31%
• Catalytic Domain 23%
• Enzymes 43%
• Epoxy Compounds 35%
• Human Activities 79%
• Hydrogen Bonding 31%
• Hydrolases 31%
• Ions 21%
• Leukotriene A4 88%
• leukotriene A4 hydrolase 89%
• Leukotriene B4 32%
• Ligands 18%
• Lipids 17%
• Metals 22%
• Molecular Dynamics Simulation 87%
• Mutation 44%
• Peptides 16%
• Proteins 9%

Agriculture & Biology

• active sites 24%
• aminopeptidases 32%
• anti-inflammatory agents 34%
• arachidonic acid 26%
• catalytic activity 75%
• crystal structure 27%
• enzymes 35%
• epoxides 24%
• hydrogen 23%
• hydrolases 77%
• leukotrienes 65%
• ligands 23%
• lipids 14%
• metal ions 27%
• molecular dynamics 100%
• mutation 54%
• peptides 17%
• proteins 8%
• tripeptides 65%

Chemical Compounds

• Anti-Inflammatory Agent 33%
• Arachidonic Acid 29%
• Catalysis 16%
• Crystal Structure 13%
• Epoxide 23%
• Hydrogen Bond 15%
• Hydrolase Inhibitor 41%
• Leukotriene A4 83%
• Lipid 18%
• Metal Ion 16%
• Molecular Dynamics 57%
• Mutation 66%
• Peptide 15%
• Simulation 49%
• Tripeptide 57%