Structural investigation of inhibitor designs targeting 3-dehydroquinate dehydratase from the shikimate pathway of Mycobacterium tuberculosis

Keyphrases

• Inhibitor Design 100%
• Mycobacterium Tuberculosis (M. tb) 100%
• Structural Investigation 100%
• Dehydroquinate Dehydratase 100%
• Shikimate Pathway 100%
• Reaction Products 66%
• Active Sites 33%
• Ligand Binding 33%
• Putative Drug Targets 33%
• Structural Insights 33%
• Catalytic Mechanism 33%
• High-resolution Crystal Structure 33%
• Binding Mode 33%
• π-stacking 33%
• Stacking Interactions 33%
• Inhibitor-2 33%
• Competitive Inhibitor 33%
• Enols 33%
• Structural Rearrangement 33%
• Reaction Intermediates 33%
• Enolates 33%
• Citrazinic Acid 33%
• 3-Dehydroshikimate 33%
• Biaryls 33%
• Flexible Extension 33%
• Human-made 33%
• Inhibitor Binding 33%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Mycobacterium Tuberculosis 100%
• Dehydratase 100%
• Crystal Structure 33%
• Active Site 33%
• Ligand Binding 33%
• Catalytic Mechanism 33%
• Competitive Inhibition 33%
• Enol 33%

Chemistry

• Shikimate 100%
• 3-Dehydroquinate 100%
• Crystal Structure 33%
• Drug Target 33%
• Enolates 33%
• Reaction Intermediate 33%
• Biaryl 33%
• Enol 33%
• 3-Dehydroshikimate 33%