Slow ligand-induced conformational switch increases the catalytic rate in Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase

Keyphrases

• Hypoxanthine-guanine Phosphoribosyltransferase 100%
• Plasmodium Falciparum 100%
• Conformational Switch 100%
• Catalytic Rate 100%
• PfHGXPRT 100%
• Activation Mechanism 66%
• Conformational Change 66%
• Cis Conformation 66%
• Dipeptide 66%
• Lag Phase 66%
• Isomerization 33%
• Binding Site 33%
• Low Activity 33%
• High Activity 33%
• Computational Study 33%
• Xanthine 33%
• Toxoplasma Gondii (T. gondii) 33%
• Oligomerization 33%
• Unique Mechanism 33%
• Free Energy Calculations 33%
• Pre-incubation 33%
• Km Value 33%
• Ligand-mediated 33%
• Trans Conformation 33%
• Activated State 33%
• Free Enzyme 33%
• Ligand-free 33%
• Well-tempered Metadynamics 33%
• HG(X)PRT 33%
• Rotational Energy Barrier 33%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Conformation 100%
• Phosphoribosyltransferase 100%
• Plasmodium falciparum 100%
• Guanine 100%
• Conformational Change 66%
• Dipeptide 66%
• Isomerization 33%
• Binding Site 33%
• Oligomerization 33%
• Metadynamic 33%