Residues distal to the active site contribute to enhanced catalytic activity of variant and hybrid β-lactamases derived from CTX-M-14 and CTX-M-15

Keyphrases

• Active Site Conformation 16%
• Active Sites 100%
• Amino Acids 33%
• BlaCTX-M-55 33%
• C-terminus 16%
• Catalytic Activity 16%
• Cephalosporins 66%
• China 16%
• Clavulanic Acid 16%
• Core Architectures 16%
• CTX-M 100%
• CTX-M Enzyme 16%
• CTX-M-14 100%
• CTX-M-15 100%
• Enhanced Catalytic Activity 100%
• Enzymatic Mechanism 16%
• Extended-spectrum-lactamase 16%
• Helix 33%
• High Catalytic Activity 16%
• Higher Structures 16%
• Host Strains 16%
• Hydrolytic Activity 16%
• Hydrophobic Interaction 16%
• Inhibitory Effect 16%
• Kcat 16%
• Kinetic Analysis 16%
• Lactams 16%
• N-terminus 16%
• Structure Stability 16%
• Substrate Profile 16%
• Sulbactam 33%
• Temperature Variation 16%
• β-lactamase 100%
• β-lactamase Inhibitor 33%

Biochemistry, Genetics and Molecular Biology

• Active Site 100%
• Amino Acids 50%
• C-Terminus 25%
• Catalytic Efficiency 50%
• Conformation 25%
• Enzyme 75%
• Hydrolase 25%
• Kinetics 25%
• N-Terminus 25%
• Serine 25%
• Sulbactam 50%

Chemistry

• Amino Acid 50%
• Cephalosporin 100%
• Clavulanic Acid 25%
• Kcat/Km 25%
• Kinetic Method 25%
• Lactam 25%
• Serine 25%
• Sulbactam 50%