Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase

Keyphrases

• Active Sites 100%
• Enzyme Activity 100%
• Binding Activity 100%
• Substrate Binding 100%
• Salivary alpha-amylase 100%
• Substrate Enzyme 100%
• Mobile Loop 100%
• Maltotriose 66%
• Acarbose 66%
• Specific Activity 33%
• Transition State Analogue 33%
• Deletion mutant 33%
• Cleavage Site 33%
• Oligosaccharides 33%
• Transition State 33%
• Binding Mode 33%
• Crystallographic Data 33%
• Kinetic Study 33%
• Electron Density 33%
• Amylase 33%
• Protein-ligand Interaction 33%
• Kinetic Data 33%
• Water Molecule 33%
• Starch 33%
• Minimal Change 33%
• Reducing End 33%
• Conformational Differences 33%
• Hydrogen Bonding Interaction 33%
• Maltoheptaose 33%
• Kcat 33%
• Saccharide Binding 33%
• Transglycosylation 33%
• Glycine-rich Loop 33%
• Hydrolysis-condensation Reactions 33%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Active Site 100%
• Binding Affinity 100%
• Enzyme Activity 100%
• Koji 100%
• Crystal Structure 66%
• Oligosaccharide 66%
• Acarbose 66%
• Glycosylation 33%
• Hydrogen Bond 33%
• Transition State Analog 33%
• Wild Type 33%
• Enzymatic Hydrolysis 33%
• Deletion Mutant 33%
• Starch 33%
• Turnover Number 33%
• Protein-Ligand Interaction 33%