Saturation-transfer-difference NMR to characterize substrate binding recognition and catalysis of two broadly specific glycoside hydrolases

Keyphrases

• Substrate Binding 100%
• Leaving Group 100%
• Glycoside Hydrolase 100%
• Saturation Transfer Difference NMR 100%
• Low Temperature 50%
• Alcohol 50%
• Lactose 50%
• Non-covalent 50%
• Aspergillus Fumigatus 50%
• Active Sites 50%
• Distinct Patterns 50%
• Glycosidase 50%
• Glucopyranosyl 50%
• Glucoside 50%
• Sugar Binding 50%
• Substrate Effect 50%
• Glucopyranose 50%
• Galactosylated 50%
• Cellobiose 50%
• Binding Effect 50%
• Pyrococcus Furiosus 50%
• Multiple Contacts 50%
• Cellobiose Hydrolysis 50%
• Enzyme-substrate Interaction 50%

Biochemistry, Genetics and Molecular Biology

• Glycoside Hydrolases 100%
• Saturation Transfer 100%
• Enzyme 100%
• Cellobiose 100%
• Active Site 50%
• Nuclear Magnetic Resonance Spectroscopy 50%
• Enzymatic Hydrolysis 50%
• Enzyme Substrate Complex 50%
• Pyrococcus furiosus 50%
• Aspergillus fumigatus 50%
• Lactose 50%
• Glucoside 50%