Crystal structure of β-glucosidase 1A from Thermotoga neapolitana and comparison of active site mutants for hydrolysis of flavonoid glucosides. [electronic resource]
Producer: 20170728Description: 872-884 p. digitalISSN:- 1097-0134
- Amino Acid Motifs
- Amino Acids -- chemistry
- Bacterial Proteins -- chemistry
- Binding Sites
- Biocatalysis
- Crystallography, X-Ray
- Isoflavones -- chemistry
- Kinetics
- Models, Molecular
- Molecular Docking Simulation
- Mutagenesis, Site-Directed
- Mutation
- Protein Binding
- Protein Conformation, alpha-Helical
- Protein Conformation, beta-Strand
- Protein Interaction Domains and Motifs
- Quercetin -- analogs & derivatives
- Structure-Activity Relationship
- Substrate Specificity
- Thermodynamics
- Thermotoga neapolitana -- chemistry
- beta-Glucosidase -- chemistry
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Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
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