Crystal structure of β-glucosidase 1A from Thermotoga neapolitana and comparison of active site mutants for hydrolysis of flavonoid glucosides. [electronic resource]
- Proteins 05 2017
- 872-884 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
1097-0134
10.1002/prot.25256 doi
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