Crystal structure and identification of amino acid residues for catalysis and binding of GH3 AnBX β-xylosidase from Aspergillus niger

Keyphrases

• Aspergillus Niger 100%
• β-xylosidase 100%
• Xyloside 100%
• Amino Acid Residues 100%
• Hydrolysis 66%
• 3D Structure 33%
• Biochemical Data 33%
• Structural Information 33%
• NMR Spectroscopy 33%
• Substrate Binding 33%
• Binding Residues 33%
• Disulfide Bond 33%
• Site-directed mutagenesis 33%
• Azides 33%
• High Catalytic Activity 33%
• Acid-base Catalyst 33%
• Nucleophile 33%
• Catalytic Efficiency 33%
• Kinetic Analysis 33%
• Glucoside 33%
• Xylose 33%
• Asymmetric Unit 33%
• Lignocellulosic Biomass 33%
• Enzymatic Properties 33%
• Substrate Preference 33%
• Xylooligosaccharides 33%
• TIM Barrel 33%
• Fibronectin Type III Domain-containing Protein 5 (FNDC5) 33%
• Hemicellulose Degradation 33%

Biochemistry, Genetics and Molecular Biology

• Amino Acids 100%
• Crystal Structure 100%
• Aspergillus Niger 100%
• Xyloside 100%
• Enzymatic Hydrolysis 66%
• Catalytic Efficiency 66%
• N-Terminus 33%
• C-Terminus 33%
• Site-Directed Mutagenesis 33%
• Kinetics 33%
• Disulfide Bond 33%
• Xylooligosaccharide 33%
• TIM Barrel 33%
• Fibronectin Type III Domain 33%
• Hemicellulose 33%
• Xylose 33%
• Nuclear Magnetic Resonance Spectroscopy 33%
• Glucoside 33%