Related Experiment Video
Updated: Jan 25, 2026

Characterization of Metabolic Status in Nonhuman Primates with the Intravenous Glucose Tolerance Test
Published on: November 13, 2016
Structural characterization of a glucose-activated β-glucosidase from Bacillus thermoamylovorans
Wendi Yang1, Panpan Dong2, Guosi Li3
1Fujian Metrology Institute, Fuzhou, 350003, China.
Abstract:
β-glucosidases play crucial roles in lignocellulosic biomass conversion, but their applications were limited by thermostability and glucose sensitivity. In this study, the high-resolution crystal structure of a thermostable glucose-activated β-glucosidase Bgl52 from Bacillus thermoamylovorans was determined at 2.00 Å. Bgl52 belongs to the GH1 family, and exhibited a canonical (β/α)8 TIM barrel architecture typical to GH1 enzymes. Comparison analysis and site-directed mutagenesis revealed that its catalytic sites were Glu166 and Glu353 and its gatekeeper residues were Trp169 and Leu173, which involved in the glucose tolerance. Features contributing to its thermostability were also explored, including the composition of amino acids, number of mobile loops, total area of major hydrophobic clusters and number of salt bridges. Our study shed light on the molecular basis for glucose tolerance and thermostability of GH1 β-glucosidases and provide possibility of improving the characteristics for potential industrial applications by structure-guided engineering.
Related Concept Videos
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Oral Hypoglycemic Agents: α-Glucosidase Inhibitors
Acarbose and miglitol are...
Glucose Homeostasis: Regulation of Blood Glucose
During fasting, when blood glucose levels are low, the pancreas secretes glucagon. it...
Structure-Activity Relationships and Drug Design
SAR studies the intricate relationship between a drug's chemical structure and biological activity. It focuses on understanding how modifications to a drug's structure can influence...
Glucose Transporters
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes:
Cholinergic Antagonists: Chemistry and Structure-Activity Relationship

