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Updated: Jul 4, 2025
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Spectrophotometric Methods for the Study of Eukaryotic Glycogen Metabolism
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Structural analysis of Tris binding in β-glucosidases.
1College of General Education, Kookmin University, Seoul, 20707, Republic of Korea.
Biochemical and Biophysical Research Communications
|February 2, 2024
Summary
Tris inhibits β-glucosidases (Bgls) by binding to the glycone site. Structural analysis reveals Tris mimics glucose binding, with variations in binding affecting enzyme inhibition.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- β-glucosidases (Bgls) are crucial industrial enzymes.
- Tris is known to inhibit some Bgls, but its binding and selectivity are not fully understood.
Purpose of the Study:
- To elucidate the binding mechanism and structural basis of Tris inhibition in Thermoanaerobacterium saccharolyticum Bgl (TsaBgl).
Main Methods:
- X-ray crystallography to determine three crystal structures of TsaBgl complexed with Tris at high resolution (1.55-1.95 Å).
Main Results:
- Tris consistently binds to the glycone site of TsaBgl, mimicking glucose binding through its hydroxyl groups.
- Amino acid interactions with Tris are conserved across Bgl enzymes.
- Comparison with other Bgl structures reveals variations in Tris and water molecule arrangements, particularly at the aglycone site.
Conclusions:
- The binding configuration and affinity of Tris for Bgls are influenced by residues in the aglycone and gatekeeper regions.
- This study enhances understanding of Tris inhibition mechanisms in TsaBgl.
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