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Insights into Glucose-6-phosphate Allosteric Activation of β‑Glucosidase A

A. Gomes, Anderson ; da Silva, Gustavo F ; Lakkaraju, Sirish K ; Guimarães, Beatriz Gomes ; Magalhães, Maria de Lourdes B

Journal of chemical information and modeling, 2021-04, Vol.61 (4), p.1931-1941 [Periódico revisado por pares]

United States: American Chemical Society

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  • Título:
    Insights into Glucose-6-phosphate Allosteric Activation of β‑Glucosidase A
  • Autor: A. Gomes, Anderson ; da Silva, Gustavo F ; Lakkaraju, Sirish K ; Guimarães, Beatriz Gomes ; Magalhães, Maria de Lourdes B
  • Assuntos: Agricultural wastes ; Allosteric Regulation ; beta-Glucosidase - metabolism ; Binding Sites ; Catalytic activity ; Cellobiase ; Cellulose ; Computational Biochemistry ; Ethanol ; Glucose ; Glucose-6-Phosphate ; Glucosidase ; Hydrolysis ; Sugar
  • É parte de: Journal of chemical information and modeling, 2021-04, Vol.61 (4), p.1931-1941
  • Descrição: Second-generation ethanol production involves the use of agricultural and forestry waste as feedstock, being an alternative to the first-generation technology as it relies on low-cost abundant residues and does not affect food agriculture. However, the success of second-generation biorefineries relies on energetically efficient processes and effective enzyme cocktails to convert cellulose into fermentable sugars. β-glucosidases catalyze the last step on the enzymatic hydrolysis of cellulose; however, they are often inhibited by glucose. Previous studies demonstrated that glucose-6-phosphate (G6P) is a positive allosteric modulator of Bacillus polymyxa β-glucosidase A, improving enzymatic efficiency, providing thermoresistance, and imparting glucose tolerance. However, the precise molecular details of G6P-β-glucosidase A interactions have not yet been described so far. We investigated the molecular details of G6P binding into B. polymyxa β-glucosidase A through in silico docking using the site identification by ligand competitive saturation technology followed by site-directed mutagenesis studies, from which an allosteric binding site for G6P was identified. In addition, a mechanistic shift toward the transglycosylation reaction as opposed to hydrolysis was observed in the presence of G6P, suggesting a new role of G6P allosteric modulation of the catalytic activity of β-glucosidase A.
  • Editor: United States: American Chemical Society
  • Idioma: Inglês
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