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Literature summary for 3.2.1.20 extracted from

  • Zeng, Y.; Lü, Z.; Yan, L.; Oh, S.; Yang, J.; Lee, J.; Ye, Z.
    Towards alpha-glucosidase folding induced by trifluoroethanol: Kinetics and computational prediction (2012), Process Biochem., 47, 2284-2290.
No PubMed abstract available
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Inhibitors

Inhibitors Comment Organism Structure
trifluoroethanol the activity of alpha-glucosidase is significantly inactivated by trifluoroethanol in a dose-dependent manner. The inactivation is composed of two-phases. Inhibition follows a parabolic mixed-type reaction. Trifluoroehanol directly induces the unfolding and hydrophobic exposure of alpha-glucosidase. Computational simulations suggest that several residues, such as Asp68, Tyr71, Val108, His111, Phe177, Asp214, Thr215, Glu276, His348, Asp349, and Arg439, interact with trifluoroethanol. The molecular dynamics simulation confirmed the binding mechanisms,and suggest that trifluoroethanol inhibits the glucose binding site Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.72
-
 trifluoroethanol pH not specified in the publication, temperature not specified in the publication Saccharomyces cerevisiae