Towards alpha-glucosidase folding induced by trifluoroethanol: Kinetics and computational prediction

Cited 13 time in scopus
Metadata Downloads
Title
Towards alpha-glucosidase folding induced by trifluoroethanol: Kinetics and computational prediction
Author(s)
Y F Zen; Z R Lu; L Yan; Sangho Oh; J M Yang; Jinhyuk Lee; Z M Ye
Bibliographic Citation
Process Biochemistry, vol. 47, no. 12, pp. 2284-2290
Publication Year
2012
Abstract
Alpha-glucosidase (EC 3.2.1.20) is an enzyme, which is related with diabetes mellitus type 2 clinically, and is also generally used to convert starch to fermentable sugars in the industry. Therefore, study on this enzyme structures and functions is important. In this study, we investigated structural changes in the alpha-glucosidase during trifluoroethanol (TFE)-induced unfolding. The activity of alpha-glucosidase was significantly inactivated by TFE in a dose-dependent manner. The inactivation was composed of two-phases. TFE inhibited alpha-glucosidase in a parabolic mixed-type reaction (Ki = 0.72 ± 0.08 M). TFE directly induced the unfolding and hydrophobic exposure of alpha-glucosidase. We also simulated the docking between alpha-glucosidase and TFE, as well as molecular dynamics. The computational simulations suggested that several residues, such as ASP68, TYR71, VAL108, HIS111, PHE177, ASP214, THR215, GLU276, HIS348, ASP349, and ARG439, interact with TFE. The molecular dynamics simulation confirmed the binding mechanisms, between the alpha-glucosidase and TFE, and suggested that TFE inhibits the glucose binding site. Our study provides insights into the alpha-glucosidase folding behaviors, and cosolvent binding under a 3D structural simulation.
Keyword
Alpha-glucosidaseDocking simulationMolecular dynamicsTrifluoroethanolUnfolding
ISSN
0032-9592
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.procbio.2012.09.005
Type
Article
Appears in Collections:
Division of Biomedical Research > Genome Editing Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.