Alpha-glucosidase folding during urea denaturation: enzyme kinetics and computational prediction

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Title
Alpha-glucosidase folding during urea denaturation: enzyme kinetics and computational prediction
Author(s)
Z Q Wu; J Wang; Z R Lu; H M Tang; D Park; Sang Ho Oh; J Bhak; L Shi; Y D Park; F Zou
Bibliographic Citation
Applied Biochemistry and Biotechnology, vol. 160, no. 5, pp. 1341-1355
Publication Year
2010
Abstract
In this study, we investigated structural changes in alpha-glucosidase during urea denaturation. Alpha-glucosidase was inactivated by urea in a dose-dependent manner. The inactivation was a first-order reaction with a monophase process. Urea inhibited alpha-glucosidase in a mixed-type reaction. We found that an increase in the hydrophobic surface of this enzyme induced by urea resulted in aggregation caused by unstable folding intermediates. We also simulated the docking between alpha-glucosidase and urea. The docking simulation suggested that several residues, namely THR9, TRP14, LYS15, THR287, ALA289, ASP338, SER339, and TRP340, interact with urea. Our study provides insights into the alpha-glucosidase unfolding pathway and 3D structure of alpha-glucosidase.
Keyword
Docking simulationUrea unfoldingAlpha-glucosidase
ISSN
0273-2289
Publisher
Springer
DOI
http://dx.doi.org/10.1007/s12010-009-8636-6
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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