Alpha-Glucosidase Folding During Urea Denaturation: Enzyme Kinetics and Computational Prediction |
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| Authors: | Xue-Qiang Wu Jun Wang Zhi-Rong Lü Hong-Min Tang Daeui Park Sang-Ho Oh Jong Bhak Long Shi Yong-Doo Park Fei Zou |
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| Institution: | (1) Department of Environmental Health, School of Public Health and Tropical Medicine, Southern Medical University, Baiyun District, North of Guangzhou Road No.1838, Guangzhou, 510515, People’s Republic of China;(2) School of Medicine, Shenzhen University, Shenzhen, 518060, People’s Republic of China;(3) Yangtze Delta Region Institute of Tsinghua University, Jiaxing, 314050, People’s Republic of China;(4) Korean BioInformation Center (KOBIC), KRIBB, Daejeon, 305-806, South Korea |
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| 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. |
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