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Title 

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

Authors 

Z Q WuJ WangZ R LuH M TangD ParkSang Ho OhJ BhakL ShiY D ParkF Zou

Publisher 

Humana Press

Issue Date 

2010

Citation 

Applied Biochemistry and Biotechnology, vol. 160, no. 5, pp. 1341-1355

Keywords 

Alpha-glucosidaseDocking simulationUrea unfolding

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.

ISSN 

0273-2289

Link 

http://dx.doi.org/10.1007/s12010-009-8636-6

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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