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.
journal_name
Appl Biochem Biotechnoljournal_title
Applied biochemistry and biotechnologyauthors
Wu XQ,Wang J,Lü ZR,Tang HM,Park D,Oh SH,Bhak J,Shi L,Park YD,Zou Fdoi
10.1007/s12010-009-8636-6subject
Has Abstractpub_date
2010-03-01 00:00:00pages
1341-55issue
5eissn
0273-2289issn
1559-0291journal_volume
160pub_type
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