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

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.

authors

Wu XQ,Wang J,Lü ZR,Tang HM,Park D,Oh SH,Bhak J,Shi L,Park YD,Zou F

doi

10.1007/s12010-009-8636-6

subject

Has Abstract

pub_date

2010-03-01 00:00:00

pages

1341-55

issue

5

eissn

0273-2289

issn

1559-0291

journal_volume

160

pub_type

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