Alpha-glucosidase folding during urea denaturation: enzyme kinetics and computational prediction.
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.
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.
Xue-Qiang
XQ
Wu
Jun
J
Wang
Zhi-Rong
ZR
Lü
Hong-Min
HM
Tang
Daeui
D
Park
Sang-Ho
SH
Oh
Jong
J
Bhak
Long
L
Shi
Yong-Doo
YD
Park
Fei
F
Zou
D000817:Anilino Naphthalenesulfonates / Q000378:metabolism; D019295:Computational Biology; D004789:Enzyme Activation / Q000187:drug effects; D007700:Kinetics; D056004:Molecular Dynamics Simulation; D011489:Protein Denaturation / Q000187:drug effects*; D017510:Protein Folding / Q000187:drug effects*; D020836:Protein Structure, Quaternary; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012996:Solutions; D013050:Spectrometry, Fluorescence; D013997:Time Factors; D014508:Urea / Q000494:pharmacology*; D000520:alpha-Glucosidases / Q000737:chemistry* / Q000378:metabolism*
D000817:Anilino Naphthalenesulfonates; D012996:Solutions; C027132:1-anilino-8-naphthalenesulfonate; D014508:Urea; D000520:alpha-Glucosidases