Linked Life Data

19418260

Source:http://linkedlifedata.com/resource/pubmed/id/19418260

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2010-2-10
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1559-0291
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
160
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1341-55
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Alpha-glucosidase folding during urea denaturation: enzyme kinetics and computational prediction.
pubmed:affiliation
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.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't