SGD Paper 
Wu XQ, et al. (2010) Alpha-glucosidase folding during urea denaturation: enzyme kinetics and computational prediction. Appl Biochem Biotechnol 160(5):1341-55
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.
| Status: Published | Type: Journal Article | Research Support, Non-U.S. Gov't | PubMed ID: 19418260 |
Topics addressed in this paper
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.
| Topics | Topics not linked to Genes | Genes linked to topics |
|---|---|---|
| MAL12 | ||
| Computational analysis |  | |
| Mutants/Phenotypes | | |
| Omics | 
| |
| Primary Literature | | |
| Protein Physical Properties | | |
| Protein/Nucleic Acid Structure | |
