Effect of Ba2+ on the activity and structure of α-glucosidase: inhibition kinetics and molecular dynamics simulation

Cited 19 time in scopus
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Title
Effect of Ba2+ on the activity and structure of α-glucosidase: inhibition kinetics and molecular dynamics simulation
Author(s)
X Li; Z R Lu; W Wang; X P Han; J M Yang; Y D Park; H M Zhou; Q Sheng; Jinhyuk Lee
Bibliographic Citation
Process Biochemistry, vol. 50, no. 4, pp. 582-588
Publication Year
2015
Abstract
It is important to study enzyme inhibition of α-glucosidase (EC 3.2.1.20) due to its physiological role as well as clinical relevance. In the present study, we examined the effect of Ba2+ on α-glucosidase (EC 3.2.1.20) by integrating enzyme kinetics and computational simulations. The results showed that Ba2+ directly bound to this enzyme and induced inhibition through structural changes. Ba2+ inhibited α-glucosidase in a mixed-type reaction (Ki = 55.50 ± 2.12 mM) and directly induced the regional unfolding of alpha-glucosidase, resulting in a slight hydrophobic exposure. The computational simulations via molecular dynamics showed that Ba2+ directly bound to the active site entrance on α-glucosidase resulting in structural changes in this enzyme. Thus, this study provides insights into the mechanism of Ba2+ ligand binding-induced inhibition and structural change in α-glucosidase to increase the current understanding of the toxicity of Ba2+ on the carbohydrate catabolic enzyme α-glucosidase.
Keyword
Ba2+Docking simulationInhibition kineticsMolecular dynamicsUnfoldingα-Glucosidase
ISSN
0032-9592
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.procbio.2015.01.014
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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