Effect of Ca2+ on the activity and structure of α-glucosidase: Inhibition kinetics and molecular dynamics simulations

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dc.contributor.authorX Zhang-
dc.contributor.authorL Shi-
dc.contributor.authorX Li-
dc.contributor.authorQ Sheng-
dc.contributor.authorL Yao-
dc.contributor.authorD Shen-
dc.contributor.authorZ R Lu-
dc.contributor.authorH M Zhou-
dc.contributor.authorY D Park-
dc.contributor.authorJinhyuk Lee-
dc.contributor.authorQ Zhang-
dc.date.accessioned2017-04-19T09:53:09Z-
dc.date.available2017-04-19T09:53:09Z-
dc.date.issued2014-
dc.identifier.issn1389-1723-
dc.identifier.uri10.1016/j.jbiosc.2013.12.003ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11987-
dc.description.abstractUnderstanding the mechanism of inhibition of α-glucosidase (EC 3.2.1.20) is clinically important because of the involvement of this enzyme in type 2 diabetes mellitus. In this study, we conducted inhibition kinetics of α-glucosidase with Ca2+ and 10-ns molecular dynamics simulations. We found that direct binding of Ca2+ to the enzyme induced structural changes and inhibited enzyme activity. Ca2+ inhibited α-glucosidase in a mixed-type reaction (Ki=27.0±2.0mM) and directly induced the unfolding of α-glucosidase, which resulted in the exposure of hydrophobic residues. The simulations suggest that thirteen Ca2+ ions may interact with α-glucosidase residues and that the Ca2+ binding sites are associated with the structural changes in α-glucosidase. Our study provides insight into the mechanism of the Ca2+-induced structural changes in α-glucosidase and the inhibition of ligand binding. These results suggest that Ca2+ could act as a potent inhibitor of α-glucosidase for the treatment of type 2 diabetes mellitus.-
dc.publisherSoc Bioscience Bioengineering Japan-
dc.titleEffect of Ca2+ on the activity and structure of α-glucosidase: Inhibition kinetics and molecular dynamics simulations-
dc.title.alternativeEffect of Ca2+ on the activity and structure of α-glucosidase: Inhibition kinetics and molecular dynamics simulations-
dc.typeArticle-
dc.citation.titleJournal of Bioscience and Bioengineering-
dc.citation.number6-
dc.citation.endPage705-
dc.citation.startPage696-
dc.citation.volume117-
dc.contributor.affiliatedAuthorJinhyuk Lee-
dc.contributor.alternativeNameZhang-
dc.contributor.alternativeNameShi-
dc.contributor.alternativeNameLi-
dc.contributor.alternativeNameSheng-
dc.contributor.alternativeNameYao-
dc.contributor.alternativeNameShen-
dc.contributor.alternativeNameLu-
dc.contributor.alternativeNameZhou-
dc.contributor.alternativeName박용두-
dc.contributor.alternativeName이진혁-
dc.contributor.alternativeNameZhang-
dc.identifier.bibliographicCitationJournal of Bioscience and Bioengineering, vol. 117, no. 6, pp. 696-705-
dc.identifier.doi10.1016/j.jbiosc.2013.12.003-
dc.subject.keywordANS-
dc.subject.keywordInhibition kinetics-
dc.subject.keywordMolecular dynamics-
dc.subject.keywordPNP-
dc.subject.keywordPNPG-
dc.subject.keywordSimulation-
dc.subject.keywordα-Glucosidase-
dc.subject.localANS-
dc.subject.localInhibition kinetics-
dc.subject.localinhibition kinetics-
dc.subject.localMolecular dynamics-
dc.subject.localmolecular dynamics-
dc.subject.localPNP-
dc.subject.localPNPG-
dc.subject.localSimulations-
dc.subject.localSimulation-
dc.subject.localsimulation-
dc.subject.localα-glucosidase-
dc.subject.localα-Glucosidase-
dc.subject.localAlpha-glucosidase-
dc.subject.localalpha-glucosidases-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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