Structural analysis and inhibitory kinetics of brain type creatine kinase by sodium dodecyl sulfate

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dc.contributor.authorZ R Lu-
dc.contributor.authorSang Ho Oh-
dc.contributor.authorS S Zhou-
dc.contributor.authorH C Zou-
dc.contributor.authorD Park-
dc.contributor.authorSeongjin Park-
dc.contributor.authorH W Zhou-
dc.contributor.authorJ Bhak-
dc.contributor.authorY D Park-
dc.contributor.authorF Zou-
dc.date.accessioned2017-04-19T09:20:50Z-
dc.date.available2017-04-19T09:20:50Z-
dc.date.issued2010-
dc.identifier.issn0273-2289-
dc.identifier.uri10.1007/s12010-008-8470-2ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9873-
dc.description.abstractThe studies regarding the effect of sodium dodecyl sulfate (SDS) on enzyme activities and structures can provide a valuable insight into public health. We have predicted the 3D structure of the brain creatine kinase (CK-BB) with a high resolution and simulated the docking between CK-BB and SDS. The predicted structure had a root mean square deviation of 0.51 A. The docking between CK-BB and SDS was successful with significant scores (-4.67 kcal/mol, AutoDock4 and -48.32 kcal/mol, DOCK6). We have also investigated the inactivation by using SDS to study CK-BB's folding behaviors. The two-phase rate constants as a first-order reaction were measured during inactivation. SDS strongly inhibited the CK-BB activity in a noncompetitive inhibition manner (K i=1.22 mM). The tertiary structural change was induced by SDS binding with the exposure of hydrophobic surface. The methyl-β-cyclodextrin was used to strip SDS from the enzyme molecule to reactivate. The changes of thermodynamic parameters for the SDS ligand binding such as enthalpy, Gibbs free energy, and entropy were obtained as -13±7.0 MJ/mol, 8.39 kJ/mol, and -42.754 kJ/(K mol), respectively. Our study provides important structural information for CK-BB and its interaction with SDS with an insight on its folding and inhibition kinetics.-
dc.publisherSpringer-
dc.titleStructural analysis and inhibitory kinetics of brain type creatine kinase by sodium dodecyl sulfate-
dc.title.alternativeStructural analysis and inhibitory kinetics of brain type creatine kinase by sodium dodecyl sulfate-
dc.typeArticle-
dc.citation.titleApplied Biochemistry and Biotechnology-
dc.citation.number3-
dc.citation.endPage842-
dc.citation.startPage831-
dc.citation.volume160-
dc.contributor.affiliatedAuthorSang Ho Oh-
dc.contributor.affiliatedAuthorSeongjin Park-
dc.contributor.alternativeNameLu-
dc.contributor.alternativeName오상호-
dc.contributor.alternativeNameZhou-
dc.contributor.alternativeNameZou-
dc.contributor.alternativeName박대의-
dc.contributor.alternativeName박성진-
dc.contributor.alternativeNameZhou-
dc.contributor.alternativeName박종화-
dc.contributor.alternativeName박용두-
dc.contributor.alternativeNameZou-
dc.identifier.bibliographicCitationApplied Biochemistry and Biotechnology, vol. 160, no. 3, pp. 831-842-
dc.identifier.doi10.1007/s12010-008-8470-2-
dc.subject.keywordBrain creatine kinase-
dc.subject.keywordFolding-
dc.subject.keywordSodium dodecyl sulfate-
dc.subject.keywordStructure prediction-
dc.subject.keywordThermodynamics-
dc.subject.localbrain creatine kinase-
dc.subject.localBrain creatine kinase-
dc.subject.localFolding-
dc.subject.localSodium dodecyl sulfate-
dc.subject.localstructure prediction-
dc.subject.localStructure prediction-
dc.subject.localThermodynamics-
dc.subject.localthermodynamics-
dc.description.journalClassY-
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