Mixed-type inhibition of tyrosinase from agaricus bisporus by terephthalic acid: Computational simulations and kinetics

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dc.contributor.authorS J Yin-
dc.contributor.authorY X Si-
dc.contributor.authorY F Chen-
dc.contributor.authorG Y Qian-
dc.contributor.authorZ R Lu-
dc.contributor.authorS Oh-
dc.contributor.authorJin Hyuk Lee-
dc.contributor.authorSanghyuk Lee-
dc.contributor.authorJ M Yang-
dc.contributor.authorD Y Lee-
dc.contributor.authorY D Park-
dc.date.accessioned2017-04-19T09:23:56Z-
dc.date.available2017-04-19T09:23:56Z-
dc.date.issued2011-
dc.identifier.issn1572-3887-
dc.identifier.uri10.1007/s10930-011-9329-xko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10190-
dc.description.abstractTyrosinase inhibition studies are needed due to the agricultural and medicinal applications. For probing effective inhibitors of tyrosinase, a combination of computational prediction and enzymatic assay via kinetics were important. We predicted the 3D structure of tyrosinase from Agaricus bisporus, used a docking algorithm to simulate binding between tyrosinase and terephthalic acid (TPA) and studied the reversible inhibition of tyrosinase by TPA. Simulation was successful (binding energies for Autodock4 = -1.54 and Fred2.0 = -3.19 kcal/mol), suggesting that TPA interacts with histidine residues that are known to bind with copper ions at the active site. TPA inhibited tyrosinase in a mixed-type manner with a K i = 11.01 ± 2.12 mM. Measurements of intrinsic and ANS-binding fluorescences showed that TPA induced no changes in tertiary structure. The present study suggested that the strategy of predicting tyrosinase inhibition based on hydroxyl groups and orientation may prove useful for screening of potential tyrosinase inhibitors.-
dc.publisherSpringer-
dc.titleMixed-type inhibition of tyrosinase from agaricus bisporus by terephthalic acid: Computational simulations and kinetics-
dc.title.alternativeMixed-type inhibition of tyrosinase from agaricus bisporus by terephthalic acid: Computational simulations and kinetics-
dc.typeArticle-
dc.citation.titleProtein Journal-
dc.citation.number4-
dc.citation.endPage280-
dc.citation.startPage273-
dc.citation.volume30-
dc.contributor.affiliatedAuthorJin Hyuk Lee-
dc.contributor.affiliatedAuthorSanghyuk Lee-
dc.contributor.alternativeNameYin-
dc.contributor.alternativeNameSi-
dc.contributor.alternativeNameChen-
dc.contributor.alternativeNameQian-
dc.contributor.alternativeNameLu-
dc.contributor.alternativeName오상호-
dc.contributor.alternativeName이진혁-
dc.contributor.alternativeName이상혁-
dc.contributor.alternativeName양준모-
dc.contributor.alternativeName이동연-
dc.contributor.alternativeName박용두-
dc.identifier.bibliographicCitationProtein Journal, vol. 30, no. 4, pp. 273-280-
dc.identifier.doi10.1007/s10930-011-9329-x-
dc.subject.keywordDocking simulation-
dc.subject.keywordHydroxyl group-
dc.subject.keywordInhibition kinetics-
dc.subject.keywordTerephthalic acid-
dc.subject.keywordTyrosinase-
dc.subject.localDocking simulation-
dc.subject.localDocking simulations-
dc.subject.localdocking simulation-
dc.subject.localHydroxyl group-
dc.subject.localInhibition kinetics-
dc.subject.localinhibition kinetics-
dc.subject.localTerephthalic acid-
dc.subject.localtyrosinase-
dc.subject.localTyrosinase-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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