Effect of Cd2+ on tyrosinase: Integration of inhibition kinetics with computational simulation

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dc.contributor.authorL M Yue-
dc.contributor.authorJinhyuk Lee-
dc.contributor.authorZ R Lu-
dc.contributor.authorJ M Yang-
dc.contributor.authorZ M Ye-
dc.contributor.authorY D Park-
dc.date.accessioned2017-04-19T10:31:46Z-
dc.date.available2017-04-19T10:31:46Z-
dc.date.issued2017-
dc.identifier.issn0141-8130-
dc.identifier.uri10.1016/j.ijbiomac.2016.09.001ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13660-
dc.description.abstractCadmium ions (Cd2+) are a widespread and easily absorbed toxin to both humans and animals that can be spread via food, water, and air pollution. Tyrosinase (EC 1.14.18.1) is a multifunctional copper-containing enzyme that is ubiquitously expressed in animals and plays a critical role in melanin production. We evaluated the toxic effects of Cd2+ on tyrosinase activity and conformation by measuring kinetics and computationally simulating the interactions. We found Cd2+ to be a slope-hyperbolic noncompetitive-inhibition reversible inhibitor of tyrosinase, with an IC50 of 2.92 ± 0.16 mM and Ki of 0.23 ± 0.02 mM. Spectrofluorimetric measurements of intrinsic and ANS-binding fluorescence showed that Cd2+ did not induce significant changes to tyrosinase overall or to its regional active site conformations. Cd2+ showed its inactivation effect not by modulating apparent structural changes to tyrosinase, but by occupying binding sites. To gain further insight into the Cd2+/tyrosinase interaction, we performed computational docking and molecular dynamics simulations. The results consistently indicated that Cd2+ can interact with several residues near the tyrosinase active site, primarily HIS85 and ASN260. Our study provides insight into the mechanism of the toxic effects Cd2+ has on tyrosinase, which could affect the normal pigmentation pathway in animals-
dc.publisherElsevier-
dc.titleEffect of Cd2+ on tyrosinase: Integration of inhibition kinetics with computational simulation-
dc.title.alternativeEffect of Cd2+ on tyrosinase: Integration of inhibition kinetics with computational simulation-
dc.typeArticle-
dc.citation.titleInternational Journal of Biological Macromolecules-
dc.citation.numberB-
dc.citation.endPage844-
dc.citation.startPage836-
dc.citation.volume94-
dc.contributor.affiliatedAuthorJinhyuk Lee-
dc.contributor.alternativeNameYue-
dc.contributor.alternativeName이진혁-
dc.contributor.alternativeNameLu-
dc.contributor.alternativeName양정모-
dc.contributor.alternativeNameYe-
dc.contributor.alternativeName박용두-
dc.identifier.bibliographicCitationInternational Journal of Biological Macromolecules, vol. 94, no. B, pp. 836-844-
dc.identifier.doi10.1016/j.ijbiomac.2016.09.001-
dc.subject.keywordCd2+-
dc.subject.keywordMolecular dynamics-
dc.subject.keywordTyrosinase inhibition-
dc.subject.localCd2+-
dc.subject.localMolecular dynamics-
dc.subject.localmolecular dynamics-
dc.subject.localTyrosinase inhibition-
dc.subject.localtyrosinase inhibition-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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