DC Field | Value | Language |
---|---|---|
dc.contributor.author | L M Yue | - |
dc.contributor.author | Jinhyuk Lee | - |
dc.contributor.author | Z R Lu | - |
dc.contributor.author | J M Yang | - |
dc.contributor.author | Z M Ye | - |
dc.contributor.author | Y D Park | - |
dc.date.accessioned | 2017-04-19T10:31:46Z | - |
dc.date.available | 2017-04-19T10:31:46Z | - |
dc.date.issued | 2017 | - |
dc.identifier.issn | 0141-8130 | - |
dc.identifier.uri | 10.1016/j.ijbiomac.2016.09.001 | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/13660 | - |
dc.description.abstract | Cadmium 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.publisher | Elsevier | - |
dc.title | Effect of Cd2+ on tyrosinase: Integration of inhibition kinetics with computational simulation | - |
dc.title.alternative | Effect of Cd2+ on tyrosinase: Integration of inhibition kinetics with computational simulation | - |
dc.type | Article | - |
dc.citation.title | International Journal of Biological Macromolecules | - |
dc.citation.number | B | - |
dc.citation.endPage | 844 | - |
dc.citation.startPage | 836 | - |
dc.citation.volume | 94 | - |
dc.contributor.affiliatedAuthor | Jinhyuk Lee | - |
dc.contributor.alternativeName | Yue | - |
dc.contributor.alternativeName | 이진혁 | - |
dc.contributor.alternativeName | Lu | - |
dc.contributor.alternativeName | 양정모 | - |
dc.contributor.alternativeName | Ye | - |
dc.contributor.alternativeName | 박용두 | - |
dc.identifier.bibliographicCitation | International Journal of Biological Macromolecules, vol. 94, no. B, pp. 836-844 | - |
dc.identifier.doi | 10.1016/j.ijbiomac.2016.09.001 | - |
dc.subject.keyword | Cd2+ | - |
dc.subject.keyword | Molecular dynamics | - |
dc.subject.keyword | Tyrosinase inhibition | - |
dc.subject.local | Cd2+ | - |
dc.subject.local | Molecular dynamics | - |
dc.subject.local | molecular dynamics | - |
dc.subject.local | Tyrosinase inhibition | - |
dc.subject.local | tyrosinase inhibition | - |
dc.description.journalClass | Y | - |
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