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

Title
Mixed-type inhibition of tyrosinase from agaricus bisporus by terephthalic acid: Computational simulations and kinetics
Authors
Yin S.-J.Si Y.-X.Chen Y.-F.Qian G.-Y.Lu Z.-R.Oh S.Lee J.Lee S.Yang J.-M.Lee D.-Y.Park Y.-D.
Ewha Authors
이상혁
SCOPUS Author ID
이상혁scopus
Issue Date
2011
Journal Title
Protein Journal
ISSN
1572-3887JCR Link
Citation
vol. 30, no. 4, pp. 273 - 280
Indexed
SCIE; SCOPUS WOS scopus
Abstract
Tyrosinase 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. © 2011 Springer Science+Business Media, LLC.
DOI
10.1007/s10930-011-9329-x
Appears in Collections:
자연과학대학 > 생명과학전공 > Journal papers
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