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

Cited 34 time in scopus
Metadata Downloads
Title
Mixed-type inhibition of tyrosinase from agaricus bisporus by terephthalic acid: Computational simulations and kinetics
Author(s)
S J Yin; Y X Si; Y F Chen; G Y Qian; Z R Lu; S Oh; Jin Hyuk Lee; Sanghyuk Lee; J M Yang; D Y Lee; Y D Park
Bibliographic Citation
Protein Journal, vol. 30, no. 4, pp. 273-280
Publication Year
2011
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.
Keyword
Docking simulationHydroxyl groupInhibition kineticsTerephthalic acidTyrosinase
ISSN
1572-3887
Publisher
Springer
DOI
http://dx.doi.org/10.1007/s10930-011-9329-x
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.