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Title 

The effect of thiobarbituric acid on tyrosinase: inhibition kinetics and computational simulation

 

타이로시네이즈내 Thiobarbituric 산의 영향: 저해제 반응 속도론 및 분자동력학 모의실험

Authors 

S J YinY X SiZ J WangS F WangSangho OhSanghyuk LeeS M SimJ M YangG Y QianJin Hyuk LeeY D Park

Publisher 

Adenine Press

Issue Date 

2011

Citation 

Journal of Biomolecular Structure & Dynamics, vol. 29, no. 3, pp. 463-470

Keywords 

Docking simulationInhibition kineticsThiobarbituric acidTyrosinase

Abstract 

Tyrosinase plays various roles in organisms and much research has focused on the regulation of tyrosinase activity. We studied the inhibitory effect of thiobarbituric acid (TBA) on tyrosinase. Our kinetic study showed that TBA inhibited tyrosinase in a reversible noncompetitive manner (Ki = 14.0 ± 8.5 mM and IC50 = 8.0 ± 1.0 mM). Intrinsic and ANS-binding fluorescences studies were also performed to gain more information regarding the binding mechanism. The results showed that no tertiary structural changes were obviously observed. For further insight, we predicted the 3D structure of tyrosinase and simulated the docking between tyrosinase and TBA. The docking simulation was successful with significant scores (binding energy for AutoDock4: -5.52 kcal/mol) and suggested that TBA was located in the active site. The 11 ns molecular dynamics simulation convinced that the four HIS residues (residue numbers: 57, 90, 250, and 282) were commonly responsible for the interaction with TBA. Our results provide a new inhibition strategy that works using an antioxidant rather than targeting the copper ions within the tyrosinase active site.

ISSN 

0739-1102

Link 

http://dx.doi.org/10.1080/07391102.2011.10507398

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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