The effect of trifluoroethanol on tyrosinase activity and conformation: Inhibition kinetics and computational simulations

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Title
The effect of trifluoroethanol on tyrosinase activity and conformation: Inhibition kinetics and computational simulations
Author(s)
Z R Lu; L Shi; J Wang; Dae Ui Park; Jong Hwa Park; J M Yang; Y D Park; H W Zhou; F Zou
Bibliographic Citation
Applied Biochemistry and Biotechnology, vol. 160, no. 7, pp. 1896-1908
Publication Year
2010
Abstract
We studied the inhibitory effects of trifluoroethanol (TFE) on the activity and conformation of tyrosinase. TFE increased the degree of secondary structure of tyrosinase, which directly resulted in enzyme inactivation. A reciprocal study showed that TFE inhibited tyrosinase in a slope-parabolic mixed-type inhibition manner (K I=0.5±0.096 M). Time-interval kinetic studies showed that the inhibition was best described as first order with biphasic processes. Intrinsic and 1-anilinonaphthalene-8-sulfonate-binding fluorescences were also measured to gain more insight into the supposed structural changes; these showed that TFE induced a conspicuous tertiary structural change in tyrosinase by exposing hydrophobic surfaces. We also predicted the tertiary structure of tyrosinase and simulated its docking with TFE. The docking simulation was successful with significant scores (binding energy for Autodock4=-4.75 kcal/mol; for Dock6=-23.07 kcal/mol) and suggested that the TRP173 residue was mainly responsible for the interaction with TFE. Our results provide insight into the structure of tyrosinase and allow us to describe a new inhibition strategy that works by inducing conformational changes rather than targeting the active site of the protein.
Keyword
Docking simulationInhibition kineticsSecondary structureTrifluoroethanolTyrosinase
ISSN
0273-2289
Publisher
Springer
DOI
http://dx.doi.org/10.1007/s12010-009-8730-9
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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