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Title 

Effects of piperonylic acid on tyrosinase: mixed-type inhibition kinetics and computational simulations

Authors 

Y X SiS JiN Y FangW WangJ M YangG Y QianY D ParkJinhyuk LeeS J Yin

Publisher 

Elsevier

Issue Date 

2013

Citation 

Process Biochemistry, vol. 48, no. 11, pp. 1706-1714

Keywords 

Docking simulationInhibition kineticsMolecular dynamicsPiperonylic acidTyrosinase

Abstract 

Piperonylic acid is a natural molecule with a benzoic acid group and high antioxidant capacity. Based on its aromatic acid structure and antioxidant properties, we studied the effects of piperonylic acid on tyrosinase by the analysis of its inhibitory kinetics and computational simulations. Piperonylic acid reversibly inhibited tyrosinase through a mixed-type inhibitory mechanism. The time courses of the tyrosinase inhibition showed that piperonylic acid binds to tyrosinase very quickly and the inactivation processes follow first-order kinetics. The continuous substrate reactions indicated that piperonylic acid induced a tight-binding inhibition and the substrate can promote the inactivation process. The ANS-binding fluorescence of tyrosinase suggested that piperonylic acid did not detectably disrupt the tertiary structure of the enzyme. The results of the computational docking and molecular dynamics simulations showed that piperonylic acid closely interacts with three residues and it might block the active site of tyrosinase. Abbreviations*L- DOPA*3,4-dihydroxyphenylalanine*ANS*1-anilinonaphthale ne-8-sulfonate.

ISSN 

0032-9592

Link 

http://dx.doi.org/10.1016/j.procbio.2013.08.006

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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