Journal of South China University of Technology(Natural Science Edition) ›› 2012, Vol. 40 ›› Issue (12): 134-138.

• Biological Engineering • Previous Articles     Next Articles

Inhibition Mechanism of 4-Methoxycinnamic Acid to Tyrosinase

Mu Yan  Li Lin  Dong Fang-yuan  Hu Song-qing   

  1. School of Light Industry and Food Sciences,South China University of Technology,Guangzhou 510640,Guangdong,China
  • Received:2012-04-19 Revised:2012-05-23 Online:2012-12-25 Published:2012-11-02
  • Contact: 胡松青(1972-) ，男，博士，教授，主要从事天然产物化学及蛋白质结构生物学研究． E-mail: fesqhu@ scut． edu． cn E-mail:muyan325@ gmail.com
  • About author:穆燕(1984-) ，女，博士，主要从事天然产物化学及蛋白质结构生物学研究．
  • Supported by:

    国家"973”计划项目( 2012CB720801) ; 国家自然科学基金资助项目( 31130042， 31171630) ; 教育部新世纪优秀人才支持计划项目( NCET-10-0362) ; 华南理工大学中央高校基本科研业务费专项资金资助项目( 2012ZG0007)

PDF

929

Abstract:

In this paper,L-tyrosine and L-dopa were used as the substrates to reveal the inhibition of 4-methoxycinnamic acid ( MCA) to tyrosinase,finding that MCA greatly inhibits the catalytic activity of tyrosinase for monohydric phenol L-tyrosine but has no effect on the catalytic activity for diphenol L-dopa. Then,the inhibition mechanism of MAC to tyrosinase was investigated by means of the fluorescence spectroscopy and the molecular docking. It
is shown that ( 1) the quenching mechanism of MCA to tyrosinase belongs to a static type; ( 2) MCA forms a complex with tyrosinase through hydrogen bonds and hydrophobic forces in the catalytic center of tyrosinase; and ( 3) as MCA occupies the position of monohydric phenols in the catalytic center of tyrosinase,it may provide a competitive inhibition to tyrosinase.

Key words: tyrosianse, 4-methoxycinnamic acid, inhibition, fluorescence quenching, molecular docking