对甲氧基肉桂酸对酪氨酸酶的抑制机理  

Inhibition Mechanism of 4-Methoxycinnamic Acid to Tyrosinase

作　　者：穆燕[1] 李琳[1] 董方圆[1] 胡松青[1] 

机构地区：[1]华南理工大学轻工与食品学院,广东广州510640

出　　处：《华南理工大学学报（自然科学版）》2012年第12期134-138,共5页Journal of South China University of Technology(Natural Science Edition)

基　　金：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)

摘　　要：以L-酪氨酸和L-多巴为底物研究了对甲氧基肉桂酸对酪氨酸酶的抑制能力,结果表明,对甲氧基肉桂酸对酪氨酸酶催化单酚底物L-酪氨酸有较强的抑制作用,但对酪氨酸酶催化二酚底物L-多巴没有抑制作用.文中采用荧光光谱以及分子对接手段探讨了对甲氧基肉桂酸对酪氨酸酶的抑制机理,认为对甲氧基肉桂酸对酪氨酸酶的荧光光谱属于静态猝灭,在酪氨酸酶活性中心与酪氨酸酶结合形成复合物,以氢键和疏水作用力稳定结构;在酪氨酸酶活性中心,对甲氧基肉桂酸占据了单酚底物的空间位置,对酪氨酸酶的抑制应该是一种竞争性抑制.In this paper, L-tyrosine and L-dopa were used as the substrates to reveal the inhibition of 4-methoxycin- namic 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.

关 键 词：酪氨酸酶 对甲氧基肉桂酸 抑制 荧光猝灭 分子对接 

分 类 号：Q554.1[生物学—生物化学]