Irreversible competitive inhibitory kinetics of cardol triene on mushroom tyrosinase.
Cardol triene was first purified from cashew (Anacardium occidentale L.) nut shell liquid and identified by gas chromatography coupled to mass spectroscopy and nuclear magnetic resonance. The effects of this compound on the activity of mushroom tyrosinase were studied. The results of the kinetic study showed that cardol triene was a potent irreversible competitive inhibitor and the inactivation was of the complexing type. Two molecules of cardol triene could bind to one molecule of tyrosinase and lead to the complete loss of its catalytic activity. The microscopic rate constants were determined for the reaction of cardol triene with the enzyme. The anti-tyrosinase kinetic research of this study provides a comprehensive understanding of inhibitory mechanisms of resorcinolic lipids and is beneficial for the future design of novel tyrosinase inhibitors.
Key Laboratory of the Ministry of Education for Coastal and Wetland Ecosystems, School of Life Sciences,Xiamen University, Xiamen 361005, China.
Jiang-Xing
JX
Zhuang
Yong-Hua
YH
Hu
Mei-Hua
MH
Yang
Feng-Jiao
FJ
Liu
Ling
L
Qiu
Xing-Wang
XW
Zhou
Qing-Xi
QX
Chen
D000363:Agaricales / Q000737:chemistry / Q000201:enzymology*; D031021:Anacardium / Q000737:chemistry*; D001667:Binding, Competitive; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D005656:Fungal Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry; D007700:Kinetics; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors* / Q000737:chemistry; D012118:Resorcinols / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology
D004791:Enzyme Inhibitors; D005656:Fungal Proteins; D012118:Resorcinols; C088114:5-(8,11,14-pentadecatrienyl)resorcinol; D014442:Monophenol Monooxygenase