The effect of rutin on arginine kinase: inhibition kinetics and thermodynamics merging with docking simulation.
Arginine kinase (AK; EC 2.7.3.3) is a key enzyme in the cellular energy metabolism of insects. Screening on potential effective inhibitors of AK may provide a pathway for novel, environmentally friendly insecticides. The results in this study indicated that rutin, as a noncompetitive inhibitor, interacts with AK mainly by a hydrophobic force forming an intermolecular complex with AK, which is according to the thermodynamic parameters obtained. Using a flexible docking method (AutoDock) the interaction between rutin and AK were further analyzed, which suggested in order to screen effective inhibitors, flexible active sites of AK (Ser63, Gly64, Val65, Tyr68) should be taken in account.
Wu
Xue-Qiang
XQ
College of Life Science, Shandong Agricultural University, Tai'an, Shandong 271018, PR China.
Zhu
Wen-Jing
WJ
Lü
Zhi-Rong
ZR
Xia
Yong
Y
Yang
Jun-Mo
JM
Zou
Fei
F
Wang
Xiao-Yun
XY
D000818:Animals; D001122:Arginine Kinase / Q000037:antagonists & inhibitors*; D001665:Binding Sites; D003198:Computer Simulation; D006110:Grasshoppers / Q000201:enzymology; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D007700:Kinetics; D008958:Models, Molecular; D012431:Rutin / Q000737:chemistry / Q000494:pharmacology*; D013050:Spectrometry, Fluorescence; D013696:Temperature; D013816:Thermodynamics
D012431:Rutin; D001122:Arginine Kinase