title: The effect of rutin on arginine kinase: inhibition kinetics and thermodynamics merging with docking simulation.
abstract: 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.
authors.affiliation: College of Life Science, Shandong Agricultural University, Tai'an, Shandong 271018, PR China.
authors.forename: Xue-Qiang
authors.initials: XQ
authors.lastname: Wu
authors.forename: Wen-Jing
authors.initials: WJ
authors.lastname: Zhu
authors.forename: Zhi-Rong
authors.initials: ZR
authors.lastname: Lü
authors.forename: Yong
authors.initials: Y
authors.lastname: Xia
authors.forename: Jun-Mo
authors.initials: JM
authors.lastname: Yang
authors.forename: Fei
authors.initials: F
authors.lastname: Zou
authors.forename: Xiao-Yun
authors.initials: XY
authors.lastname: Wang
mesh_terms: 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
chemical_list: D012431:Rutin; D001122:Arginine Kinase