title: Statistical Mechanics of Allosteric Enzymes.
abstract: The concept of allostery in which macromolecules switch between two different conformations is a central theme in biological processes ranging from gene regulation to cell signaling to enzymology. Allosteric enzymes pervade metabolic processes, yet a simple and unified treatment of the effects of allostery in enzymes has been lacking. In this work, we take a step toward this goal by modeling allosteric enzymes and their interaction with two key molecular players-allosteric regulators and competitive inhibitors. We then apply this model to characterize existing data on enzyme activity, comment on how enzyme parameters (such as substrate binding affinity) can be experimentally tuned, and make novel predictions on how to control phenomena such as substrate inhibition.
authors.affiliation: Department of Physics, California Institute of Technology , Pasadena, California 91125, United States.
authors.forename: Tal
authors.initials: T
authors.lastname: Einav
authors.affiliation: Institute of Biotechnology, Vilnius University , Vilnius, 02241 Lithuania.
authors.forename: Linas
authors.initials: L
authors.lastname: Mazutis
authors.affiliation: Department of Applied Physics and Division of Biology, California Institute of Technology , Pasadena, California 91125, United States.
authors.forename: Rob
authors.initials: R
authors.lastname: Phillips
mesh_terms: D000494:Allosteric Regulation; D000495:Allosteric Site; D001665:Binding Sites; D001667:Binding, Competitive; D055162:Biocatalysis; D020134:Catalytic Domain; D004791:Enzyme Inhibitors / Q000737:chemistry*; D004798:Enzymes / Q000737:chemistry*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008956:Models, Chemical; D011485:Protein Binding; D013816:Thermodynamics
chemical_list: D004791:Enzyme Inhibitors; D004798:Enzymes