英文课件-酶5.pptVIP

Enzyme Regulation  Allosteric regulation Covalent Modifications  Aspartate transcarbamoylase ATCase Organization of ATCase catalytic unit: 6 subunits organized into 2 trimers regulatory unit: 6 subunits organized into 3 dimers ATCase in metabolic pathway ATCase’s kinetics (a) Rate of ATCase catalysis vs substrate conc. ATCase’s kinetics (b) ATCase catalysis in presence of CTP; ATP ATCase’s allosteric effectors Why ? The key to allosteric behavior is the existence of multiple forms for the 4o structure of the enzyme. Allosteric effector modifies the 4o structure of an allosteric enzyme. Allosteric enzymes Allosteric enzyme: an oligomer whose biological activity is affected by other substances binding to it these substances change the enzyme’s activity by altering the conformation(s) of its 4° structure Homoallostery: Binding of one substrate favors binding of additional substrates. Heteroallostery :The kinetics of the enzyme can be controlled by any other substance that, in binding to the protein. Allosteric Effectors Allosteric effector: a substance that modifies the behavior of an allosteric enzyme; may be an Allosteric Activators(positive effectors)increase substrate binding and/or the rate of the chemical step (kcat). Allosteric inhibitors(negative effectors) reduce substrate binding and/or the rate of the chemical step. Allosteric Effects homotropic effects: allosteric interactions that occur when several identical molecules are bound to the protein; e.g., the binding of aspartate to ATCase heterotropic effects: allosteric interactions that occur when different substances are bound to the protein; e.g., inhibition of ATCase by CTP and activation by ATP Allosteric Activation Allosteric Inhibition homotropic effects homotropic effects homotropic effects Heteroallostery The Concerted Model(WMC Model) Wyman, Monod, and Changeux – 1965 WMC Model explains the sigmo