Enzymes
n Catalytic proteins n Catalyst - a chemical agent that changes the rate of reaction, without being consumed by the reaction
Free energy of activation n Initial investment of energy to start a reaction n Energy used to break the bonds in the reactant n Activation energy = E A
Enzymes Lower Activation Energy
Active Site - Catalytic region n Lowers the Ea in a variety of ways –Provides a template for orientation of the substrate –Changes the substrate, stressing critical bonds –Provides correct microenvironment
Active Site
Substrate Specificity n Uniquely shaped active site determines the particular substrate that can be acted upon n Induced fit - binding of the Enzyme to Substrate causes a slight change in shape of the Enzymes
Induced Fit
Environmental effects n Environment can influence 3-D structure of the protein (enzyme) i.e. adding H 2 SO 4 denatures the enzyme n Each enzyme has optimum conditions for pH and temp
pH and Temperature effects
Cofactors n Nonprotein ions or organic molecules (coenzymes) n Required for the proper function of some enzymes –NADH –Coenzymes –Vitamins –Metals
Cofactors Metal Ion Changes the active site shape
Inhibitors n Selectively reduce Enzyme function n Competitive –Structurally similar to Substrate –Competes for active site binding
Competitive Inhibitors
n Noncompetitive –Binds to a place other than the active site –Disrupts Enzyme’s shape or function
Non-Competitive Inhibitor
Allosteric Interaction-Inactivator
Allosteric Interaction- Activator
Regulatory molecules n Activator (increases rate) n Inhibitor (decreases rate) n Binds to allosteric sites = noncatalytic sites that alter the Enzyme conformation/function