Presentation on theme: "Topic 3.6 & 7.6: Enzymes. Enzymes are organic molecules which act as catalysts Enzymes are long chains of amino acids that have a very specific three-dimensional."— Presentation transcript:
Enzymes are organic molecules which act as catalysts Enzymes are long chains of amino acids that have a very specific three-dimensional shape – Globular shape Shape is complex but very specific – Somewhere in the three- dimensional shape of the enzyme is an area that is designed to match a specific molecule known as that enzymes substrate (active site)
Enzymes are organic molecules which act as catalysts Two Analogies – Glove fits over a hand Glove represents the active site and hand represents the substrate – Lock and Key Lock represents the enzyme’s active site and the key represents the substrate (Emil Fischer 1890)
Enzymes are organic molecules which act as catalysts As catalysts, enzymes influence the rate of reactions – Reactants in the presence of an enzyme will form products at a faster rate than without the enzyme Lowers the energy level needed to start the reaction (referred to Activation Energy) Catalysts (enzymes) can be reused over and over again
Factors affecting enzyme-catalyzed reactions The reaction rate are affected by temperature, pH, and substrate concentration
Factors affecting enzyme-catalyzed reactions Temperature: – Both the enzyme and substrate are in motion and the rate of that motion is dependent on the temperature of the fluids. Fluids with higher temperature will have faster-moving molecules. Reactions are dependent on molecular collisions and the faster the molecules are moving the more often they collide.
Factors affecting enzyme-catalyzed reactions Temperature: – Reactions which use enzymes do have an upper limit Limit is based on the temperature at which the enzyme begins to lose its three-dimensional shape When the enzyme loses its shape, including the shape of the active site, it is said to be denatured – Denaturation is sometimes permanent and sometimes only temporary until the molecule re-forms its normal shape.
Factors affecting enzyme-catalyzed reactions pH – The pH of a solution is dependent on the relative number of hydrogen ions (H+) compared to hydroxide ions (OH-) in the same solution Any solution that gives off hydroxide ions is a base and results in a solution with a pH higher than 7 Any solution that give off hydrogen ions is an acid and results in a solution with a pH lower than 7 Any solution that results in an equal number of hydrogen ions and hydroxide ions
Factors affecting enzyme-catalyzed reactions The negative and positive areas of a substrate must match the opposite charge when the substrate is in the active site of an enzyme in order for enzyme to have catalytic action – When the solution is too acidic, the relatively large number of hydrogen ions can bond with the negative charges of the enzyme or substrate and not allow proper charge matching between the two (same thing with base)
Factors affecting enzyme-catalyzed reactions Most enzymes in the human body are active at or near neutral. – Pepsin is an exception to this rule. Pepsin is an enzyme that is active in the stomach. The environment of the stomach is highly acidic and pepsin is most active in an acidic pH
Factors affecting enzyme-catalyzed reactions Substrate concentration – If there is a constant amount of enzyme, as the concentration of a substrate increases, the rate of reaction will increase as well. If there is more reactant molecules, there are more to collide There is a limit to this however. The limit is due to the fact that enzymes have maximum rate at which they can work – If every enzyme molecule is working as fast as possible, adding more substrate to the solution will not further increase the reaction rate
Use of lactase in the production of lactose-free milk Lactose is a disaccharide (glucose + Galactose) milk sugar – Around 90% of all humans show some kind of lactose intolerance. People who are lactose intolerant can drink milk if it is lactose free. Lactase is an enzyme extracted from yeast that can digest the milk sugar to glucose and galactose.
Induced Fit Model As knowledge about enzyme action has increased Fischer’s model has been modified.
Mechanism of Enzyme Action 1.Surface of substrate contacts the active site of the enzyme 2.Enzyme changes shape to accommodate the substrate 3.Temp complex called enzyme-substrate is formed 4.Activation Energy is lowered and the substrate is altered by the rearrangement 5.The transformed substrate (the product) is released from the active site 6.The unchanged enzyme is free to repeat process E + S ES E + P
Inhibition Competitive Inhibition- inhibitor competes directly for the active site Non-Competitive Inhibition- inhibitor that doesn’t compete for the site…another name is allosteric inhibition End-product Inhibition (feedback inhibition)- end product stops the production of new product
Competitive Inhibition VS Non-Competitive Inhibition
End-Product Inhibition (also called feed back inhibition)