Enzymes
Characteristics All Enzymes are Proteins Catalysts – i.e. control the rate of a chemical reaction
How Enzymes work Enzymes bind and hold substrates (aka reactants) in a certain orientation to speed the chemical reaction along Enzymes change shape as they bind the substrates
the binding + substrates active site enzyme-substrate complex
the reaction, the release enzyme-substrate complex product
What about the other way? enzyme-substrate complex substrate enzyme product
Lactase 1926 aa’s long cell membranes - small intestines Lactase
Beano - alpha galactosidase breaks down trisaccharides raffinose – in beans, cabbage enzyme not in humans in bacteria in large intestines +
introducing activation energy net energy change activation energy –activation energy is the energy required to get a reaction going
How do Enzymes work? They lower the “activation energy” of the reaction net energy change –activation energy is the energy required to get a reaction going activation energy
Enzyme performance is affected by: – amount of substrate present –temperature –pH –Inhibitors –Poisons
Enzymes and Amount of Reactants [ reactants ] reaction rate because increased chance of finding molecules [reactants] reaction rate because decreased chance of finding molecules Experiment with amount and rate 1. Measure [S] or [P] 2. Combine and Plot
Enzymes and Temperature temperature reaction rate because increased kinetic energy breaks H-bonds temperature reaction rate because decreased kinetic energy does not break H-bonds
pH Acids – excess Hydrogen ions Bases – excess hydroxyl ions Neutral – equal numbers of H + and OH -
Enzymes and pH pH changes reaction rate because H-bonds are altered pH changes reaction rate because H-bonds are altered Experiment with pH and rate
Enzymes and pH each enzyme has an optimal pH; some work best in acidic conditions (<4) (pepsin) while others work best closer to a neutral pH (7) pH for Optimum Activity Enzyme pH Optimum Lipase (pancreas) 8.0 Lipase (stomach) Lipase (castor oil) 4.7 Pepsin Trypsin Urease 7.0 Invertase 4.5 Maltase Amylase (pancreas) Amylase (malt) Catalase 7.0
Enzymes and Inhibitors
bind to specific enzymes and decrease the reaction rate Normal substrate enzyme binding Competitive inhibitor binds to the active site Noncompetitive inhibitor binds to the enzyme and changes its shape
Competitive Inhibitors
Noncompetitive Inhibitors
Poisons - KCN Specific Irreversible Inhibitor of Cytochrome C Oxidase, ATP cannot be made Anaerobic respiration only Fatal build up - Lactic Acid
Poisons - Arsenic Nonspecific Inhibitor of cellular respiration enzymes Inhibits glucose break down Cell death results