Goals 6.3, Enzyme Kinetics:
- Describe how the Michaelis-Menten model is consistent with rate data for a typical enzyme (first order regime/mixed order regime/zero order regime)
- Describe, mathematically and otherwise, what is meant by the phrase "steady-state assumption"
- Be able to explain how other kinetic models don't fit the experimental data
- Explain the significance of Lineweaver-Burke plots of enzyme kinetic data (linear curve fitting and ability to measure Vmax)
- Interpret Lineweaver-Burke plots
- Describe three methods of enzyme inhibition (competitive, uncompetitive, and noncompetitive inhibition)
Goals 6.3, Enzyme Kinetics; 6.1 Properties of Enzymes:
- Describe three methods of enzyme inhibition (competitive, uncompetitive, and noncompetitive inhibition)
- Interpret Lineweaver-Burke plots of kinetic data from the reactions of inhibited enzymes
- Explain why enzyme being inhibited via competitive inhibition can still achieve their uninhibited Vmax, whereas enzymes experiencing uncompetitive or noncompetitive inhibition have a reduced Vmax
- Compare and contrast the obsolete lock and key model with the induced fit model for substrate recognition
- Understand that enzymes effect the kinetics of a reaction not the thermodynamics of the reaction
Goals 6.1, Properties of Enzymes; 6.2, Classification of Enzymes; and 6.4, Catalysis:
- Describe some of the basic ways enzymes acomplish their jobs (proximity and strain, stabilizing transition states, electrostatic effects, general acid-base catalysis, covalent catalysis)
- Explain electron movemnt arrows that are drawn on the mechanisms of enzyme catalyzed reactions
- Draw electron movement arrows for single steps of enzyme catalyzed reactions when the starting and ending states are drawn
- Explain the role of amino acids, coenzymes, or cofactors present in the active site of the enzyme
Goals 6.4, Catalysis; 6.5 Enzyme Regulation:
- Explain electron movemnt arrows that are drawn on the mechanisms of enzyme catalyzed reactions
- Draw electron movement arrows for single steps of enzyme catalyzed reactions when the starting and ending states are drawn
- Explain the role of amino acids, coenzymes, or cofactors present in the active site of the enzyme
- Decribe some of the basic mechanisms of enzyme regulation