Study Guide - Biochemistry, The Molecular Basis of Life, 4th Ed., 2009, T. & J.R. McKee (Oxford Univ. Press)
Chapter 6: Enzymes
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Define Catalysis. How do enzymes differ from laboratory catalysts? (for example: control, specificity and saturation)
What is a spontaneous reaction? Know what exergonic and endergonic mean.
What determines the rate of a reaction? What is activation energy
and how does the transition state apply?
Explain the lock-and-key and induced-fit models of enzyme
activity, using the terms substrate and active site.
How does enzyme concentration affect the rate of reaction? How does substrate concentration affect the rate of reaction?
Understand the hyperbolic relationship between [S] (substrate concentration) and V0 (initial reaction velocity). You should also know what Km, Vmax and the turnover number are, but not how to derive them, unless it helps you.
What is the difference between reversible and irreversible inhibitors?
What is the difference between competitive and noncompetitive inhibitors? Why is methanol poisonous? How is ingestion treated? Relate this to inhibitors.
What is an allosteric enzyme? If the effector is an inhibitor, which of the above is it?
Describe a specific example of a zymogen.
What part of a protein's mass is the active site? How does this site affect catalysis?
All coenzymes are cofactors, but not all cofactors are coenzymes. What are these substances? What is their function in enzymatic reactions? Which are vitamins?
In what two categories do we classify vitamins? List their names, functions and deficiency symptoms/diseases (see Table 6.3).
How does pH affect the rate of reaction, and why? How does temperature affect the rate of reaction, and why? The Q10 rule is?
How are enzymes regulated? Why are they so regulated?
End of the chapter 6 review questions: 1.-12. 14-17. 22.-27. 30. 32. 36. 37. 39.-50.
End of the chapter 7 review questions: 24.-29. 48.-50.
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Last Modified on 7/16/2008