Problem 1
Raisons dêtre. What are the two properties of enzymes that make them especially useful catalysts?
Problem 2
Shared properties. What are the general characteristics of enzyme active sites?
Problem 3
Partners. What does an apoenzyme require to become a holoenzyme?
Problem 6
A function of state. What is the fundamental mechanism by which enzymes enhance the rate of chemical reactions?
Problem 7
Nooks and crannies. What is the structural basis for enzyme specificity?
Problem 8
Mutual attraction. What is meant by the term binding energy?
Problem 9
Catalytically binding. What is the role of binding energy in enzyme catalysis?
Problem 11
Made for each other. Match the term with the proper description. (a) Enzyme________ (b) Substrate________ (c) Cofactor________ (d) Apoenzyme________ (e) Holoenzyme________ (f) Coenzymes________ (g)\(\Delta G^{0}\)________ (h) Transition state________ (i) Active site________ (j) Induced fit________ 1\. The least-stable reaction intermediate 2\. Site on the enzyme where catalysis takes place 3\. Enzyme minus its cofactor 4\. Protein catalyst 5\. Function of \(K_{\mathrm{eq}}^{\prime}\) 6\. Change in enzyme structure 7\. Reactant in an enzyme-catalyzed reaction 8\. A coenzyme or metal 9\. Enzyme plus cofactor 10\. Small vitamin-derived organic cofactors
Problem 12
Give with one hand, take with the other. Why does the activation energy of a reaction not appear in the final \(\Delta G\) of the reaction?
Problem 14
Mountain climbing. Proteins are thermodynamically unstable. The \(\Delta G\) of the hydrolysis of proteins is quite negative, yet proteins can be quite stable. Explain this apparent paradox. What does it tell you about protein synthesis?
