LEARNING OBJECTIVES By the end of this chapter, you should be able to: 1. Discuss four general strategies used by enzymes to accelerate particular reactions. 2. Give examples of specific chemical features of enzyme active sites that facilitate increasing the rates of specific reactions. 3. Give an example of when high absolute rate acceleration is physiologically important and how an enzyme achieves this acceleration. 4. Understand when high specificity is important for an enzyme and how this specificity is achieved. 5. Describe an example of when large conformational changes that occur during an enzymatic reaction cycle are used to drive other processes. 6. Discuss some of the experimental approaches that are used to elucidate enzymatic mechanisms.
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Four general strategies used by enzymes to accelerate particular reactions are: - Proximity and orientation effects: Enzymes bring substrates close together and in the correct orientation, reducing the entropy of the system and increasing the reaction rate. Show more…
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Classify the enzyme inhibitors by giving the names, mechanisms, and effects on the kinetic parameters Km and Vmax. Draw and annotate a double reciprocal plot for each type of inhibition. 2. For an enzyme reaction followed spectrophotometrically at 340 nm, the Vmax was calculated at 0.14 ΔA340/min (ε340 = 5.22 mM-1.cm-1). The 1 mL reaction in a 1 cm cuvette contained 30 ng of an enzyme (Mr of 100,000 g/mole). Calculate the Kcat for this enzyme. 3. An example of an enzyme-catalyzed reaction proceeding via a transition-state stabilization mechanism is the hydrolysis of peptides by chymotrypsin, while lysozyme is often cited as an example of an enzyme which operates by a strain mechanism. Discuss both mechanisms in the context of each enzyme.
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(a) Explain the importance of enzymes in biological systems. (b) What chemical transformations are catalyzed (i) by the enzyme catalase, $(i i)$ by nitrogenase? (c) Many enzymes follow this generic reaction mechanism, where $\mathrm{E}$ is enzyme, $\mathrm{S}$ is substrate, ES is the enzyme-substrate complex (where the substrate is bound to the enzyme's active site), and $\mathrm{P}$ is the product: 1. $\mathrm{E}+\mathrm{S} \rightleftharpoons \mathrm{ES}$ 2. $\mathrm{ES} \longrightarrow \mathrm{E}+\mathrm{P}$ What assumptions are made in this model with regard to the rate of the bound substrate being chemically transformed into bound product in the active site?
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