Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Transcribed Image Text:28. Describe the role of an amplifier enzyme.
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- Explain the induced-fit model of enzymes function and describe the catolytic cycle of an enzymearrow_forwardam. 206.arrow_forward4. Enzyme performance (a) Compare chymotrypsin, MutY, and carbonic anhydrase in terms of chemical difficulty. (Hint: compare kcat). (b) Which enzyme is faster? And by how much? (c) Draw a molecular sketch comparing TS stabilization strategies for Muty and chymotrypsin. (d) Compare chymotrypsin, Muty, and carbonic anhydrase in terms of how quickly they find their substrates. (Hint: compare kcat/KM). Which enzyme has the more "perfect" enzyme performance rating? (e) What is the molecular explanation for the apparently impossible fast rate at which Muty finds its substrate? (f) What is the biological constraint demanding this very high level of enzyme performance? Enzyme\Parameter Carbonic anhydrase Muty Chymotrypsin kcat (s-1) 600,000 0.2 100 KM (M) 0.008 1.2 x 10-10 0.005arrow_forward
- 1. For enzymatic reaction, a mechanism was proposed by Michaelis and Menten as follows: ES k, and k,' ES à E and P k,. E + S a. Use steady state assumption, derive expression for the reaction rate. Where E is concentration of enzyme, S substrate, ES complex of E and S, E = E, – ES. (If you have difficulty in doing it, please consult lecture note) b. Assume K = 0.038 mol.L' at 25 °C, when the substrate concentration is 0.156 Mol.L', the rate of the reaction is 1.21 m mol/L.s. The maximum rate of conversion reaction is reached at high substrate concentrations. Calculate the maximum rate of this enzyme catalyzed reaction.arrow_forward48arrow_forward1. Construct a model that demonstrates how enzyme catalyzed reactions harvest energy from simple carbohydrates.arrow_forward
- 1. Compare and contrast the activation free energy and the free energy change for an enzyme-catalyzed reaction.arrow_forward111 The Michaelis constant is represented by what variable, and is comprised of which rate constants in the overall enzyme rate equation? e. Km, kf, kr and k_cat f. Vmax, kf and kcat g. Km, kf, kr and kcat h. Vmax, kf, kr and kcat Km, kf and kcat i.arrow_forward(a) Lock and key model versus induced fit model of enzyme activity. (b) Competitive and non-competitive enzyme inhibitors. (c) Reversible and irreversible enzyme inhibitors.arrow_forward
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