3. Which of the following statements regarding enzymes and transition states is true?a. stabilization of the transition state must be less than stabilization of ES forcatalysis to occurb. binding of substrate to an enzyme often causes strain, thus promoting transitionstate formationc. the transition state conformation of an enzyme catalyzed reaction is identical to theconformation seen in the uncatalyzed transition stated. formation of the transition state always assures that the reaction will proceed toproducte. none of the above are true4. What is the starting point for selection of a suitable ion-exchange chromatography matrixfor purification of a recombinant protein?a. Prediction of isoelectric point (pl) from the amino acid sequence.b. Test protein binding to an ion-exchange matrix at a range of pHs and saltconcentrations.c. Test protein binding to a selection of anion and cation exchange matrices.d. Pass your sample through a preparative column and elute with a salt gradient.e. Calculation of net charge from the amino acid sequence.5. The unfolding rate of a protein in the absence of denaturant is ~10 s!. The refolding rate ofthe protein is 2 x 10$ s''. If we assume that the system is a two-state folding process, whatis the conformational stability (in kJ mol-l at 25°C) for the protein?а. 25b. 10с. 15d. 20е. 306. An enzymatic reaction has a Vmax of 20 min-!. At a substrate concentration of 50 µM, thevelocity of the reaction is 20 min-!. Which of the following is most likely true?a. the Km of the reaction is much less than 50 µMb. the Km of the reaction is much greater than 50 µMc. the Km of the reaction is equal to 50 µMd. the Km of the reaction is equal to 25 µMe. cannot be determined from the information given

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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24. Consider the figure below, which is an alternate way to depict the energy changes occurring during a reaction from Substrate (S) to Product (P), when uncatalyzed (curve A) and when catalyzed by an enzyme (curve B). Note that curve B is not the same way we modeled an enzyme-catalyzed reaction in class; this model is a different, perhaps slightly more realistic, way of conceptualizing the energy changes over the course of a reaction than what we did in class. S and ES represent the transition states for reaction of the free substrate (S) or the enzyme-substrate complex (ES). T T activation energy for uncatalyzed reaction EST S edhosob nohtum od bluo woH abiow yedio 2 wwolaixa-y odi no vaigin oroda dapng odt ni o nfog) r gibadhoa P B ES EP progress of reaction activation energy for catalyzed reaction a) Explain briefly why, in curve B, the energy state of the enzyme-substrate complex is less than the energy state of the substrate alone. b) Suppose the enzyme in the diagram was mutated…
8. Which of the following is characteristic of a competitive inhibitor of an enzyme-catalyzed reaction? A. The inhibitor binds covalently to the enzyme. B. The inhibitor increases the substrate binding affinity to the enzyme. C. In the presence of the inhibitor, the reaction exhibits an apparent increase in Km. D. In the presence of the inhibitor, the reaction exhibits an apparent decrease in Vmax- E. Increasing the substrate concentration fails to overcome the effects of the inhibitor.
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.
1. If a molecule is interating with its side chains of an enzymes active site but it is not the substrate of the enzyme what kind of enzyme regulation is this? 2. What is the change in thetype of bond between Ser 80 -> Arg. 3. Will this change cause the complex to be more or less stable. Explain
1. Compare and contrast the activation free energy and the free energy change for an enzyme-catalyzed reaction.
4. An enzyme-substrate complex has a Kd = 100 nM. A competitive inhibitor with which of the following Ki values will be most effective at inhibiting this enzyme? A) K₁ = 10 nM B) K₁ = 100 nM C) K₁ = 1000 nM D) None of the above - only the KM is important Briefly explain:
1. define in your own words enzyme 2. explain how enzymes act on a substrate 3. explain the term catalyst 4. what is meant by optimal conditions for enzymes and what are the conditions 5. explain what catalase is: what it helps to break down and into what parts.
37. Consider the following energy diagram for an enzyme-catalyzed reaction. D B A C E G Which step is probably the slowest? a. A →B →C b. C D E c. E F G d. G H I
1. ( . tion can be represented by the so-called Michaelis equation ) The velocity of an enzyme catalyzed reac- Vmax [S] Vo = Km Vo = max kcat [Eo] [So] (Км + [Sol) V max where [So] is the initial substrate concentration, [Eo] is the total enzyme concentration, kcat is the cataly- tic rate constant or turnover number, and KM repre- sents the Michaelis constant. The graph on the right illustrates the dependence of the velocity of the reaction as a function of substrate concentration. Ex- Km [S] (mm) plain why the maximal velocity can be represented by the expression Vmax = Kcat [Eo] at very high substrate concentrations. Vo (µm/min)
8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.
3. The reaction shown below is catalyzed along the pathway of glycolysis by an enzyme with the active site architecture shown. A. The enzyme has two Mg2+ ions, a lysine general base (deprotonated) and a glutamate general acid. In the box below, draw a plausible mechanism for this reaction, which has two formal steps with one intermediate between them (hint: one step uses the general acid and the other uses the general base.) O +(87 -00 11 R-00 00 00 + H₂O OH O Mg2+ Mg2+ Lys (general base) NH₂ OH Glu (general acid) enzyme active site
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes

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