Matching Question:Researchers characterized a new enzyme and determined its Km=200 uM. Moreover, they found that at (Etotad10 nM this enzyme reaches maximum reaction velocity Venasa5 is1. What is the keat of this enzyme?2. At which concentration of the substrate this enzyme reaches initial reaction velocity (Vo) of 500 nM/s (assuming (Etotal is the same 10 nMy?3. What is the maximum reaction velocity (Vmax) of the reaction catalyzed by this enzyme at (Etotail4 nM?Make sure to choose the correct units of measure. Note that some of the items from the answer list should NOT be used.v kcat1. 400 uM- (S] -- Vmax2 100 uM500 s450 uM250 s1* 5017. so00 s1 UM'sSuMis10 200 uM11. 10 uMis12 25 s13. 500 nM/s

Given, Km = 200 μM [ETotal] = 10 nm = 0.01 Vmax = 2.5 μM/s

Answered: 1. What is the keat of this enzyme? 2.…

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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2. An enzyme-catalyzed reaction is carried out at several different substrate concentrations (listed below), either (1) with no inhibitor, or (2) in the presence of an inhibitor, I, at 0.63 g/L. Given the following data, determine: A. what type of inhibitor I is B. the value of Ki No Inhibitor: With Inhibitor: Substrate Concentration (g/L) 0.86 Reaction Velocity (g/L-s) Reaction Velocity (g/L-s) 0.179 0.161 2.35 3.80 4.90 6.10 18.4 0.398 0.567 0.666 0.726 0.950 0.322 0.407 0.443 0.495 0.639
2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…
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15) The graph at right shows the results of reaction rate vs. substrate concentration for a Michaelis-Menten type enzyme 16) Th a. True b. False* reaction rate substrate concentration
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.
1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)
4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.
1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? Explain
Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…

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