For glycolysis, what is the sum of the flux control coefficient (C) values for all 10 enzymes involved? a. 0 b. Can't tell from data given c. 1.3 d. 0.7 e. 1.0
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- It takes 9.4 msec for Enzyme X to catalyse a single reaction when it is fully saturated with substrate. Calculate the Vmax of the reaction if the concentration of Enzyme X is 2.4 mM. Select one: a. 26 mM/sec X b. 3.9/sec c. 0.26 M/sec d. 0.039 M/sec e. 106.4 M/secConsider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?A scientist is studying the enzyme X which is an important point of regulation in the metabolism of the inhabitants of Sumeru. He developed four Akademiyan-derived compounds which may possibly work against this enzyme, and tested using an eudiometer the metabolic rate of the sample cell lines. Data are below. Time for each compound (min) Eudiometer volume reading (mL) A B C D 0 83.1 62.6 89.0 66.4 5 83.2 100.6 90.2 71.4 10 83.2 83.6 95.0 77.2 15 83.2 83.6 100 84.6 20 83.3 110.8 104.6 88.2 Show the properly labeled volume versus time plot for each eudiometer, with the equation of the line and R2. What is the most effective inhibitor among the four compounds? It was found that the most effective inhibitor exhibits uncompetitive inhibition. Illustrate the Lineweaver-Burk plots of uninhibited and inhibited enzyme X with properly labeled axes.
- The Km value of an enzyme-catalyzed reaction and its Vmax is 70 mmol/min. What is the rate of the reaction of the reaction when the substrate concentration is 7 × 10−2 mmol/min? a. 35 mmol/min b. 50 mmol/min c. 60 mmol/min d. 70 mmol/minSucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…The initial rate for an enzyme-catalyzed reaction has been determined at several substrate concentrations. Data are as follows: [S] µmol/L V[(umol/L) min1] 5 22 10 39 20 65 50 102 100 120 200 135 If the total enzyme concentration was 1nmol/L, how many molecules of substrate can a molecule of enzyme process in each minute? A. 175000 B. 325000 C. 900000 D. 10000 E. 375000 F. 166000 G. 3750 H. 1000000 I. 12500
- Sketch and label a plot showing the enzyme's initial velocity relative to pH over the pH range 4 - 9 for the enzyme-catalyzed reaction under these two conditions: A. The substrate concentration is very, very high. B. The substrate concentration is less than the enzyme's Km.If we examine all of the enzymes involved in the CAC as it's own isolated pathway. What would be the sum of the Flux Control Coefficients (C) of all the enzymes involved in this pathway? O 2.3 O 0.4 O 1.5 1.0 O 0.0Evaluate the following statements concerning enzyme kinetics. Which one of the statements is false? a. Enzyme saturation fluctuates. b. In an uninhibited enzymatic reaction system, adding an excess of substrate will increase the reaction velocity beyond Vmax. c. The Vmax of an enzyme kinetics graph represents the point at which the enzyme is saturated with substrate. d. Non-competitive inhibition of an enzymatic reaction can be overcome by adding more unaltered enzyme. e. The activation energy of a reaction can be reduced by the presence of an enzyme.
- You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered enzyme known as BILISTASE. The kinetics data are shown below: [Substrate, uM) Vo with DEDS (uM/min) Vo without DEDS (uM/min) 1.667 1.600 3.544 2.500 1.923 4.259 3.333 2.139 4.737 14.000 2.268 5.019 5.000 2.410 5.336 Using linear regression analysis, determine the values of Vmax and KM of the enzyme in the ABSENCE of inhibitor: (Express your answer in 3 decimal places, do NOT include the units) Vmax KMConsider the following enzyme cartoons or structures carefully. Note active sites, presence of cofactors, substrates, etc. and then answer the following questions with the applicable numbers 1, 2, 3, 4, None or All. More than one number may apply. 3. 2. 1. GO Substrate Enzyme Substrate Enzyme Pepsin Enolase a. Example(s) of an allosteric enzyme b. Example(s) of a proteolytic enzyme c. Example(s) of an enzyme(s) with cofactor(s) e. Example(s) of an enzyme(s) that could be impacted by an irreversible competitor. d. Example(s) of an enzyme(s) with a second site for feedback control. f. Enzyme(s) definitely composed of two or more protein chains.Which of the following statements about the Michaelis Menten constant (Km) is correct......A. can be determined by plotting the data v/[S] against 1/[S] B. A large Km indicates a low affinity between the enzyme and the substrate C. A large Km means that a large concentration of substrate is needed for the enzyme to work D. is a measure of the affinity of enzymes for proteins, minerals and vitamins E. Small Km means that a large concentration of substrate is needed for the enzyme to work