5. Examine the graphic below and answer the questions about the enzyme we reviewed in lecture. 1.0 0.01 mM Vo АТР Vmax 1 mM ATP 0.5 1 mM ATP + 0.1 mM AMP 1 [Fru-6-P] (mM) 2 A) What enzyme is this? What reaction does it perform? Of what metabolic pathway is this enzyme a part? B) What allosteric regulator, shown on the graph as presented here, is considered to be a homotropic allosteric factor? C) Which allosteric regulator, shown on the graph as presented here, has the greatest influence on this enzyme? Explain the reasoning behind your answer. D) Name a positive allosteric effector of this enzyme NOT shown on the graph as presented here. What is the origin of this positive allosteric effector..that is, where is it coming from? E) Name a negative allosteric effector of this enzyme NOT shown on the graph as presented here. What is the origin of this negative allosteric effector,..that is, where is it coming from? F) Explain how the regulation of this enzyme is tied to the "energy state" of the cell.

Sample pH vs Initial Velocity (AA450/60 seconds) a bo16 0.0014 0.0012 o.001 0.0008 0.0006 0.0004 0 0002 pH Sample what does it mean? Does it agree with what we know about enzyme kinetics and why or why nol? If there were anomalies, what were they and what are some possible reasons for this occurring? Was an optimal pH identifiable? Why or why not? Initial Velocity (AA450/60seconds)

Assume that in a certain cell, the ratio of products/reactants or Keg = 809.5 (Keq is dimensionless) for the reaction Glucose + 2ATP > Glucose-1,6-diP + 2ADP, at a particular instant, the concentrations of each compound were Glucose =2.4M, ATP =11.1M, ADP -12.8M and G-6-P -28.4M. Calculate the difference (dimensionless) between Keq and the ratio of products/ractants at this instance, in this cell, to five decimal places

Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the catalytic efficiency for this reaction. Report your answer in scientific notation to three significant figures in units of M-1s-1.

Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vma) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 [S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide. Sketch a graph of V versus [S] showing curves in the absence of an inhibitor and in the presence of the types of inhibitors not shown by acetazolamide. ("AJO %) A

8 7- 6 2- 180 225 270 315 [Substrate] (nM) 45 90 135 360 405 450 495 540 58! What is the KM of the enzyme data shown above? rate (nM/sec) 3.

Please answer this question and the highlighted question is wrong please explain why and give me the correct answer

Please handraw this graph with all the necessary detailed information:   Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.

Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.

=display&toolld3calendar-mybb, Gmail YouTube Maps calendar-tool Home Courses C A Question Completion Status: 20 3D 70 100| 11凸|12D|| 130 14 150 16 170 QUESTION 14 A newly isolated bacterial isocitrate dehydrogenase is found to have a molecular mass of 180KDA and SDS-PAGE shows it to be a homodimer. 1mg of enzyme produces 0.05 mmoles of product per minute per mL. What is the turnover number of this enzyme in µmol product produced per pmol of enzyme subunit per mL? O a. 4.5 Ob.4500 O c. 9000 O d.9 QUESTION 15 The absorption spectrum of NAD" and its reduced form NADH are shown below: Absorption 2,4 2,0 1,6 Click Save and Submit to save and submit. Click Save All Answers to save all answers. Save All Ar 8 11 JAN 9. tv W ... LO