6 3. The rates of a carbonic anhydrase catalyzed reaction of CO2 and H20, in the absence andpresence of an inhibitor (I), are measured and given below. The initial concentration of theenzyme carbonic anhydrase was 20 mM, and the initial concentration of the inhibitorconcentration was 6.0 mM. (Attach any necessary graphs)R. (M s)Ro (M s²)[S]. (M)No inhibitorWith Inhibitor1.00E-031.76E-061.17E-062.00E-032.50E-061.45E-065.00E-033.34E-061.70E-061.00E-023.77E-061.81E-062.00E-024.02E-061.86E-06a) Determine the mode of inhibitionb) Calculate the values of Km, Ki, Rmax, k2.

Carbonic anhydrases catalyze the interconversion between CO2 and H2O, maintain acid-base…

Answered: 3. The rates of a carbonic anhydrase…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter19: The Tricarboxylic Acid Cycle

Section: Chapter Questions

Problem 4P: Understanding the Mechanism of the -Ketoglutarate Dehydrogenase Reaction tshe first step of the...

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The equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)
6. If inhibitor X changes lactase activity to a Vo of 0.333333333333 mM per minute when [S] = 2.0 mM, and a Vo of 0.50 mM per minute when [S] = 3.33333333333 mM, calculate the new Vmax. 1.0 mM per minute 2.0 mM per minute 2.5 mM per minute 5.0 mM per minute 10.0 mM per minute 7. Calculate the new Km of the lactase reaction with inhibitor X. 1.0 mM 2.0 mM 2.5 mM 5.0 mM 10.0 mM 8. Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. 1.0 per minute 2.0 per minute 2.5 per minute 5.0 per minute 10.0 per minute Inhibitor X exerts which of the following effects on the above enzyme (lactase)? uncompetitive inhibition mixed noncompetitive inhibition competitive inhibition pure noncompetitive inhibition all of the above
1) How is the TCA cycle regulated? a) Draw the TCA diagram that fills in all possible regulation points.
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1.In a kinetics data set, in case a substrate concentration is given [S] in uM and inhibitor concentration [I] uM, initial velocity (Vo) in umol/min , Km , Vmax, apparent Km, apparent Vmax, and Ki, is there any way of finding Kcat ? 2.Which formula would be used in that case? What would the process be for finding Kcat?
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1. Bypass reaction in the anabolic pathway often occurs when A The ΔG of the reverse reaction in the catabolic pathway has a large negative value B The ΔG of the reverse reaction in the catabolic pathway has a large positive value C The ΔG of the reaction in the anabolic pathway is close to zero D The ΔG of the reaction in the anabolic pathway is positive E None of the above
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1 the concentration of the enzyme competition inhibitor was 1×10-3M. If 1 µmol of the inhibitor is present inthe 1 mL reaction mixture, Indicate how much the initial degree of hydrolysis decreases as a proportion(in thepresence of inhibitors/in the absence of inhibitors) with respect to the absence of inhibitors.
A researcher wants to look for glucaronic acid conjugated metabolites in sample of urine(glucaronic acid conjugation is a common method of metabolism for excretion.) Pronotated glucaronic acid conjugated metabolite ions often lose anhydroglucaronic acid(176 Da) during low energy CID. Which triple quadrupole experiment might be best for finding these conjugates?
Which of the following statements is true about the chymotrypsin reaction? 1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser 2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate. 3. During the reaction, LBHB forms when the proton is donated to His from Ser or water. 4. The chymotrypsin reaction involves “only” specific acid-base catalysis 5. The “oxyanion hole” is formed by the amide nitrogens of Ser and Glu

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