1:335G. 46%Problem 12 of 15SubmitUsing the following reaction datapoints, construct a Lineweaver-Burkplot for an enzyme with and withoutan uncompetitive inhibitor bydragging the points to their relevantcoordinates on the graph and drawinga line of best fit.with 10 μg per mL inhibitor1-1s mMV'72<54454138Answer:||| 1:335G. 46%Problem 12 of 15SubmitUsing the following reaction datapoints, construct a Lineweaver-Burkplot for an enzyme with and withoutan uncompetitive inhibitor bydragging the points to their relevantcoordinates on the graph and drawinga line of best fit.1-1 1mM[S]'20V's mM¹ with 10 μg per541036>ст5272.5231.2520Answer:|||

The Lineweaver-Burk plot is a way to represent enzyme kinetics by plotting the reciprocal of the…

Answered: 1:33 5G. 46% Problem 12 of 15 Submit…

Biochemistry

9th Edition

ISBN:9781305961135

Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Chapter6: The Behavior Of Proteins: Enzymes

Section: Chapter Questions

Problem 60RE

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MATHEMATICAL The enzyme -methylaspartase catalyzes the deamination of -methylaspartate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]. The rate of the reaction was determined by monitoring the absorbance of the product at 240 nm(A240). From the data in the following table, determine KM for the reaction. How does the method of calculation differ from that in Questions 26 and 27?
MATHEMATICAL For the Vmax obtained in Question 26, calculate the turnover number (catalytic rate constant) assuming that 131024mol of enzyme were used.
The energy released by the hydrolysis of ATP is primarily stored between the alpha and beta phosphates equal to -57 kcal/mol harnessed as heat energy by the cell to perform work providing energy to coupled reactions
MATHEMATICAL You do an enzyme kinetic experiment and calculate a Vmax of 100 mol of product per minute. If each assay used 0.1 mL of an enzyme solution that had a concentration of 0.2 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol?
Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is â€” 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37Â°C.
MATHEMATICAL The kinetic data in the following table were obtained for the reaction of carbon dioxide and water to produce bicarbonate and hydrogen ion catalyzed by carbonic anhydrase: CO2+H2OHCO3+H+ [H. De Voe and G. B. Kistiakowsky, J. Am. Chem. Soc. 83, 274 (1961)]. From these data, determine KM and Vmax for the reaction. CarbonDioxideconcentration(mmolL1)1/Velocity(M1sec)1.252.55.020.00.25036103201031210361030.256
Which of the following analogies best describes the induced-fit model of enzyme-substrate binding? a hug between two people a key fitting into a lock a square peg fitting through the square bole and a round peg fitting through the round hole of a children’s toy the fitting together of two jigsaw puzzle pieces
MATHEMATICAL The free-energy change (G) for the oxidation of the cytochrome aa3 complex by molecular oxygen is 2102.3kJ=224.5kcal for each mole of electron pairs transferred. What is the maximum number of moles of ATP that could be produced in the process? How many moles of ATP are actually produced? What is the efficiency of the process, expressed as a percentage?
RECALL The accompanying figure is from an electrophoresis experiment using SDSPAGE. The left lane has the following standards: bovine serum albumin (MW 66,000), ovalbumin (MW 45,000), glyceraldehyde 3-phosphate dehydrogenase (MW 36,000), carbonic anhydrase (MW 24,000), and trypsinogen (MW 20,000). The right lane is an unknown. Calculate the MW of the unknown.
Nearly all organisms on Earth carry out some form of glycolysis. How does this fact support or not support the assertion that glycolysis is one of the oldest metabolic pathways?
Inhibition of Purine and Pyrimidine Metabolism by Pharmacological Agents Indicate which reactions of purine or pyrimidine metabolism are affected by the inhibitors (a) azaserine, (b) methotrexate, (c) sulfonamides, (d) allopurinol, and (e) 5-fluorouracil.
Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.

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