The rate constants of an enzyme-catalyzed reaction, obeying the Michaelis-Mentenkinetics, have been determined :E + SK₁ = 2 x 108 M-¹ S-¹-1-1-1K-₁= 1 x 10³ SK₂ = 5 x 10³ S-1K₁1K-1ESK₂E +P1- Determine the Michaelis constant Km of the enzyme.2- Determine the catalytic constant (kcat) of the enzyme.3- Determine the catalytic efficiency of the enzyme.

The enzyme interacts with the substrate by attaching to its active site to produce the…

Answered: The rate constants of an…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter25: Nitrogen Acquisition And Amino Acid Metabolism

Section: Chapter Questions

Problem 22P

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Similar questions

Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
b. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Denote the point in the pathway in which each individual is blocked.
a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.
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.
Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.
Allosteric Regulation of Ribonucleotide Reductase by ATP and Deoxynucleotides Describe the underlying rationale for the regulatory effects exerted on ribonucleotide reductase by ATP, dATP, dTTP, and dGTP.
The Energy Cost of dTTP Synthesis (Integrates with Chapter 20.) Starting from HCO3, glutamine, aspartate, and ribosc-5-P, how many ATP equivalents are consumed in the synthesis of dTTP in a eukaryotic cell, assuming dihydroorotate oxidation is coupled to oxidative phosphorylation? How does this result compare with the ATP costs of purine nucleotide biosynthesis calculated in problem 2?
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?
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
Understanding the Mechanism of Hemolytic Anemia Genetic defects in glycolytic enzymes can have serious consequences for humans For example, defects in the gene for pyruvate kinase can result in a condition known as hemolytic anemia. Consult a reference to learn about hemolytic anemia, and discuss why such genetic defects lead to this condition.
Is aerobic respiration more or less efficient than glycolysis? Explain your answer.
Do you think that the Ea for ATP hydrolysis is relatively low or high? Explain your reasoning.

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