V2 1. To the right is a Michaelis-Menten plot for a wildtype enzyme (SECS)and three different mutants. The substrate is OAS. The mutantshave a methionine (M) changed to alanine (A)-three differentmethionine resudes were mutated.A12090a. What is the KM for StM92A?b. What is the Vmax for StM92A?c. Which enzyme has the highest kar?.e SICSO SIM92AE SIM96Aa SEM120A6030d. What is the Vmax for StCS?.(OAS) (mM)e. What is the KM for StM92A?,f. Is StCs or STM92A more efficient?(show your work below)t ed bilueb2. Shown below is a reaction catalyzed by "HA".a. What amino acid could serve as the "HA" in this reaction? Why did you choose this amino acid?b. Draw the energy diagram for the catalyzed and uncatalyzed reaction for this enzyme (assume there isonly this one step to this reaction).HAActivity Mal min)

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Answered: To the right is a Michaelis-Menten plot…

Introductory Chemistry: A Foundation

9th Edition

ISBN:9781337399425

Author:Steven S. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Donald J. DeCoste

Chapter21: Biochemistry

Section: Chapter Questions

Problem 28QAP: . Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate...

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Similar questions

. Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate important in this model? What does it mean to say that an enzyme is inhibited by a particular molecule? What happens if this inhibition is irreversible? Can you think of a situation in which it might be advantageous to be able to inhibit an enzyme?
In the multienzyme sequence shown below, molecules of D are able to fit to the enzyme E1 and prevent the conversion of A to B. What is this action of E called? AE1BE2CE3D a. effector inhibition b. allosteric inhibition c. feedback inhibition d. competitive inhibition by nonproduct
How can the Michaelis constant (Km) be identified and used to represent the affinity between the enzyme and the substrate?
How can distance validate non-covalent interactions? Also, please explain if the distance between c-alpha of a particular residue in an enzyme and c-alpha of its ligand are 12.4 Å, 11.7 Å, 6.5 Å, 7.6 Å, and 7.7 Å, what does that mean? What is the meaningful distance, what is the legth of hydrophobic,hydrophilic, h-bond...?
How does the near attack conformation (NAC) contribute to enzyme function?
Calculate the specificity constant for an enzyme-catalyzed reaction if the total enzyme concentration is 15 nM, Vmax is 9 M/s, and Km is 150 M. A. Has the enzyme achieved catalytic perfection? (Y or N)
An enzyme whose KM is 10-4 M in the presence of a substrate concentration of 10-2 M It is capable of transforming 20% of the substrate in 10 minutes. Calculate how much substrate is had transformed in 20 minutes.
An enzyme catalyzes the reaction M ⇌ N. The enzyme is present at a concentration of 1 nM, and the Vmax is 2 μM s−1. The Km for substrate M is 4 μM. (a) Calculate kcat. (b) What values of Vmax and Km would be observedin the presence of sufficient amounts of an uncompetitive inhibitor to generate an α′ of 2.0?
If we made a Lineweaver-Burk plot of an irreversible inhibitor, which type of reversible inhibition would it be most likely to resemble?
3) The enzyme aldolase catalyzes the conversion of fructose-1,6-diphosphate (FDP)to dihydroxyacetone phosphate (DHAP) and glyceraldehide-3-phosphate (G3P). Thereaction isFDP ⇄ DHAP + G3P , ∆rG0(298.15 K) = 23.8 kJ mol−1In red blood cells the concentration of these species are [FDP] = 35 µM, [DHAP] =130 µM, and [G3P] = 15 µM. (Remember that 1.0 µM = 1.0 × 10−6 mol L−1. Thestandard state for reactions in solution can be taken as c0 = 1.0 mol L−1).Calculate ∆rG in a red blood cell at 25 0C. Will the reaction occur spontaneouslyin the cell at this temperature?
4. The amino acid Asp189 lies at the base of the substrate specificity pocket in the enzyme trypsin. a. How is this related to typsin’s substrate specificity? Briefly describe the interactions between the substrate and the Asp 189. b. If the Asp189 was replaced with a lysine residue, how would this affect substrate specificity? c. The scientists that actually mutated the Asp189 to a lysine analyzed the three-dimensional structure of the enzyme and found that the lysine is actually not located in the specificity pocket. Instead, the Lys side chain reaches out of the base of the pocket, rendering the pocket nonpolar. With this additional information, determine how the substrate specificity would differ in the lysine-mutated enzyme.
From the given activity, 1.) What is the effect of temperature to the enzyme? 2.) What are some generalizations and conclusions in this activity?

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