### Enzyme Kinetics Problem Set#### Question #2The \( K_m \) of an enzyme is 5.0 mM.##### 2A. Calculate the substrate concentration when this enzyme operates at 10% of its maximum rate.*Answer: ______________*##### 2B. List the fraction of \( V_{max} \) that would be obtained when [S] (substrate concentration) = 0.1* \( K_m \), 0.5* \( K_m \), 2* \( K_m \), 10* \( K_m \).*Answer:- When [S] = 0.1 * \( K_m \) = ________- When [S] = 0.5 * \( K_m \) = ________- When [S] = 2 * \( K_m \) = ________- When [S] = 10 * \( K_m \) = ________*

Kinetics is the scientific discipline that studies reaction rates. Enzyme kinetics investigates the…

Answered: Question # 2 The Km of an enzyme is 5.0…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Question 1: When the CAC is run in reverse by microorganisms that use it to fix carbon, the citrate synthase reaction is different and is catalyzed by an enzyme called ATP-citrate lyase. Write the reaction catalyzed by ATP-citrate lyase, then briefly (in one sentence) explain why the use of different chemistry (different from the ‘normal’ direction) makes sense here.
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Question 31 True/False Question: Side chain of a serine residue in the active site of an enzyme can serve as a nucleophile during the catalysis. OTrue O False
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Question 2 of 13 Fill in the blanks: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, Mif both statements are incorrect. A. The dissociation of the ES complex to the product is more energetically favored than its dissociation into the separate enzyme and substrate. B. The rate determining step in enzymatic catalysis is the binding of the substrate to the active site of the enzyme.
QUESTION 2 What TYPE of inhibition is observed in the following plot: 1/v₂ Intersect at Y axis 1/Km Competitive Non-competitive Uncompetitive Allosteric 1/V, max 1/[S]
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QUESTION 20 Which enzyme (Enzyme 1, circle; Enzyme 2 square) has the best affinity for the substrate? 5.0 4.0 3.0 EnzGraph 8 2.0 1.0 0.0 10 15 20 25 30 35 40 45 50 substrate (mM) Enz1 Enz2 A. both have the same affinity B. Enzyme 2 (squares) C. cannot tell with information given D. Enzyme 1 (circles)
Question 1 a. What enzyme works on glucose-6-P when the energy charge is 0.80? b. What enzyme works on glucose-6-P when the energy charge is 0.97? c. What enzyme works on glycogen when the energy charge is 0.80?d. d. What enzyme works on glycogen when the energy charge is 0.97? e. What enzyme works on pyruvate when the energy charge is 0.80 (assume high O2)? f. What enzyme works on pyruvate when the energy charge is 0.97?
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Question # 2 The Km of an enzyme is 5.0 mM. 2A Calculate the substrate concentration when this enzyme operates at 10% of its maximum rate. 2B List the fraction of Vmax that would be obtained when [S] (substrate concentration) = 0.1*Km, 0.5*Km, 2*Km, 10*Km

Question # 2 The Km of an enzyme is 5.0 mM. 2A Calculate the substrate concentration when this enzyme operates at 10% of its maximum rate. 2B List the fraction of Vmax that would be obtained when [S] (substrate concentration) = 0.1Km, 0.5Km, 2Km, 10Km