Experiment #1:The Effect ofConcentration onReaction RateNumber ofDrops ofEnzyme246Reaction Rate(kPa/min)0.270.731.29Experiment #2:The Effect of pH onReaction RatepH ofSolution4710Reaction Rate(kPa/min)0.360.970.89Experiment #3:The Effect ofTemperature onReaction RateTemperature10°C35°C55°CReaction Rate18. Predict what would happen if you added 20 drops of enzyme to the test tube.(kPa/min)0.581.430.3617. What type of relationship exists between substrate concentration and reaction rate? Couldyou explain why you think this relationship exists?

During a biochemical reaction, substrate molecules get converted into product according to the…

Answered: Experiment #1: The Effect of…

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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Similar questions

Suppose you were running out of substrate (PNPP) and decided to reduce the concentration used in your reactions (25 µM, 50 µM, 100 µM, 200 µM, 300 µM) by a factor of 100. How might this affect your kinetic analysis?
From the chart below, comment on the temperature dependence of this enzyme catalyzed reaction.
Using the table below can you please help me answer the following. Based on your results, what can you conclude about the effect of enzyme concentration on reaction rate? Explain
What are the answers in number 4,5,6?
You run a series of assays at 25°C on enzyme A. You measure the velocity for a range of S concentrations. What is the Km (in mM) for Enzyme A?
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
Explain how the observation that reaction (B) runs faster than reaction (A) is related to the enzyme catalysis.
As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG°) of ATP = -31 kJ/mol; RT = 2,58 kJ/mol) Select one: O a. -28 kJ/mol O b. -33 kJ/mol OC. -19 kJ/mol O d. -42 kJ/mol
What would be the turnover number and specific activity of an enzyme (molecular weight=32,000 D) in a reaction. (Vmax= 4 μmol of substrate reacted/min), with enzyme amount = 2 μg
1. A reaction in which a substrate is converted to a product is catalyzed by an enzyme. The reaction was determined to have ket = 10,000. s', KM = 90.0 µM, and a standard Gibbs free energy change of -13.8 kJ mol. Answer the following questions about experiments performed with 2.00 nM enzyme. R= 8.3145 J mol K. !3! a) Calculate the change in free energy for this reaction at room temperature (25.0°C) under the following conditions, and indicate whether the forward reaction is favored or not. i. [(S] = 2.00 µM and [P] = 2.00 nM. !! it. [S] = 2.00 uM and (P) = 2.00 uM.
Why is it important to know the Km and Vmax values of an enzyme?
Answer #2

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