7.,For the enzyme reaction mechanism with an inhibitor that produces product from both ES and EIS,E+S1→ ES -2➜ E+ PE+1+3 → ElEl +S4→ EIS -5→ El + Pwith reaction rate constants of k₁ and k-1 (and so on) for each of the reactions:A. Write the enzyme balanceB. Write each of the equations that result from applying the quasi steady state assumption.C. Write each of the equations that result from applying the rapid equilibrium assumption.D. Based on the mechanism, what type of inhibitor is this? (competitive, uncompetitive or non-competitive)Why?

Enzymes are proteins that act as catalysts to speed up biochemical reactions in living organisms.…

Answered: For the enzyme reaction mechanism with…

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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Consider an enzyme that catalyzes the reaction S2 P, by the following simple reaction mechanism: k, E + S 2 E•S →E kcat + P Suppose the enzyme acquires a mutation that causes k1 to be 10-times smaller than for the wild-type (non-mutant) enzyme. Suppose you measure the initial reaction rate (vo) at several different [S] for the mutant and the wild-type enzymes. Under what conditions would the mutation have a greater effect on the reaction rate (vo) of the mutant enzyme compared to the wild-type enzyme - at very low [S], or at very high [S]? Explain briefly how you decided.
An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each substrate concentration. [S] = 1.75 mM MM-s-1 [S] = 7.50 mM [S] = 11.0 mM DO mM-s mM-s
The reaction: A + B <-> P + Q is catalysed by enzyme E. Draw a Cleland diagram for a Non-sequential (Ping-Pong) mechanism for this reaction.
Derive an Equation that explains the realtionship between kE and kN with respect to the equilibrium constants provided in the reaction scheme provided below. Assume that the enzyme must bind with A before it binds with B. The two reactions are related by the following reaction scheme:provided below.
Question 23 An enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation... SHOW MORE V The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d. The V for X will be affected if Y is present in the reaction mixture. max pH dependence of Vmax reflects the ionization state of catalytic site e residues. Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X = 0.01 M and the Km for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of g products to reactants (Keg).
Following is a Dixon plot for PNPP inhibition by inorganic phosphates. What answer choice shows the correct combination of the mode of inhibition and Ki of the EI complex? - Mixed inhibition, Ki= -21.2 uM - Mixed inhibition, Ki= 1/16.5 uM - Competitive inhibition, Ki= 16.5 uM - Competitive inhibition , Ki= -1/16.5 uM - None of the above
(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. The enzyme activity data are shown in the table below. Construct a [substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90
You begin to study enzyme Z, which catalyzes a simple reversible reaction that interconverts compound S and compound P. You observe that the ∆G´° for the S to P conversion to be –6 kJ/mol, and that compound S has ∆G´° for binding to enzyme Z of –15 kJ/mol, while compound P has a ∆G´° for binding to enzyme Z of –13 kJ/mol. Please explain the effect of enzyme Z on conversion of S to P. (Your answer should include a graph qualitatively showing energy versus reaction progress; however, you still need to explain youranswer in words!) not sure how to make the correct graph.
Most of the enzyme reactions followed the mathematical kinetic plots suggested by the Michaelis-Menten plots:viii. Draw another Lineweaver-Burk plot and on the same plot, draw a graphto indicate un-competitive inhibition.Note: In the graphs, lable Vmax and KM clearly.
A particular reaction has a ΔG‡ of 30.0 kJ mol-1 at 25.0 °C. In the presence of an enzyme, the same reaction has a ΔG‡ of 1.50 kJ mol-1 at the same temperature. Calculate the rate enhancement of this enzyme. (R = 8.3145 J mol-1 K-1)
Using the appropriate graph and table above, explain what the R48C mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.
a particular enzyme catalyzes a single reactant S to a single product P, following michaelis-menten kinetics rp=(VmaxCs) / (Km + Cs) 1. A reaction with this enzyme is carried out at very low substrate concentrations. Draw and label a curve on the plot that describes the reaction kinetics under those conditions.

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