9. For the following aspartate reaction in the presence of inhibitor, Km = 0.00065 M. Determine Vmax in bothreactions and in the reaction without inhibitor, the Km. Identify whether the inhibition is competitive, non-competitiveor uncompetitive.1101001/V7060-40-30-20-10-10. For your answer in #9, explain briefly:a. 1. how / and S bind to the E as shown by the Lineweaver Burk plot.b. the significance of the following obtained values for Km and Vmax.c. effect in slope and x-interceptF000F0000Fo008F0009F000Fo00

Enzymes are biocatalyst that increases the speed of reaction by lowering the activation energy.…

Answered: 9. For the following aspartate reaction…

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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For the following aspartate reaction in the presence of inhibitor, Km = 0.00065 M. Determine Vmax in both reactions and in the reaction without inhibitor, the Km. Identify whether the inhibition is competitive, non-competitive or uncompetitive. ( see attached picture ) how I and S bind to the E as shown by the Lineweaver Burk plot. the significance of the following obtained values for Km and Vmax. effect in slope and x-intercept
The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). [S], M V w/o inhibitor, M/s V w/ inhibitor, M/s 1x10-4 0.0259 0.0098 5x10-4 0.0917 0.040 1.5x10-3 0.136 0.086 2.5x10-3 0.150 0.120 5x10-3 0.165 0.142 In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.
A particular enzyme-catalyzed reaction has an apparent Vmax = 9.00 nmol s-1 and α' = 3.00 when 2.00 µmol L-1 inhibitor X is present and uncompetitively inhibiting the reaction. Calculate Vmax for the uninhibited reaction in nmol s-1.
The KM values for the reaction of chymotrypsin with two different substrates are given in the table below. Considering this information, which substrate has the lower apparent affinity for the enzyme? Which substrate is likely to give a lower value for Vmax? Substrate N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester KM (M) 8.8 X 10-² 6.6 X 10-4 N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give a lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give the lower V₁ max. N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; N- acetyltyrosine ethyl ester is likely to give the lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; N- acetylvaline will likely to give the lower Vmax. None of the above statements are correct.
For the following aspartase reaction in the presence of the inhibitor hydroxymethylaspartate, determine Km and whether the inhibition is competitive or noncompetitive. You have to plot thegraph on the graph paper and also by using excel.[S] V, No Inhibitor V, Inhibitor Present(molarity) (arbitrary units) (same arbitrary units) 1 x 10-4 0.026 0.0105 x 10-4 0.092 0.0401.5 x 10-3 0.136 0.0862.5 x 10-3 0.150 0.1205 x 10-3 0.165 0.142
The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.
An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.
Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea
HOW TO SOLVE THIS IN EXCEL? For the following aspartate reaction in the presence of inhibitor, Km = 0.00065 M. Determine Vmax in both reactions and in the reaction without inhibitor, the Km. Identify whether the inhibition is competitive, non-competitive or uncompetitive. ( see attached picture ) Briefly explain: how I and S bind to the E as shown by the Lineweaver Burk plot. the significance of the following obtained values for Km and Vmax. effect in slope and x-intercept
22) answer the following question.. Refer to the kinetic scheme for competitive inhibition and the structures shown below to E+S ES E +P -co- CO- 1 2 EI Compound 1 was determined to act as a competitive inhibitor through standard inhibition studies. Structural studies did not show any resemblance to the transition state. Compound 2 was also determined to act as a competitive inhibitor. Structural studies showed that it does resemble the transition-state. The K, constant is used to assess relative affinity of inhibitors for enzymes. That is, each compound has its own K, value. We can interpret K, the same way we do with Ka values. True or False: K, > Kµ2. Briefly explain your answer.
The KMof the enzyme for the substrate adenosine is 3 × 10ꟷ5M. The product inosine acts as an inhibitor of the reaction, with an inhibition constant (KI, the dissociation constant for enzyme-inhibitor binding) of 3 × 10ꟷ4M. However, a transition state analog,Inhibits the reaction with KIof 1.5 × 10ꟷ13M. Explain why 1,6-dihydroinosine serves as a better inhibitor of adenosine deaminase than inosine. Elaborate on your answe
In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC Inhibitor XYZ Inhibitor PQR Without Inhibitor Vmax 40.2 mM/ sec 40.3 mM/ sec 12.32 mM/ sec 65.43 mM/ sec Km 24.3 mM 28.5 mM 24.3 mM 15.7 mM d. Draw the estimated Michaelis Menten Curve of Inhibitor ABC and the curve without the inhibitor.

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