Q17: Substrate concentration, [S], has units of micromolar, µM.Enzyme velocity, Vo, has units of micromole per minute, (µmol/min).Using data from only the extremes of the [S] range is unreliable.Vmax; no inhibitor =Vmax; with inhibitor A =Vmax; with inhibitor B =μmol/minO noncompetitiveO competitiveO uncompetitiveµmol/minμmol/minSelect the type of inhibition displayed by inhibitor A.KM; no inhibitor =KM; with inhibitor A=KM; with inhibitor B =Select the type of inhibition displayed by inhibitor B.O uncompetitiveO competitiveOnoncompetitiveμΜμΜμM Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and KM ofthe enzyme with no inhibitor, with inhibitor A, and with inhibitor B.[S] (µm)351030901/V Slope = KM/VmaxIntercept = -1/KMVo (μmol/min); with noinhibitor10.414.522.533.8040.5Intercept = 1/Vmax1/[S]Vo (μmol/min); withinhibitor A4.16.411.322.633.8V (μmol/min); withinhibitor BSubstrate concentration, [S], has units of micromolar, µM.Enzyme velocity, Vo, has units of micromole per minute, (µmol/min).Using data from only the extremes of the [S] range is unreliable.2.12.94.56.88.1

For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…

Answered: Substrate concentration, [S], has units…

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

If 287.9 umol of enzyme X has a Vmax = 47.8 mmol/sec, what is the value of kcat %3D sec-1? Please report answer with 1 decimal place. Please do not report units. Your Answer: Answer units MacBook Air 888 F5 F4 F3 F2 %23 %24 %24
If a michaelis-type enzyme has an apparent Km of 2*10^-8 and apparent Vmax of 1*10^-4 moles/min in the presence of 1*10^-3 M uncompetitive inhibitor (Ki=1*10^-7 M), what is the true Km of the enzyme
Use the relationships revealed by a Lineweaver–Burk plot and the table of enzyme performance to calculate the ?max and ?M of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B. Substrate concentration, [S], has units of micromolar, μM. Enzyme velocity, ?0, has units of micromole per minute, (μmol/min). Using data from only the extremes of the [S] range is unreliable. Select the type of inhibition displayed by inhibitor A. competitive noncompetitive uncompetitive Select the type of inhibition displayed by inhibitor B. competitive noncompetitive uncompetitive
From your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.
Make a v vs. [S] plot for an enzyme that obeys Michaelis-Menten kinetics with a Vmax of 150 mM/min and Km of 1.5 mM.
7.1 The following results were obtained for an enzyme-catalysed reaction Substrate concentration (mmolr'): Initial velocity (umol I' min"): 6.67 182 10.0 20.0 40.0 147 233 323 400 Calculate Km and Vmax
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An enzyme catalyzes a reaction with a Km of 9.50 mM and a Vmax of 2.10 mM · s-1. Calculate the reaction velocity, vo, for each substrate concentration. [S] = 3.25 mM vo : mM · s-1 [S] = 9.50 mM mM · s-1 Vo :
Suppose that the data shown in the margin are obtained for an enzyme -catalyzed reaction. [S] (mM) V (mmol/ml min) 0.1 3.33 0.2 5.0 0.5 7.14 0.8 8.00 1.0 8.33 2.0 9.09 a.) Determine the Km and Vmaxb.) Assuming htat the enzyme present in the system had a concentration of 10-6M, calculate the turn -over number
If the data from an enzyme experiment is plotted as a Lineweaver-Burk plot, and the Vmax is 0.02 mol/sec, and x-intercept is –2.5 mM then what is the KM value? Show yourwork/reasoning.
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minute
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.

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