Use the Michaelis-Menten plot to answer this question. What is the estimated value of Vmax ofthe enzyme catalyzed reaction (square data points)? (choose the one best answer)30 mM30 mm/sec60 mm/sec60 mMPage 20 of 36Previous PageNext Page Vo6050403020mm/sec0100 0O00 50 100 150 200 250 300Substrate (mM)Use the Michaelis-Menten plot to answer this question. What is the estimated value of Vmax ofthe enzyme catalyzed reaction (square data points)? (choose the one best answer)10

Vmax : Reaction rate- when the enzyme gets fully occupied by substrate. Vmax- Maximum velocity

Answered: Use the Michaelis-Menten plot to answer…

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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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
An enzyme that follows Michaelis-Menten kinetics has a KM value of 3.00 µM and a keat value of 181 s1. At an initial enzyme concentration of 0.0100 µM, the initial reaction velocity was found to be 1.07 x 10-0 µM/s. What was the initial concentration of the substrate, S, used in the reaction ? Express your answer in micromolar to three significant figures. > View Available Hint(s) ? [S] !! µM Submit
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphatase
An enzyme has a V of 1.2 uM s The Km for its substrate is 10 µM. max Calculate the initial reaction velocity, Vo, for each substrate concentration, [S]. Calculate Vo when [S] is 2 µM. Vo = µM s Calculate Vo when [S] is 10 µM. Vo = µM s-1 Calculate Vo when [S] is 30 µM. Vo = µM s-1
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the Vmax value for this reaction. Report your answer to four significant figures in units of uM/min.
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 table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis–Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect (no change, half as large doubles, increases, decreases) on the maximal velocity, Vmax, and Michaelis constant, KM, of the hypothetical enzyme.
L(24 points) Explain How is the Michaelis constant defined. and what does a low or high value for Km tell you? What is the difference between the velocity and initial velocity of an enzyme reaction? What determines the efficiency of an enzyme reaction, and what terms are used to describe it? 2. (50 points) About how to obtain kinetic data experimentally Lisa decides to obtain values for the Km and Vmax of an enzyme she has just isolated from liver cells (it is now pure), using a Michaelis Menten plot. Describe in detail what kinds of measurements she would have to make, and what she would need to plot on graphs in order to estimnte the values for Km and Vmax. (Show the kinds of graphs she would have to plot, and how these will allow her to estimate Km and Vmax.) Describe how she would be able to obtain Vmax experimentally and from the Michaelis Menten plot - what conditions are needed and what would be measured). Also, describe what she would have to do to obtain the turnover number of…
An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 μM and a kcat value of 206 s−1 . At an initial enzyme concentration of 0.0100 μM , the initial reaction velocity was found to be 1.07×10−6 μM/s . What was the initial concentration of the substrate, [S] , used in the reaction ? Express your answer in micromolar to three significant figures..
41 The following data describe an enzyme-catalyzed reaction (hydrolysis of carbobenzoxyglycyl-L-tryptophan) Plot these results using the Lineweaver-Burk method, and determine values for KM and Vmax Velocity (mM.sec-) 0 024 0 036 0 053 0 060 0 061 0 062 Substrate Concentration (mM) 25 50 10 0 15 0 200 25 0 42 If the KM of an enzyme for its substrate remains constant as the concentration of the inhibitor increases, what can be said about the mode of inhibition and why? 43 Calculate the turnover number for an enzyme, assumıng Vmax IS 05 M sec1 and the concentration of the enzyme used is 0 002 M Why is it useful to know this? 44 Dıscuss the mechanism of the Bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues Make use of relevant graphs and diagrams to explain your answer
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.

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Use the Michaelis-Menten plot to answer this question. What is the estimated value of Vmax of the enzyme catalyzed reaction (square data points)? (choose the one best answer) 30 mM 30 mm/sec 60 mm/sec 60 mM Previous Page Page 20 of 36 ha Next Page