1. A Lineweaver-Burk Plot is shown below.3025Curve Ay = 3.1207x + 2.49782015Curve By = 1.0003x + 2.3602105-3157111/[Catechol] (mM1)With these curves, determine the following enzyme parameters. Show all pertinent solutions.a. Km of Curve A and Curve Bb. Vmax of Curve A and Curve Bc. Assuming that one of these curves corresponds to the kinetics of one enzyme and one substrate, which curverepresents the effect of an inhibitor? Why do you say so?d. What type of inhibition is exhibited by your answer in question c? Why do you say so?1/V, (units of activity 1)

Lineweaver-Burk plot is a graphical representation used in enzymology. It can be used in the absence…

Answered: A Lineweaver-Burk Plot is shown below.…

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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A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).
If the enzyme lactase has a Vo of 0.40 mM per minute when [S] = 1.25 mM, and a Vo of 1.0 mM per minute when [S] = 5.0 mM, what is its Vmax? Calculate the Km of the above enzyme. Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the above enzyme.
Various concentrations of recombinant human insulin were prepared for use standards for an HPLC method. To verify the prepared concentrations, the samples were analyzed by measuring the absorbance at 280 nm in a short path length (5 mm) cuvette. The molar absorption coefficient for human insulin is approximately 5.875 x 10³ M-¹cm-¹. a. Calculate the extinction coefficient in mL mg-¹cm-¹. b. Calculate the concentrations of the following human insulin standards if the measured absorbances and dilutions used are: Standard 1 Standard 2 Abs. (at 280 nm) of Diluted Sample 0.305 0.685 Dilution 145.0 µL sample, 25.0 μL buffer 130.0 µL sample, 40.0 μL buffer
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
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the above enzyme (lactase). (enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM) 0.125 per minute 0.25 per minute 0.50 per minute 1.25 per minute 5.0 per minute
How many net molecules of nucleoside triphosphate (ATP and equivalent molecules) are produced by complete aerobic catabolism of a glucose going through glycolysis, the pyruvate dehydrogenase complex and the citric acid cycle (TCA cycle)? Do not count the ATP eventually generated by re-oxidation of reduced coenzymes, just the number of NTPs produced in reactions of these pathways. Choose the one best answer. 02 03 04 05 06 8
A solution of [U 14C] glucose-1-phosphate (specific activity = 16,000 cpm/mmole) was incubated with glycogen and glycogen phosphorylase, an enzyme which adds glucose units on to glycogen. Radioactivity was incorporated into the glycogen primer at a rate = 2550 cpm/min. The rate of the enzymatic reaction in units of mmole glucose incorporated per minute is: (a) 0.016 mmol/min (b) 0.57 mmol/min (c) 0.16 mmol/min (d) 5.7 mmol/min
The Lineweaver-Burke plot was originally developed in order to "linearize" the data obtained from enzyme kinetics experiments, in order to facilitate the determination of kinetic parameters. Why is it not considered to be an accurate method for this purpose? It is very difficult to draw a straight line on a computer. It is very difficult to calculate the variables required for the "x" and "y" axis. It is more accurate to use the standard "V versus [S]" plot to determine Vmax and KM- The plot weights the least accurate data points the most heavily. It is no longer considered to be acceptable to extrapolate from known data.
8L.3.4
The table contains data about how different ASFV mutants affect enzyme activity-- for example the D29A mutant, where the D at position 29 was mutated to an A. Select three mutants at random, and for each mutant explain how that mutation could affect intermolecular force interactions (an example: hydrogen bonding could be disrupted by this mutation because…
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.
The hexapeptide Ala-Met-Leu-Lys-Phe-Asp is digested in the same tube with both Cyanogen Bromide and Trypsin at the same time at pH=7. Draw the structure of the product(s) that would bind to a cation exchange column. (Relevant pKa values are 2.2, 3.9, 9.5 and 10.5. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.5 and 2.2 respectively)

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