EXPERIMENT 3: Why do enzymes react differently?DATA SHEETGiven the following standards and the corresponding standard curve table, what is theamount of substrate consumed given that 1.6 mM of substrate is prepared with anenzyme gave an absorbance of 0.345?0.40.81.21.6Substrate with enzymeConcentration (mM)Standard curve table:Varying Absorbance Absorbance AbsorbanceFinalInitialAcPComponentChangeDepletedumolmM540 nm540nm0.10.0370.0880.0290.07840.20.0740.0220.0520.14060.40.0740.0740.0860.1480.20000.60.2220.1360.23250.80.2960.2040.0920.24871.20.4440.3450.0990.26760.1040.1061.60.5920.7400.4880.28112.00.6340.2865

The enzymes are protein molecules that increase the rate of reactions by decreasing the activation…

Answered: Given the following standards and the…

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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pls explainWhy was absorbance measured at 420 nm in the enzyme kinetics experiment? To monitor thea. decrease in catechol concentrationb. increase in quinone concentrationc. decrease in polyphenol oxidase concentrationd. polyphenol oxidase-catechol complex concentrationLineweaver-Burk plot is the most used linearization method of the MichaelisMenten equation, but the main drawback is a/an:a. overemphasis to low substrate concentration and less emphasis to high substrate concentration.b. overemphasis to high substrate concentration and less emphasis to low substrate concentration.c. exaggeration to both ends of the reciprocal of the substrate concentration.d. lack of independent variables to x- and y- coordinates
Sample pH vs Initial Velocity (AA450/60 seconds) a bo16 0.0014 0.0012 o.001 0.0008 0.0006 0.0004 0 0002 pH Sample what does it mean? Does it agree with what we know about enzyme kinetics and why or why nol? If there were anomalies, what were they and what are some possible reasons for this occurring? Was an optimal pH identifiable? Why or why not? Initial Velocity (AA450/60seconds)
BIOCHEMISTRY QUESTION The initial rate (VO) data as a function of substrate concentration [S] for an enzyme (Enzyme1) that obeys Michaelis-Menten kinetics are shown in the table below. The total enzyme concentration is 2.5 nM. [S](μm) 16.0 8.0 4.0 2.0 1.0 v (μMsec ¹) 48.5 32.7 19.8 11.1 5.88 (a) Calculate KM for the enzyme, using the estimated slope (slope = (y2-y1)/(x2-x1)) from a Lineweaver-Burk plot. Show your work and don't forget the units! (b) When the enzyme concentration is 2.5 nM, a Lineweaver-Burk plot of this data gives a line with a y- intercept of 0.0106 μ M-1 sec. Calculate kcat for the enzyme. (Show your work and don't forget to include units). (c) A second enzyme (Enzyme2) also obeys Michaelis-Menten kinetics. Its kcat and KM are 800 sec-1 and 5 µM, respectively. Which is the more efficient enzyme? Briefly explain d) Is Enzyme 1 diffusion limited? Explain.
Exercise The following data describe an enzyme-catalyzed reaction. Plot these results using the Lineweaver-Burk method, and determine values for KM and Vinax- The symbol mM represents millimoles per liter; 1 mM = 1 × 10 3 mol L. (The concentration of the enzyme is the same in all experiments.) Velocity (mM sec-") Substrate Concentration (тм) 2.5 0.024 5.0 0.036 10.0 0.053 15.0 0.060 20.0 0.061 Ippt.com
Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
An enzyme catalyzes a reaction with a Km of 7.50 mM and a Vmax of 2.90 mM - s-1. Calculate the reaction velocity, un, for each substrate concentration. [S] = 2.75 mM mM · s- * TOOLS x10 [S] = 7.50 mM mM · s-! [S] = 11.0 mM mM - s-
Calculate the Km of the enzyme with these parameters. kcat = 130s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM
Chemistry Q4 1mL of the stock solution acetaminophen (1mg/mL) is used for the estimation of PC using n-octanol. After extraction, 0.1mL of the extracted solution was added to 0.9mL of water and 100uL of this solution was loaded in 96 well plate to the absorbance at 260nm. If the observed absorbance of the extraction phase is 0.2 using the following standard curve equation, Calculate the concentration of acetaminophen in aqueous Phase. Note: If you need the standard curve equation, please make It up because I want to understand the concept. Please explain in steps like how to approach the problem
Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…
Result nad Discussion Lead Acetate Reaction: Samples: lysine, cysteine, methionine Reagents: 10% Sodium Hydroxide (NaOH) and Lead Acetate Pb(CH3COO)2 -To 1 ml of the amino acid solution taken in a test tube, add few drops of sodium hydroxide (40%) and boil the contents for 5-10 mins over a bunsen burner. Cool the contents and add few drops of 10% Lead acetate solution and observe.
calculate the reaction velocity at saturating substrate concentrations. Your numerical answer is assumed to be in units of M sec-1. [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
Table below shows the kinetic data obtained for an enzyme in the absence of any inhibitor (1), and in the presence of an inhibitor (2), at a concentration of 7.0 mM. Assume the total enzyme concentration, [E]T, is the same for each experiment. Table 1 [S] (mM) Vo Vo {umol/(mL•s)} {umol/(mL•s)} Without Inhibitor With Inhibitor (1) 3.8 (2) 2.2 1 2 7.3 4.3 4 13.3 8.2 8 22.9 14.9 12 30.0 20.4 a); Construct a Lineweaver -Burk plot using the kinetic data shown in Table 1. Determine Vmax and Km for the uninhibited enzyme and inhibited enzyme.

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