. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterialwall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzymeactivity if the temperature will rise up to 60 °C and pH will be changed to 8.0. Toanswer the question:a) draw the graph of the velocity dependency on temperature and pH;b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes theformation of 5 uM of the product per 2 minutes.ConcidorNH3:5.

Lysozyme is a naturally occurring enzyme found in bodily secretion such as- tears, saliva and milk.…

Answered: . The optimal conditions for salivary…

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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1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:
at what substrate concentration is v= 5.0 mM s^-1 for the enzyme catalyzed hydrolysis of trehalose?
5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the rates of reaction with glucopyranoside for various substrate concentrations was obtained. By constructing a Leaver-Burk plot, determine the value of the Michaelis constant. [S]/ (10-6 mol dm-3) v/ (10-3 mol dm-3 s-1) 1.00 2.00 3.00 4.00 16.7 33.3 41.1 49.8
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
Calculate the turnover number for an enzyme, assuming Vmax is 0.5 M.sec-1 and the concentration of the enzyme used is 0.002 M. Why is it useful to know this?
The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1
The equil ibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200.In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1.What is the rate constant for the loss of the unreacted substrate from the active site?
Sketch on one reaction rate vs. substrate concentration graph & sketch on one Lineweaver-Burk type plot the following:a) A Michaelis-Menten enzyme with a Vmax = 60 1/s and a KM = 125 M.b) An uncompetitive inhibitor of the enzyme described in a).c) An allosteric enzyme with the same Vmax as the enzyme described in a) and follows the sequential model
The initial rates of an enzyme-catalyzed reaction have been determined for five different [S] (see table below). [S]o (mol.L-¹) 1.0 x 10 1.5 x 10-4 2.0 x 10-4 -4 5.0 x 10 7.5 x 10-4 -1 Vo (μmol.L-¹ min-¹) 28 35 42 63 75 1- Determine graphically the value of Km (first with the Michaelis-Menten representation and then with the Lineweaver-Burk representation, then compare by reporting on the Michaelis-Menten representation the values found by the Lineweaver-Burk representation) 2- Calculate the concentration of a competitive inhibitor 1, with a K₁ value of 2.4.104 M, whose action would quadruple the apparent value of Km.
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…
Determine the values of KM and Vmax for the decar-boxylation of a β-keto acid given the following data. You have to plot the graph by using excel. Please include slope Substrate Concentration (mol L1) Velocity (mM min1)2.500 0.5881.000 0.5000.714 0.4170.526 0.3700.250 0.256
For an enzyme obeying the Michaelis-Menten equation with Km = 5 µM, kcat = 10 s-¹ and a total enzyme concentration of 1 nM, Calculate Vmax. Calculate the substrate concentration at which v = 0.1 Vmax Calculate the substrate concentration at which v = 0.9 Vmax What fraction of the enzyme is bound to substrate when v = 0.9 Vmax? Sketch a graph showing the Michaelis-Menten plot. Make sure you label the axes on your plot. Label on the graph: i) the point on the graph at which S=Km ii) Vmax At low substrate concentration, v = Keat [Etot] [S] Km Circle on your graph where this equation applies. What name is used to refer to keat/Km? : Calculate keat/Km for this enzyme. How does this value compare with the fastest enzymes?

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