Substrate Concentration (mol L1) Velocity (mM min-1) 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256 Determine the values of Km and Vmax for the decarboxylation of a 훃-keto acid given the following data. You have to plot the graph by using excel and please include the scope of graph
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Substrate Concentration (mol L1) |
Velocity (mM min-1) |
2.500 |
0.588 |
1.000 |
0.500 |
0.714 |
0.417 |
0.526 |
0.370 |
0.250 |
0.256 |
Determine the values of Km and Vmax for the decarboxylation of a 훃-keto acid given the following
data. You have to plot the graph by using excel and please include the scope of graph
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- 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 0.256Determine the values of Km and Vmax for the decarboxylation of β-keto acid given the following data. Please show and label your plot. Show your calculations and box your final [S] in mol/l V in mM/ min 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256Determine the values of KM and Vmax for the decar-boxylation of a β-keto acid given the following data. Substrate Concentration (mol L1) Velocity (mM min1)2.500 0.5881.000 0.5000.714 0.4170.526 0.3700.250 0.256
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- A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 m mol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM?Calculate the boiling points of a 8.50 m aqueous solution of fructose. Boiling point constants can be found in the list of constant. Tb= In CelsiusUtilising 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 that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10 µmol⋅min−110 µmol⋅min−1 when the substrate concentration is five times greater than the ?M.KM. What is the ?maxVmax of this enzyme?Calculate the equilibrium concentration of H2O for the following esterification reaction performed in ethanol(C2H5OH) C2H5OH + CH3CO2H ⇌CH3CO2C2H5 + H2O KC= 4.0 At equilibrium: [CH3CO2H] = 0.75 M; [CH3CO2C2H5 ]= 2.2 M1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062