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Determine the value of the turnover number of the enzyme catalase, given that Rmax (Vmax) for...
help with these please The turnover number is defined as the maximum number of substrate molecules...
help with these please
The turnover number is defined as the maximum number of substrate molecules that can be converted into product molecules per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily equal to the concentration of enzyme molecules, because some enzyme molecules have more than one active site. If the enzyme molecule has one active site, the turnover number is given by turnover number = - -=k2 (Rmax is often written as...
Catalase (MW250,000Da) has one of the highest turnover numbers we know of. It catalyzes the decomposition...
Catalase (MW250,000Da) has one of the highest turnover numbers we know of. It catalyzes the decomposition of hydrogen peroxide as shown in the reaction (2H2O2à2H2O + O2) If 15.0 mg of pure catalasecatalyzes the decomposition of 0.40 g of H2O2in 1 min at 37 °C at its Vmax, what is the turnover number (kcat) of catalase(in units of sec-1)? Plot a graph of Abs vs. time at different concentrations of enzyme and replot a figure and find out the optimal...
The maximum catalytic rate of an enzyme is defined as the turnover number (also called kcat)and...
The maximum catalytic rate of an enzyme is defined as the turnover number (also called kcat)and is the maximum number of reactions a single active site can carry out per second for a given concentration of enzyme. i.Would a competitive inhibitor reduce the turnover number for an enzyme?Why? ii.Would an irreversible inhibitor reduce the turnover number for an enzyme?Why?
41. You want to determine the initial velocity (Vo) of an enzyme, which has a Vmax...
41. You want to determine the initial velocity (Vo) of an enzyme, which has a Vmax of 0.3??/s and you are using an enzyme concentration of 50mM. The concentration of substrate in the reaction is 8 times greater than the Km. Which value below is the correct initial velocity A. 0.09 HM/s B. 0.27 ??/s C. 0.04 HM/s D. 1??/s E. 0.7 ??/s
Calculate turnover number if Vmax = 0.681 mMmin-1 assuming that 1 x 10^-4 mol of enzyme...
Calculate turnover number if Vmax = 0.681 mMmin-1 assuming that 1 x 10^-4 mol of enzyme was used The book says the answer is 20.43, but I got 1.61. I used Vmax/Km (Km=0.421), but evidently that's wrong. Any help would be great! Thank you!
Vmax II. Enzyme Kinetics 1. Vocabulary - match the term on the left with the definition...
Vmax II. Enzyme Kinetics 1. Vocabulary - match the term on the left with the definition on the right (each used only once) keat a. Concentration of inhibitor where the velocity is the maximum under a given set of conditions. Allostery b. Changes in active site properties through ligand binding to another site. K c. Rate of an enzyme reaction under a given set of conditions. Hill coefficent d. Maximum rate for an enzyme under a given set of conditions....
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a...
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a series of assays where you measured the rate of reactions as you varied the concentration of substrate in each assay (Table A). Estimate from a Michaelis-Menten plot approximate values for Vmax, KM, Kcat, and the specificity constant for this enzyme and substrate. (The only information that is given is this paragraph and the table below). Table 1: [S] (μM) v (μmol/L/min) 0 0 5...
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number...
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below: 5 27 23 65 1. Estimate V and K from a Michaelis-Menten graph of V versus [S] 2. Use a Lineweaver-Burk plot to analyze the same data. a. Determine V and Ka from the Lineweaver-Burk BONUS: If the total enzyme concentration was I nmol/L, what is K?
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction...
Need help with number 13! I already asked about number 12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the...
Need help with number 13! I already asked about number
12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
help with these please
The turnover number is defined as the maximum number of substrate molecules that can be converted into product molecules per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily equal to the concentration of enzyme molecules, because some enzyme molecules have more than one active site. If the enzyme molecule has one active site, the turnover number is given by turnover number = - -=k2 (Rmax is often written as...
41. You want to determine the initial velocity (Vo) of an enzyme, which has a Vmax of 0.3??/s and you are using an enzyme concentration of 50mM. The concentration of substrate in the reaction is 8 times greater than the Km. Which value below is the correct initial velocity A. 0.09 HM/s B. 0.27 ??/s C. 0.04 HM/s D. 1??/s E. 0.7 ??/s
Vmax II. Enzyme Kinetics 1. Vocabulary - match the term on the left with the definition on the right (each used only once) keat a. Concentration of inhibitor where the velocity is the maximum under a given set of conditions. Allostery b. Changes in active site properties through ligand binding to another site. K c. Rate of an enzyme reaction under a given set of conditions. Hill coefficent d. Maximum rate for an enzyme under a given set of conditions....
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below: 5 27 23 65 1. Estimate V and K from a Michaelis-Menten graph of V versus [S] 2. Use a Lineweaver-Burk plot to analyze the same data. a. Determine V and Ka from the Lineweaver-Burk BONUS: If the total enzyme concentration was I nmol/L, what is K?
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction...
Need help with number 13! I already asked about number
12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
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