Km is: A. the concentration of an inhibitor needed to give 1/2 Vmax B. a measure...
Km is:
A. the concentration of an inhibitor needed to give 1/2 Vmax
B. a measure of the rate of product formation
C. related to the affinity of the enzyme for its substrate
D. a measure of the activation energy of the enzyme-catalyzed reaction
E. the velocity equal to one-half of the maximum velocity
Homework Answers
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Km is:
A. the concentration of an inhibitor needed to give 1/2 Vmax
B. a measure...
Please answer all of those questions 7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bo...
Please answer all of those questions
7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point where the enzyme is working at its maximum rate (Vmax/2), and amount of substrate needed to bind half of the active sites (Km). Label these points on the graph. Vmax represents: Vm Vmax/2 represents: Reaction velocity v Vmax 2 Km represents: Kim Substrate concentration (5)
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....
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When...
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When substrate concentration is 40 uM what is the initial reaction rate? b. An enzyme with a Vmax of 100 umol/minute and a Km of 10 uM was reacted with a irreversible active site specific inhibitor. After reaction with the inhibitor, the enzyme was assayed using a 2 mM concentration of substrate, and it gave a reaction rate of 20 umol/min. What percentage of the...
biochemistry if you could please help me answer the following questions! 741) (5 pts) Transition state theory relate...
biochemistry
if you could please help me answer the following questions!
741) (5 pts) Transition state theory relates the rate constant to the free energy of activation, AG. How can enzymes reduce the activation energy barrier? a) decrease the free energy of the product b) high affinity binding to the transition state c) increase the free energy of the substrate d) increase entropy upon release of product e) bind to the substrate with high affinity 2) (5 pts) Which is...
b. Look at the graph below of how a competitive inhibitor affects the kinetics of an...
b. Look at the graph below of how a competitive inhibitor affects the kinetics of an enzyme C. Rate of reaction is the Vmax of the enzyme affected? Why or why not: explain in terms of substrate concentration and enzyme active site saturation) Without inhibitor With competitive inhibitor d. is Vmax/2 affected? Why or why not: explain in terms of Vmax. Substrate concentration e. Is Km affected? Explain in terms of the active site. Hint a competitive inhibitor is competing...
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...
You have an inhibitor for an enzyme that you are studying. The concentration of inhibitor used is...
You have an inhibitor for an enzyme that you are studying. The concentration of inhibitor used is 5.50 µM. The following data was collected for the non-inhibited reaction as well as the reaction that was inhibited. mmol/(mL min) mmol/(mL min) mM Substrate Vo Substrate Vo + Inhibitor 0.200 5.000 3.751 0.400 7.500 4.998 0.800 10.000 5.995 1.000 10.700 6.173 2.000 12.500 6.807 4.000 13.600 7.143 a. Plot this data using Excel or a graphing program. Make sure you give your graph has a...
An uncompetitive inhibitor of an enzyme catalyzed reaction
biochemistryAn uncompetitive inhibitor of an enzyme catalyzed reaction a. binds to the ES complex b. is without effect at saturating substrate concentration. c. can actually increase reaction velocity in rare cases. d. decreases Vmax e. Binds to Es completx and lowers Vmax
Estimation of Vmax and K by Inspection Although graphical methods are available for accurate determination of...
Estimation of Vmax and K by Inspection Although graphical methods are available for accurate determination of the Vmax and K of an enzyme-catalyzed reaction (see Box 6-1), sometimes these quantities can be quickly estimated by inspecting values of Vat increasing (Sl. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained. V (pm/min) V (m/min) 112 [S] (M) 2.5 x 10 4.0 x 100 1 x 10-5 2 x 10-5 [S(M) 4 x 10-5...
Please answer all of those questions
7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point where the enzyme is working at its maximum rate (Vmax/2), and amount of substrate needed to bind half of the active sites (Km). Label these points on the graph. Vmax represents: Vm Vmax/2 represents: Reaction velocity v Vmax 2 Km represents: Kim Substrate concentration (5)
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....
biochemistry
if you could please help me answer the following questions!
741) (5 pts) Transition state theory relates the rate constant to the free energy of activation, AG. How can enzymes reduce the activation energy barrier? a) decrease the free energy of the product b) high affinity binding to the transition state c) increase the free energy of the substrate d) increase entropy upon release of product e) bind to the substrate with high affinity 2) (5 pts) Which is...
b. Look at the graph below of how a competitive inhibitor affects the kinetics of an enzyme C. Rate of reaction is the Vmax of the enzyme affected? Why or why not: explain in terms of substrate concentration and enzyme active site saturation) Without inhibitor With competitive inhibitor d. is Vmax/2 affected? Why or why not: explain in terms of Vmax. Substrate concentration e. Is Km affected? Explain in terms of the active site. Hint a competitive inhibitor is competing...
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...
Estimation of Vmax and K by Inspection Although graphical methods are available for accurate determination of the Vmax and K of an enzyme-catalyzed reaction (see Box 6-1), sometimes these quantities can be quickly estimated by inspecting values of Vat increasing (Sl. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained. V (pm/min) V (m/min) 112 [S] (M) 2.5 x 10 4.0 x 100 1 x 10-5 2 x 10-5 [S(M) 4 x 10-5...
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