Homework Answers
Question 7.
E + S represents just the addition of the enzyme to the substrate.
E.S represents the formation of the enzyme-substrate complex.
From the graph, E + S lies at low energy, whereas E . S lies at high energy, hence E + S is more stable than E . S
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questions 7-11
emists, E + S and E. S have very specific meanings. Describe the differences...
13. Suppose a second enzyme binds the substrate even more tightly than the enzyme shown in model 1 (the ES complex...
13. Suppose a second enzyme binds the substrate even more tightly than the enzyme shown in model 1 (the ES complex is more stable than the one shown in graph B). Draw this new E.S complex on graph B. What happens to the magnitude of the activation energy, AGact? 14. Suppose a third enzyme binds the transition state even more tightly than the enzyme diagramed Model 2. What happens to the magnitude of the activation energy, AGact? Model 2 Generalized...
Rodrigo is an enzyme engineer. He wants to know which of four peptide substrates is bound...
Rodrigo is an enzyme engineer. He wants to know which of four peptide substrates is bound most tightly by his engineered enzyme. Which value should he measure and pay attention to? Km KCAT Vo Both A and B kcat, [S], and [E]t Rodrigo's enzyme was assayed with three substrates (A, B, and C). The SAME enzyme concentration used was for each of the three reactions. The results of the three experiments are plotted as Lineweaver-Burke plots below. Considering what you...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much of their three dimensional shape is the result of interactions between the R (variable) groups of their amino acids. The active site is the portion of the enzyme that will interact with the substrate the molecule that the enzyme acts upon. The nature and arrangement of amino acids in the active site make each enzyme specific to a substrate and to the reaction it...
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as...
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as a function of substrate concentration; label both axes. Write the associated Michaelis-Menton equation and show the location of Km and Vmax on your graph. b. Draw a second graph showing the classic Lineweaver-Burk plot; label both axes. Show the location of Km and Vmax on your graph. Discuss which plot is the most useful to determine Vmax. Draw a second line on each graph...
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...
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate (V0) for...
The Michaelis-Menten equation models the hyperbolic relationship
between [S] and the initial reaction rate (V0) for an enzyme
catalyzed, single substrate reaction: E S ES E P. The model can be
more readily understood when comparing three conditions: [S]Km.
Match each statement with the condition that it describes. Note:
\"Rate\" refers to initial velocity (V0) where steady state
conditions are assumed; [Etotal] refers to the total enzyme
concentration, and [Efree] refers to the concentration of free
enzyme.
categories: [S]<<Km, [S]=Km,...
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...
Model 2 -Amylase Re UI RECLUTT Rate of reaction 0 20 80 100 40 60 Temperature,...
Model 2 -Amylase Re UI RECLUTT Rate of reaction 0 20 80 100 40 60 Temperature, C S trate concentration always in exce) Sub s e concentration Enzyme concentration constant) 12. Amylase is an enzyme that catalyzes the digestion of carbohydrates. The graphs in Model 2 pro- vide data on several factors that affect the function of amylase in the body 4. The relationship of which two variables is illustrated in graph A of Model 2 The relationship of which...
biochemistry if you could please help me answer the following questions! * 1. (5 pts) Which...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
I answered E but I cannot figure out part F? Using your value from the previous...
I answered E but I cannot figure out part F?
Using your value from the previous question, determine how many
H bonds or dipole interactions would be required to achieve a rate
enhancement of 10^6.
Part E A rate enhancement of 100 requires that the enzyme bind its transition state complex with higher affinity than its substrate. Using the Arrhenius equation, shown before this part, find AAGEat for a rate enhancement of 106 at 298 K. Express AAGEat in kJ/mol...
13. Suppose a second enzyme binds the substrate even more tightly than the enzyme shown in model 1 (the ES complex is more stable than the one shown in graph B). Draw this new E.S complex on graph B. What happens to the magnitude of the activation energy, AGact? 14. Suppose a third enzyme binds the transition state even more tightly than the enzyme diagramed Model 2. What happens to the magnitude of the activation energy, AGact? Model 2 Generalized...
Rodrigo is an enzyme engineer. He wants to know which of four peptide substrates is bound most tightly by his engineered enzyme. Which value should he measure and pay attention to? Km KCAT Vo Both A and B kcat, [S], and [E]t Rodrigo's enzyme was assayed with three substrates (A, B, and C). The SAME enzyme concentration used was for each of the three reactions. The results of the three experiments are plotted as Lineweaver-Burke plots below. Considering what you...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much of their three dimensional shape is the result of interactions between the R (variable) groups of their amino acids. The active site is the portion of the enzyme that will interact with the substrate the molecule that the enzyme acts upon. The nature and arrangement of amino acids in the active site make each enzyme specific to a substrate and to the reaction it...
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as a function of substrate concentration; label both axes. Write the associated Michaelis-Menton equation and show the location of Km and Vmax on your graph. b. Draw a second graph showing the classic Lineweaver-Burk plot; label both axes. Show the location of Km and Vmax on your graph. Discuss which plot is the most useful to determine Vmax. Draw a second line on each graph...
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...
The Michaelis-Menten equation models the hyperbolic relationship
between [S] and the initial reaction rate (V0) for an enzyme
catalyzed, single substrate reaction: E S ES E P. The model can be
more readily understood when comparing three conditions: [S]Km.
Match each statement with the condition that it describes. Note:
\"Rate\" refers to initial velocity (V0) where steady state
conditions are assumed; [Etotal] refers to the total enzyme
concentration, and [Efree] refers to the concentration of free
enzyme.
categories: [S]<<Km, [S]=Km,...
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...
Model 2 -Amylase Re UI RECLUTT Rate of reaction 0 20 80 100 40 60 Temperature, C S trate concentration always in exce) Sub s e concentration Enzyme concentration constant) 12. Amylase is an enzyme that catalyzes the digestion of carbohydrates. The graphs in Model 2 pro- vide data on several factors that affect the function of amylase in the body 4. The relationship of which two variables is illustrated in graph A of Model 2 The relationship of which...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
I answered E but I cannot figure out part F?
Using your value from the previous question, determine how many
H bonds or dipole interactions would be required to achieve a rate
enhancement of 10^6.
Part E A rate enhancement of 100 requires that the enzyme bind its transition state complex with higher affinity than its substrate. Using the Arrhenius equation, shown before this part, find AAGEat for a rate enhancement of 106 at 298 K. Express AAGEat in kJ/mol...
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