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Choose the correct answer from the list below. is a type of mathematical model that describes...
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...
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the...
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the initial velocity, Vo, of an enzymatic reaction and substrate concentration, [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation: [S] <<Km; [S] = Km; [S] >> Km. Match each condition with the statement(s) that describe it. TV, Vmox[S] Vo =Vmax m . V Vo - Vmax [S] Km +[S] V. (um/min) max [S] (mm) (a) Doubling [S] will almost double...
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the...
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the concentration of the substrate of the reaction ([S]). In Damon's Michaelis-Menten experiment, the highest concentration of substrate used was 500 UM. What do you think will happen to the reaction velocity if higher concentrations of substrate were used? Select one: a. Vo will reach a plateau at higher (S) values O b. Vo will increase exponentially as (S) is increased O c. Vo will...
(10 points) Michaelis-Menten kinetics. Consider ving enzymatic reaction, E + A H EA → E+ P...
(10 points) Michaelis-Menten kinetics. Consider ving enzymatic reaction, E + A H EA → E+ P where E, A, and P are the concentrations of enzyme, substrate and product reen Show that rate and product respectively. V = "max [A] Km + [A]
c. 0.6 sec d. 1.67 sec 16. Which of the following about Michaelis-Menten enzyme kinetics is CORRECT? a. It assumes t...
c. 0.6 sec d. 1.67 sec 16. Which of the following about Michaelis-Menten enzyme kinetics is CORRECT? a. It assumes that the maximum reaction rate is proportional to the catalytic constant multiplied by the total enzyme concentration. b. It assumes that the enzyme-substrate complex concentration remains steady state. c. KM is defined as the substrate concentration at which the velocity of the reaction is maximal, so the unit is M. d. The KM is assigned to each enzyme regardless of...
Match each statement with the condition that it describes. Note that "rate" refers to initial velocity...
Match each statement with the condition that it describes.
Note that "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
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V for an enzyme-catalyzed, single-substrate reaction ES ES EP. The model can be more readily understood when comparing three conditions: [S] << Km, [S] = Km, and...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have any of the same values for their Vmax, Vmax/2 or Km? If so which are the affinity for substrate same which are different? Enzyme with high Enzyme with low affinity for substrate Difference in reaction rate at low [5] Reaction rater Low (S] Substrate concentration [5] b. READ THIS: Enzyme-substrate affinity is the tendency for enzyme and substrate to bind together and form 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...
an allosteric enzyme that follws the concerted mechanism (MWC model) has T/R ratio of 300 in...
an allosteric enzyme that follws the concerted mechanism (MWC model) has T/R ratio of 300 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relationship between the rate of the reaction (V) and substrate concentration ([S])? Select all that apply. The enzyme would be less active The enzyme would likely follow Michaelis-Menten kinetics The plot of V vs. [S] would be shaped like an S, sigmoidal The enzyme would be mostly in the...
QUESTION 27 Which of the following statements is a true conclusion from the kinetics and equilibrium...
QUESTION 27 Which of the following statements is a true conclusion from the kinetics and equilibrium plots shown for two reaction (A and B) shown below? 100% Y х Х 0% Sec Sec A B In the given plots, Y is the reactant and X is the product Reaction B Involves a catalyst only in the forward direction Reaction A Involves a catalyst for the forward direction. Both reactions A and B are unimolecular reversible reactions QUESTION 28 Which of...
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...
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the initial velocity, Vo, of an enzymatic reaction and substrate concentration, [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation: [S] <<Km; [S] = Km; [S] >> Km. Match each condition with the statement(s) that describe it. TV, Vmox[S] Vo =Vmax m . V Vo - Vmax [S] Km +[S] V. (um/min) max [S] (mm) (a) Doubling [S] will almost double...
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the concentration of the substrate of the reaction ([S]). In Damon's Michaelis-Menten experiment, the highest concentration of substrate used was 500 UM. What do you think will happen to the reaction velocity if higher concentrations of substrate were used? Select one: a. Vo will reach a plateau at higher (S) values O b. Vo will increase exponentially as (S) is increased O c. Vo will...
(10 points) Michaelis-Menten kinetics. Consider ving enzymatic reaction, E + A H EA → E+ P where E, A, and P are the concentrations of enzyme, substrate and product reen Show that rate and product respectively. V = "max [A] Km + [A]
c. 0.6 sec d. 1.67 sec 16. Which of the following about Michaelis-Menten enzyme kinetics is CORRECT? a. It assumes that the maximum reaction rate is proportional to the catalytic constant multiplied by the total enzyme concentration. b. It assumes that the enzyme-substrate complex concentration remains steady state. c. KM is defined as the substrate concentration at which the velocity of the reaction is maximal, so the unit is M. d. The KM is assigned to each enzyme regardless of...
Match each statement with the condition that it describes.
Note that "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
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V for an enzyme-catalyzed, single-substrate reaction ES ES EP. The model can be more readily understood when comparing three conditions: [S] << Km, [S] = Km, and...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have any of the same values for their Vmax, Vmax/2 or Km? If so which are the affinity for substrate same which are different? Enzyme with high Enzyme with low affinity for substrate Difference in reaction rate at low [5] Reaction rater Low (S] Substrate concentration [5] b. READ THIS: Enzyme-substrate affinity is the tendency for enzyme and substrate to bind together and form the...
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...
QUESTION 27 Which of the following statements is a true conclusion from the kinetics and equilibrium plots shown for two reaction (A and B) shown below? 100% Y х Х 0% Sec Sec A B In the given plots, Y is the reactant and X is the product Reaction B Involves a catalyst only in the forward direction Reaction A Involves a catalyst for the forward direction. Both reactions A and B are unimolecular reversible reactions QUESTION 28 Which of...
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