Homework Answers
Answer: Let us suppose we have a chemical reaction
A + B 
P
(Reactants)
Product
The stoichiometric equation of disapperance of reactants and appearance of product would be represented as described in the handwritten explanation attached as images starting from page 1 to page 3.
![Explanation Page 1 Rate - - AL - Alb] - All ol Rate = Reast (B38 wherein Rz rate constant) & g wefficients of equation. Keepi](http://img.homeworklib.com/questions/f90fbd80-e64a-11eb-a68b-a1b8d19125ac.png?x-oss-process=image/resize,w_560)
![New xp = K₂ [E.s] Page 2 Constant (km) Michaelis Menton as expressed as I LECSS (Absence of Inhiblton) LE-S] Се1 ( салма + LE](http://img.homeworklib.com/questions/f98e2350-e64a-11eb-ab45-21d618b1bd8f.png?x-oss-process=image/resize,w_560)
![Page 3 lp - K [Ex] [5] yang akan s en I KI (cancelling km in the denominatol and substicilting with Vmax in the numerola, we](http://img.homeworklib.com/questions/fa159ee0-e64a-11eb-b50c-93d48f1c1511.png?x-oss-process=image/resize,w_560)
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Problem 2: (Enzyme Kinetics) A competitive inhibitor I interferes with an enzyme-catalyzed reaction according to the...
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor....
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor....
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed non-competitive kinetics with y- intercepts of 15s -1 and 5 s -1 in the presence and absence of the inhibitor respectively. If the inhibitor binding constant was 0.5nM, calculate [I ] used in this reaction? a. 0.135nM b. none of the above c. 0.225nM d. InM e. 0.125nM
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...
inhibitor? 9 How are the kinetics of an enzyme-catalyzed reaction affected by a competitive A) Veax...
inhibitor? 9 How are the kinetics of an enzyme-catalyzed reaction affected by a competitive A) Veax decreased, Ke increased B) Veax decreased, A decreased C) Vax decreased K unchanged D) V unchanged, Kw increased E V unchanged, Ki decreased 20. The ability for an enzyme to pick out one particular substrate from the myriad of molecules floating around its environment is an example of A) natural selection B) specificity C) high affinity D) processivity E) none of the above The...
3) For the simplified representation of an enzyme-catalyzed reaction shown below, the statement “ES is in...
3) For the simplified representation of an enzyme-catalyzed
reaction shown below, the statement “ES is in steady-state” means
that:
A) k2 is very slow.
B) k1= k2.
C) k1= k-1.
D) k1[E][S] = k-1[ES] + k2[ES].
E) k1[E][S] = k-1[ES].
3) For the simplified representation of an enzyme-catalyzed reaction shown below, the statement “ES is in steady-state" means that: k, k, E+S <> ES Z E +P - k1 A) k2 is very slow. B) Kı= k2. C) K1= k-1....
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
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...
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equatio...
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation. b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km. c). Please draw a...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
1. The sequential mechanism for an enzyme, E, with two substrates, Si and S2 is shown...
1. The sequential mechanism for an enzyme, E, with two substrates, Si and S2 is shown below. Write the full rate equations for all species in the mechanism E+S ES ESI E S ESI S2 ESI S2 ESIS2 ESI S2 ki k. k2 k-2 k3 ESIS2 EP
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed non-competitive kinetics with y- intercepts of 15s -1 and 5 s -1 in the presence and absence of the inhibitor respectively. If the inhibitor binding constant was 0.5nM, calculate [I ] used in this reaction? a. 0.135nM b. none of the above c. 0.225nM d. InM e. 0.125nM
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...
inhibitor? 9 How are the kinetics of an enzyme-catalyzed reaction affected by a competitive A) Veax decreased, Ke increased B) Veax decreased, A decreased C) Vax decreased K unchanged D) V unchanged, Kw increased E V unchanged, Ki decreased 20. The ability for an enzyme to pick out one particular substrate from the myriad of molecules floating around its environment is an example of A) natural selection B) specificity C) high affinity D) processivity E) none of the above The...
3) For the simplified representation of an enzyme-catalyzed
reaction shown below, the statement “ES is in steady-state” means
that:
A) k2 is very slow.
B) k1= k2.
C) k1= k-1.
D) k1[E][S] = k-1[ES] + k2[ES].
E) k1[E][S] = k-1[ES].
3) For the simplified representation of an enzyme-catalyzed reaction shown below, the statement “ES is in steady-state" means that: k, k, E+S <> ES Z E +P - k1 A) k2 is very slow. B) Kı= k2. C) K1= k-1....
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...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
1. The sequential mechanism for an enzyme, E, with two substrates, Si and S2 is shown below. Write the full rate equations for all species in the mechanism E+S ES ESI E S ESI S2 ESI S2 ESIS2 ESI S2 ki k. k2 k-2 k3 ESIS2 EP
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