1. Derivation of a rate expression for two consecutive reactions reaction sequence: k₁ k₂ [ES] ₁2 K-2 k_1 where substrate S binds with enzyme E to form complex [ES]₁. Complex [ES]₁ then transforms into complex [ES]2. Complex [ES]2 then transforms into product(s) P and free enzyme E. Develop a suitable rate expression for the product P formation [r = k5 [ES] ₂] by using: a. the quasi-equilibrium (Michaelis-Menten) approach Show all of your algebraic steps for the M-M method. Assume that you can define the following reaction parameters: VMAX = K3 * [E] total K'M = 1/(K₁ K₂) Where K₁, K₂ are the equilibrium constants for reaction steps 1 and 2 in the mechanism above. S+ E * [ES] 2 : Consider the following k3 →P+E
1. Derivation of a rate expression for two consecutive reactions reaction sequence: k₁ k₂ [ES] ₁2 K-2 k_1 where substrate S binds with enzyme E to form complex [ES]₁. Complex [ES]₁ then transforms into complex [ES]2. Complex [ES]2 then transforms into product(s) P and free enzyme E. Develop a suitable rate expression for the product P formation [r = k5 [ES] ₂] by using: a. the quasi-equilibrium (Michaelis-Menten) approach Show all of your algebraic steps for the M-M method. Assume that you can define the following reaction parameters: VMAX = K3 * [E] total K'M = 1/(K₁ K₂) Where K₁, K₂ are the equilibrium constants for reaction steps 1 and 2 in the mechanism above. S+ E * [ES] 2 : Consider the following k3 →P+E
Introduction to Chemical Engineering Thermodynamics
8th Edition
ISBN:9781259696527
Author:J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Publisher:J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Chapter1: Introduction
Section: Chapter Questions
Problem 1.1P
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![1. Derivation of a rate expression for two consecutive reactions
reaction sequence:
k₁
k₂
[ES] ₁
K-1
K-2
where substrate S binds with enzyme E to form complex [ES]₁. Complex [ES]₁ then transforms into
complex [ES]2. Complex [ES]2 then transforms into product(s) P and free enzyme E.
Develop a suitable rate expression for the product P formation [r = k5 [ES]2] by using:
a. the quasi-equilibrium (Michaelis-Menten) approach
Show all of your algebraic steps for the M-M method. Assume that you can define the following reaction
parameters:
K'M = 1/(K₁ * K₂)
VMAX = K3 * [E] total
Where K₁, K₂ are the equilibrium constants for reaction steps 1 and 2 in the mechanism above.
S+ E
[ES] 2
: Consider the following
k3
→ P+E](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fd47fc2c3-8f4b-4085-b234-bc909be774e3%2F1e336b18-00f2-4bd2-a473-d2fa773ec23d%2F1xpfmk_processed.png&w=3840&q=75)
Transcribed Image Text:1. Derivation of a rate expression for two consecutive reactions
reaction sequence:
k₁
k₂
[ES] ₁
K-1
K-2
where substrate S binds with enzyme E to form complex [ES]₁. Complex [ES]₁ then transforms into
complex [ES]2. Complex [ES]2 then transforms into product(s) P and free enzyme E.
Develop a suitable rate expression for the product P formation [r = k5 [ES]2] by using:
a. the quasi-equilibrium (Michaelis-Menten) approach
Show all of your algebraic steps for the M-M method. Assume that you can define the following reaction
parameters:
K'M = 1/(K₁ * K₂)
VMAX = K3 * [E] total
Where K₁, K₂ are the equilibrium constants for reaction steps 1 and 2 in the mechanism above.
S+ E
[ES] 2
: Consider the following
k3
→ P+E
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