The thermodynamic box (linked functions diagram) below shows all the possible dissociation equilibria for an enzyme-bound reversible inhibitor and substrate (the ESI complex). Kİ' B.KI, and KES' =B KES Keat K1 E+S kı k-1 KES ES + K'₁ = BK₁ P+E I For the ß ranges/values below, fill in the type of inhibition (competitive, uncompetitive, mixed, or special case of mixed: "pure noncompetitive". Describe briefly in qualitative terms (not equations) how changing ß changes the relative binding affinities of I and S to different species (E, ES, and EI), and explain in terms of relative values of KI and KI

The thermodynamic box (linked functions diagram) below shows all the possible dissociation equilibria for an enzyme-bound reversible inhibitor and substrate (the ESI complex). Kİ' B.KI, and KES' =B KES Keat K1 E+S kı k-1 KES ES + K'₁ = BK₁ P+E I For the ß ranges/values below, fill in the type of inhibition (competitive, uncompetitive, mixed, or special case of mixed: "pure noncompetitive". Describe briefly in qualitative terms (not equations) how changing ß changes the relative binding affinities of I and S to different species (E, ES, and EI), and explain in terms of relative values of KI and KI

Chemistry: The Molecular Science

5th Edition

ISBN:9781285199047

Author:John W. Moore, Conrad L. Stanitski

Publisher:John W. Moore, Conrad L. Stanitski

Chapter11: Chemical Kinetics: Rates Of Reactions

Section: Chapter Questions

Problem 83QRT

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Concept explainers

Catalysis and Enzymatic Reactions

Catalysis is the kind of chemical reaction in which the rate (speed) of a reaction is enhanced by the catalyst which is not consumed during the process of reaction and afterward it is removed when the catalyst is not used to make up the impurity in the product. The enzymatic reaction is the reaction that is catalyzed via enzymes.

Lock And Key Model

The lock-and-key model is used to describe the catalytic enzyme activity, based on the interaction between enzyme and substrate. This model considers the lock as an enzyme and the key as a substrate to explain this model. The concept of how a unique distinct key only can have the access to open a particular lock resembles how the specific substrate can only fit into the particular active site of the enzyme. This is significant in understanding the intermolecular interaction between proteins and plays a vital role in drug interaction.

Question

Can you please help find the type of inhibition for these two question?

The thermodynamic box (linked functions diagram) below shows all the possible dissociation
equilibria for an enzyme-bound reversible inhibitor and substrate (the ESI complex).
Kİ' = B•KI , and KES' =B•KES
%3D
kı
kent
For the B ranges/values below, fill in the
type of inhibition (competitive,
uncompetitive, mixed, or special case of
mixed: "pure noncompetitive". Describe
briefly in qualitative terms (not equations)
how changing B changes the relative
binding affinities of I and S to different
species (E, ES, and EI), and explain in
terms of relative values of KI' and KI,
and of KES' and KES.
E+S
ES
P+E
KES
KI
K'I = BK1
El + S
ESI --X-- P+ EI
K'ES = BKES

C. B=1
Type of inhibition:
D. 1<B< infinity
Type of inhibition:

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Step 1: Introduction

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Step 2: Competitive inhibition (CI)

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Step 3: Out-of-competition suspension

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Step 4: Mixed inhibition

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