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VKM Allosteric Enzyme

This document discusses allosteric enzymes and the Monod-Wyman-Changeux model. The MWC model postulates that enzymes exist in two conformational states, tense (T) and relaxed (R), and that ligands can bind and stabilize one state over the other. The model explains how ligands like activators stabilize the R state, increasing substrate binding affinity, while inhibitors stabilize the T state, decreasing substrate binding affinity in a negative heterotropic effect.

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Vinod Mishra
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239 views21 pages

VKM Allosteric Enzyme

This document discusses allosteric enzymes and the Monod-Wyman-Changeux model. The MWC model postulates that enzymes exist in two conformational states, tense (T) and relaxed (R), and that ligands can bind and stabilize one state over the other. The model explains how ligands like activators stabilize the R state, increasing substrate binding affinity, while inhibitors stabilize the T state, decreasing substrate binding affinity in a negative heterotropic effect.

Uploaded by

Vinod Mishra
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PPTX, PDF, TXT or read online on Scribd
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Allosteric Enzyme

Few examples: Allosteric enzymes


Modulators of ATCase
MWC Model or Symmetry Model or Concerted Model

Monod, Wyman and Changeux, 1965

Postulates:
1. Effect of L

I. Homotopic Interaction
I. Homotopic Interaction
Effect of c
When the T state is highly
preferred (L is large
At low ligand
concentrations (low ) the
amount of ligand bound
(YS) increases with the
ligand-binding affinity of
the T state (increasing c)
since the protein is largely
in the T state
As [α] increases, the
fractional saturation (Ys)
increases for R state.
MWC model
I. Heterotropic Interaction

1. Effect of activator (r)


 Activator stabilizes R state
 The presence of activator
increases the protein’s substrate-
binding affinity (a positive
heterotropic effect), although it
decreases the protein’s degree of
substrate-binding cooperativity
2. Effect of inhibitor (β)
 Inhibitor stabilized T state
The inhibitor only binds to the T
state, reduces the binding affinity for
substrate (a negative heterotropic
effect.

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