What effect does a negative effector have on the graph of reac- tion rate (V) vs. [substrate] for an allosteric effector?

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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**Text:**

What effect does a negative effector have on the graph of reaction rate (V) vs. [substrate] for an allosteric effector?

**Explanation:**

This text references the impact of a negative effector on a reaction rate graph in the context of allosteric regulation. Typically, an allosteric effector binds to an enzyme at a site other than the active site, inducing a conformational change that alters the enzyme's activity.

For a negative allosteric effector:

1. **Decrease in Activity:** The presence of a negative effector generally decreases enzyme activity, resulting in a lower reaction rate (V) at a given substrate concentration ([substrate]).
  
2. **Graph Shape:** On a plot of reaction rate (V) versus substrate concentration ([substrate]), this effect is often visualized as a rightward shift in the curve. This shift indicates a higher substrate concentration is required to reach the same reaction rate observed without the effector.

3. **Lower Vmax:** The maximum reaction rate (Vmax) may also be lower in the presence of the negative effector.

This concept is vital in understanding enzyme kinetics and the regulatory mechanisms in biochemical pathways.
Transcribed Image Text:**Text:** What effect does a negative effector have on the graph of reaction rate (V) vs. [substrate] for an allosteric effector? **Explanation:** This text references the impact of a negative effector on a reaction rate graph in the context of allosteric regulation. Typically, an allosteric effector binds to an enzyme at a site other than the active site, inducing a conformational change that alters the enzyme's activity. For a negative allosteric effector: 1. **Decrease in Activity:** The presence of a negative effector generally decreases enzyme activity, resulting in a lower reaction rate (V) at a given substrate concentration ([substrate]). 2. **Graph Shape:** On a plot of reaction rate (V) versus substrate concentration ([substrate]), this effect is often visualized as a rightward shift in the curve. This shift indicates a higher substrate concentration is required to reach the same reaction rate observed without the effector. 3. **Lower Vmax:** The maximum reaction rate (Vmax) may also be lower in the presence of the negative effector. This concept is vital in understanding enzyme kinetics and the regulatory mechanisms in biochemical pathways.
Expert Solution
Step 1

INTRODUCTION :

Allosteric enzymes :

Allosteric enzymes are those enzymes which have an additional binding site for any effector molecules other than the active site. This binding of an effector brings conformational & chemical changes, and therefore changes its catalytic properties. The effector molecule can be an inhibitor or activator of the enzyme action. Allostery is the process of  regulation of enzyme, where binding at one site influences the binding at other subsequent sites.

Allosteric effectors :

An allosteric effector is a molecule which binds to the site which is different than the active site of an allosteric enzyme, which causes a change in configuration of the enzyme resulting in an increase (positive effector) or reduction (negative effector) in the activity of the enzyme.

Substrate:

A substrate is a molecule with which an enzyme reacts with. The active site of the enzyme, the location where weak bonds are formed between the two molecules , is loaded with a substrate. After that an enzyme substrate complex is formed, and the enzyme's action on the substrate causes it to react and become as the planned way of the enzyme. 

 

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