I’m reviewing Enzyme Inhibition and am having issues wrapping my head around non-competitive and uncompetitive inhibition (and their consequent effect on Vmax / Km.)

Biochemistry
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ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
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I’m reviewing Enzyme Inhibition and am having issues wrapping my head around non-competitive and uncompetitive inhibition (and their consequent effect on Vmax / Km.)

## Enzyme Inhibition Overview

### Graph: Enzyme Inhibition Types

**Graph Explanation:**
- The graph illustrates different types of enzyme inhibition by showing reaction velocity (V) against substrate concentration ([S]).
- **Uninhibited Reaction:** The black curve represents an uninhibited enzyme reaction, reaching a maximum velocity (Vmax). The substrate concentration at half the maximum velocity is denoted as Km.
- **Competitive Inhibition (Red Curve):** This curve shows an increase in Km with no change in Vmax, indicating the need for higher substrate concentration to reach the same velocity.
- **Non-Competitive Inhibition (Green Curve):** Here, Vmax is decreased while Km remains the same. This indicates that the inhibitor impacts Vmax but does not affect substrate binding.
- **Uncompetitive Inhibition (Purple Curve):** Both Vmax and Km are decreased. This reflects the binding of inhibitor only after the substrate is bound.

### Types of Enzyme Inhibition

1. **Competitive Inhibition**
   - **Binding Site:** Active site.
   - **Effect on Vmax:** Remains the same.
   - **Effect on Km:** Increases.
   - **Notes:** Inhibition can be overcome by increasing substrate concentration.

2. **Non-Competitive Inhibition**
   - **Binding Site:** Allosteric site.
   - **Effect on Vmax:** Decreases.
   - **Effect on Km:** Remains the same.
   - **Notes:** Does not affect substrate binding; it turns the enzyme off.

3. **Uncompetitive Inhibition**
   - **Binding Site:** Allosteric site at enzyme-substrate (E-S) complex.
   - **Effect on Vmax:** Decreases.
   - **Effect on Km:** Decreases.
   - **Notes:** Binds after the substrate, locking E-S together and preventing product formation.

4. **Mixed Inhibition**
   - **Binding Site:** Allosteric site on enzyme or E-S complex.
   - **Effect on Vmax:** Decreases.
   - **Effect on Km:** Variable (unknown).

### Important Concepts
- **Km and Vmax:** Key indicators used to understand enzyme activity under different inhibitory conditions.
- **Allosteric Sites:** Alternative binding sites on the enzyme that affect enzyme activity without competing with the substrate at the active site.
Transcribed Image Text:## Enzyme Inhibition Overview ### Graph: Enzyme Inhibition Types **Graph Explanation:** - The graph illustrates different types of enzyme inhibition by showing reaction velocity (V) against substrate concentration ([S]). - **Uninhibited Reaction:** The black curve represents an uninhibited enzyme reaction, reaching a maximum velocity (Vmax). The substrate concentration at half the maximum velocity is denoted as Km. - **Competitive Inhibition (Red Curve):** This curve shows an increase in Km with no change in Vmax, indicating the need for higher substrate concentration to reach the same velocity. - **Non-Competitive Inhibition (Green Curve):** Here, Vmax is decreased while Km remains the same. This indicates that the inhibitor impacts Vmax but does not affect substrate binding. - **Uncompetitive Inhibition (Purple Curve):** Both Vmax and Km are decreased. This reflects the binding of inhibitor only after the substrate is bound. ### Types of Enzyme Inhibition 1. **Competitive Inhibition** - **Binding Site:** Active site. - **Effect on Vmax:** Remains the same. - **Effect on Km:** Increases. - **Notes:** Inhibition can be overcome by increasing substrate concentration. 2. **Non-Competitive Inhibition** - **Binding Site:** Allosteric site. - **Effect on Vmax:** Decreases. - **Effect on Km:** Remains the same. - **Notes:** Does not affect substrate binding; it turns the enzyme off. 3. **Uncompetitive Inhibition** - **Binding Site:** Allosteric site at enzyme-substrate (E-S) complex. - **Effect on Vmax:** Decreases. - **Effect on Km:** Decreases. - **Notes:** Binds after the substrate, locking E-S together and preventing product formation. 4. **Mixed Inhibition** - **Binding Site:** Allosteric site on enzyme or E-S complex. - **Effect on Vmax:** Decreases. - **Effect on Km:** Variable (unknown). ### Important Concepts - **Km and Vmax:** Key indicators used to understand enzyme activity under different inhibitory conditions. - **Allosteric Sites:** Alternative binding sites on the enzyme that affect enzyme activity without competing with the substrate at the active site.
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