10,000 2.000 66667 Draw Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Vmax values for the inhibited and uninhibited rxns? Is the inhibitor competitive or noncompetitive? [S] (M) 1 x 104 -5 x 104 1.5 x 10-3 400-2.5 x 10-³ 2005x103 V, No Inhibitor (Arbitrary units) 0.026 38,461 0.092 10.87 37100 ONE 0.136 7.35 0.150 -67 0.165 6.0 6 1909 A L slope: 0033 yonto 5.057 V, Inhibitor Present (Arbitrary Units) Um²x=0.198 km 6.5 x 10-4 100 0.010 0.040 25 0.086 11.63 0.120 8.33 0.142 7.04 ↓ $op.= .009 yint: 5.21 900x12 km: 1.73 y/o conf. -3

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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---

### Enzyme Kinetics: Lineweaver-Burk Plots

This section explores the behavior of an enzyme through Lineweaver-Burk plots using the given experimental data. The objective is to determine the Km and Vmax values for reactions with and without inhibitors and identify whether the inhibition is competitive or noncompetitive.

**Experimental Data:**

| [S] (M)      | V, No Inhibitor (Arbitrary Units) | V, Inhibitor Present (Arbitrary Units) |
|--------------|-----------------------------------|----------------------------------------|
| 10,000 - 1 x 10⁴ | 0.026 | 0.010 |
| 2,000 - 5 x 10⁴  | 0.092 | 0.040 |
| 666.67 - 1.5 x 10⁻³ | 0.136 | 0.086 |
| 400 - 2.5 x 10⁻³  | 0.150 | 0.120 |
| 200 - 5 x 10⁻³  | 0.165 | 0.142 |

**Analysis for No Inhibitor:**

- **Slope:** 0.033
- **Y-intercept:** 5.057
- **Vmax:** 0.167 units
- **Km:** 6.57 x 10⁻⁴ M

**Analysis for Inhibitor Present:**

- **Slope:** 0.009
- **Y-intercept:** 5.21
- **Vmax:** Close to 0.142 units
- **Km:** 1.73 x 10⁻³ M

Based on this analysis and data on slope and intercept changes, the type of inhibition can be classified as *noncompetitive*.

---

### Graph Explanation (Hypothetical):

The Lineweaver-Burk plot graphs the reciprocal of the substrate concentration [1/[S]] against the reciprocal of the reaction velocity [1/V]. 

- **Plot Characteristics**:
  - A steeper slope indicates slower reaction velocity.
  - The y-intercept gives the inverse of Vmax; a higher value suggests lower maximal velocity.
  - Changes in Km and Vmax with an inhibitor present typically indicate the nature of the inhibition.

This understanding assists in comprehensively analyzing enzyme behavior under different conditions, a crucial aspect of enzyme
Transcribed Image Text:Transcription for Educational Content: --- ### Enzyme Kinetics: Lineweaver-Burk Plots This section explores the behavior of an enzyme through Lineweaver-Burk plots using the given experimental data. The objective is to determine the Km and Vmax values for reactions with and without inhibitors and identify whether the inhibition is competitive or noncompetitive. **Experimental Data:** | [S] (M) | V, No Inhibitor (Arbitrary Units) | V, Inhibitor Present (Arbitrary Units) | |--------------|-----------------------------------|----------------------------------------| | 10,000 - 1 x 10⁴ | 0.026 | 0.010 | | 2,000 - 5 x 10⁴ | 0.092 | 0.040 | | 666.67 - 1.5 x 10⁻³ | 0.136 | 0.086 | | 400 - 2.5 x 10⁻³ | 0.150 | 0.120 | | 200 - 5 x 10⁻³ | 0.165 | 0.142 | **Analysis for No Inhibitor:** - **Slope:** 0.033 - **Y-intercept:** 5.057 - **Vmax:** 0.167 units - **Km:** 6.57 x 10⁻⁴ M **Analysis for Inhibitor Present:** - **Slope:** 0.009 - **Y-intercept:** 5.21 - **Vmax:** Close to 0.142 units - **Km:** 1.73 x 10⁻³ M Based on this analysis and data on slope and intercept changes, the type of inhibition can be classified as *noncompetitive*. --- ### Graph Explanation (Hypothetical): The Lineweaver-Burk plot graphs the reciprocal of the substrate concentration [1/[S]] against the reciprocal of the reaction velocity [1/V]. - **Plot Characteristics**: - A steeper slope indicates slower reaction velocity. - The y-intercept gives the inverse of Vmax; a higher value suggests lower maximal velocity. - Changes in Km and Vmax with an inhibitor present typically indicate the nature of the inhibition. This understanding assists in comprehensively analyzing enzyme behavior under different conditions, a crucial aspect of enzyme
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