a) You evaluate the lipoxygenase inhibition by different concentrations of octyl protocathechuate. The curve numbers 0-4 are 0, 0.1, 0.2, 0.4, and 0.6 μM, respectively. What is the type of inhibition? Explain your answer in terms of the binding site of the inhibitor and the overall kinetic effect on lipoxygenase. 1/v (μmol/min) 1.0 0.8 0.6 0.4 0.2 .06 -0.03 0.00 0.03 0.06 0.09 1/[S] (μM)
a) You evaluate the lipoxygenase inhibition by different concentrations of octyl protocathechuate. The curve numbers 0-4 are 0, 0.1, 0.2, 0.4, and 0.6 μM, respectively. What is the type of inhibition? Explain your answer in terms of the binding site of the inhibitor and the overall kinetic effect on lipoxygenase. 1/v (μmol/min) 1.0 0.8 0.6 0.4 0.2 .06 -0.03 0.00 0.03 0.06 0.09 1/[S] (μM)
Biochemistry
9th Edition
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
Section: Chapter Questions
Problem 1P
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4a
![**Lipoxygenase Inhibition Analysis Using Octyl Protocatechuate**
a) You evaluate the lipoxygenase inhibition by different concentrations of octyl protocatechuate. The curve numbers 0–4 correspond to concentrations of 0, 0.1, 0.2, 0.4, and 0.6 µM, respectively. What is the type of inhibition? Explain your answer in terms of the binding site of the inhibitor and the overall kinetic effect on lipoxygenase.
**Graph Description:**
The graph plotted is a Lineweaver-Burk plot (double-reciprocal plot) showing 1/v (µmol/min) on the y-axis against 1/[S] (µM) on the x-axis. The plot provides information on enzyme kinetics and how they change in the presence of different inhibitor concentrations.
**Curve Interpretation:**
- Curve 0 (○): No inhibitor present.
- Curve 1 (△): 0.1 µM inhibitor.
- Curve 2 (▽): 0.2 µM inhibitor.
- Curve 3 (⬜): 0.4 µM inhibitor.
- Curve 4 (■): 0.6 µM inhibitor.
Each line intersects at the y-axis at different points, indicating changes in Vmax (maximum reaction velocity) and possibly KM (Michaelis constant), suggesting a specific type of inhibition pattern.
The question asks for the type of inhibition and an explanation regarding the binding site of the inhibitor and the kinetic effects on lipoxygenase.
Analyzing the pattern of line intersections and shifts can provide evidence for competitive, non-competitive, or mixed inhibition based on changes in slope, intercepts, and line crossing points.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fd7323f76-5a9c-46b6-9930-86cefe6607d1%2F167a2956-42b9-4289-bf41-6f4f9442193f%2Ffdlroo_processed.jpeg&w=3840&q=75)
Transcribed Image Text:**Lipoxygenase Inhibition Analysis Using Octyl Protocatechuate**
a) You evaluate the lipoxygenase inhibition by different concentrations of octyl protocatechuate. The curve numbers 0–4 correspond to concentrations of 0, 0.1, 0.2, 0.4, and 0.6 µM, respectively. What is the type of inhibition? Explain your answer in terms of the binding site of the inhibitor and the overall kinetic effect on lipoxygenase.
**Graph Description:**
The graph plotted is a Lineweaver-Burk plot (double-reciprocal plot) showing 1/v (µmol/min) on the y-axis against 1/[S] (µM) on the x-axis. The plot provides information on enzyme kinetics and how they change in the presence of different inhibitor concentrations.
**Curve Interpretation:**
- Curve 0 (○): No inhibitor present.
- Curve 1 (△): 0.1 µM inhibitor.
- Curve 2 (▽): 0.2 µM inhibitor.
- Curve 3 (⬜): 0.4 µM inhibitor.
- Curve 4 (■): 0.6 µM inhibitor.
Each line intersects at the y-axis at different points, indicating changes in Vmax (maximum reaction velocity) and possibly KM (Michaelis constant), suggesting a specific type of inhibition pattern.
The question asks for the type of inhibition and an explanation regarding the binding site of the inhibitor and the kinetic effects on lipoxygenase.
Analyzing the pattern of line intersections and shifts can provide evidence for competitive, non-competitive, or mixed inhibition based on changes in slope, intercepts, and line crossing points.
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