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iven the kinetics data for each enzyme in the presence and absence of its inhibitor, determine the type of inhibition. Enzyme KM (MM) 8,000 12,000 5,000 5,000 50 30 6 15 3 3 carbonic anhydrase + inhibitor A chymotrypsin + inhibitor B penicillinase inhibitor C lysozyme + inhibitor D carboxypeptisase A + inhibitor E Vmax (mmol/s) 600,000 600,000 100 75 2,000 1,500 0.5 0.5 1,000 800

iven the kinetics data for each enzyme in the presence and absence of its inhibitor, determine the type of inhibition. Enzyme KM (MM) 8,000 12,000 5,000 5,000 50 30 6 15 3 3 carbonic anhydrase + inhibitor A chymotrypsin + inhibitor B penicillinase inhibitor C lysozyme + inhibitor D carboxypeptisase A + inhibitor E Vmax (mmol/s) 600,000 600,000 100 75 2,000 1,500 0.5 0.5 1,000 800

Biochemistry
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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### Enzyme Kinetics and Inhibition The following table provides kinetic data for various enzymes in the presence and absence of specific inhibitors. The data includes values for the Michaelis constant (\(K_M\)) and the maximum velocity (\(V_{\text{max}}\)) of each enzyme reaction. Use this information to determine the type of inhibition each inhibitor imposes on its respective enzyme. #### Enzyme Data Table | Enzyme | \(K_M\) (mM) | \(V_{\text{max}}\) (mmol/s) | |--------------------|------------|---------------------| | Carbonic Anhydrase | 8,000 | 600,000 | | + Inhibitor A | 12,000 | 600,000 | | Chymotrypsin | 5,000 | 100 | | + Inhibitor B | 5,000 | 100 | | Penicillinase | 50 | 2,000 | | + Inhibitor C | 30 | 1,500 | | Lysozyme | 6 | 0.5 | | + Inhibitor D | 15 | 0.5 | | Carboxypeptidase A | 3 | 1,000 | | + Inhibitor E | 3 | 800 | ### Types of Enzyme Inhibition Below is a classification task. Based on the provided data, categorize each inhibitor into one of three types of enzyme inhibition: Competitive, Noncompetitive, and Uncompetitive. #### Inhibition Classification - **Competitive:** Inhibition increases \(K_M\) but does not affect \(V_{\text{max}}\). - **Noncompetitive:** Inhibition does not alter \(K_M\) but decreases \(V_{\text{max}}\). - **Uncompetitive:** Inhibition decreases both \(K_M\) and \(V_{\text{max}}\). #### Answer Bank - **Competitive:** - Inhibitor A - **Noncompetitive:** - Inhibitor B - Inhibitor E - **Uncompetitive:** - Inhibitor C - Inhibitor D This classification will aid in understanding how different inhibitors affect enzyme efficiency and affinity. Use this data to explore enzyme kinetics further.
Transcribed Image Text:### Enzyme Kinetics and Inhibition The following table provides kinetic data for various enzymes in the presence and absence of specific inhibitors. The data includes values for the Michaelis constant (\(K_M\)) and the maximum velocity (\(V_{\text{max}}\)) of each enzyme reaction. Use this information to determine the type of inhibition each inhibitor imposes on its respective enzyme. #### Enzyme Data Table | Enzyme | \(K_M\) (mM) | \(V_{\text{max}}\) (mmol/s) | |--------------------|------------|---------------------| | Carbonic Anhydrase | 8,000 | 600,000 | | + Inhibitor A | 12,000 | 600,000 | | Chymotrypsin | 5,000 | 100 | | + Inhibitor B | 5,000 | 100 | | Penicillinase | 50 | 2,000 | | + Inhibitor C | 30 | 1,500 | | Lysozyme | 6 | 0.5 | | + Inhibitor D | 15 | 0.5 | | Carboxypeptidase A | 3 | 1,000 | | + Inhibitor E | 3 | 800 | ### Types of Enzyme Inhibition Below is a classification task. Based on the provided data, categorize each inhibitor into one of three types of enzyme inhibition: Competitive, Noncompetitive, and Uncompetitive. #### Inhibition Classification - **Competitive:** Inhibition increases \(K_M\) but does not affect \(V_{\text{max}}\). - **Noncompetitive:** Inhibition does not alter \(K_M\) but decreases \(V_{\text{max}}\). - **Uncompetitive:** Inhibition decreases both \(K_M\) and \(V_{\text{max}}\). #### Answer Bank - **Competitive:** - Inhibitor A - **Noncompetitive:** - Inhibitor B - Inhibitor E - **Uncompetitive:** - Inhibitor C - Inhibitor D This classification will aid in understanding how different inhibitors affect enzyme efficiency and affinity. Use this data to explore enzyme kinetics further.
Expert Solution
Step 1: Competitive inhibition

A competitive inhibitor competes with the substrate for active site of an enzyme. If inhibitor occupies the active site, it prevents substrate  from binding to the enzyme. Competitive inhibitors are structurally similar to substrates. Enzymes form EI ( enzyme inhibitor ) complexes and prevent product formation.

Km value will be increased in the presence of competitive inhibitor but Vmax is unaffected. Km is the substrate concentration at which  V0 = Vmax /2

Vmax = maximum velocity

Here we have to choose the inhibitors with increased Km value and unaffected Vmax.

Inhibitors are A and D

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