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2. After conducting enzyme activity assays with one enzyme and various substrates, you generate the following table. Substrate Putrescine Flavanol Tryptophan Anthocyanin Auxin Intracellular Concentration 5 x 10-6 M 5 x 10-5 M 5 x 10-³ M 5 x 104 M 5 x 10-5 M Kcat 50000 5000 500 50 5 KM 5 x 10-4 M 5 x 10-4 M 5 x 10-³ M 5 x 10-³ M 5 x 10-² M Which is most likely the natural substrate for this enzyme? Briefly justify your answer: Kcat/KM 1 x 108 1 x 107 1 x 105 1 x 105 1 x 10²

2. After conducting enzyme activity assays with one enzyme and various substrates, you generate the following table. Substrate Putrescine Flavanol Tryptophan Anthocyanin Auxin Intracellular Concentration 5 x 10-6 M 5 x 10-5 M 5 x 10-³ M 5 x 104 M 5 x 10-5 M Kcat 50000 5000 500 50 5 KM 5 x 10-4 M 5 x 10-4 M 5 x 10-³ M 5 x 10-³ M 5 x 10-² M Which is most likely the natural substrate for this enzyme? Briefly justify your answer: Kcat/KM 1 x 108 1 x 107 1 x 105 1 x 105 1 x 10²

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 Activity Assay Results ## Introduction Enzyme activity assays are conducted to determine the efficiency and affinity of an enzyme towards various substrates. This particular study used one enzyme with different substrates to generate the data presented in the table below. ## Data Table | Substrate | Intracellular Concentration | \( k_{\text{cat}} \) | \( K_M \) | \( k_{\text{cat}}/K_M \) | |--------------|-----------------------------|----------------------|------------------|---------------------| | Putrescine | \( 5 \times 10^{-6} \, \text{M} \) | 50000 | \( 5 \times 10^{-4} \, \text{M} \) | \( 1 \times 10^{8} \) | | Flavanol | \( 5 \times 10^{-5} \, \text{M} \) | 5000 | \( 5 \times 10^{-4} \, \text{M} \) | \( 1 \times 10^{7} \) | | Tryptophan | \( 5 \times 10^{-3} \, \text{M} \) | 500 | \( 5 \times 10^{-3} \, \text{M} \) | \( 1 \times 10^{5} \) | | Anthocyanin | \( 5 \times 10^{-4} \, \text{M} \) | 50 | \( 5 \times 10^{-3} \, \text{M} \) | \( 1 \times 10^{5} \) | | Auxin | \( 5 \times 10^{-5} \, \text{M} \) | 5 | \( 5 \times 10^{-2} \, \text{M} \) | \( 1 \times 10^{2} \) | ## Analysis Question Which is most likely the natural substrate for this enzyme? **Briefly justify your answer:** The natural substrate is typically the one with the highest \( k_{\text{cat}}/K_M \) ratio, indicating the most efficient catalysis relative to the affinity. Based on this table, **Putrescine
Transcribed Image Text:# Enzyme Activity Assay Results ## Introduction Enzyme activity assays are conducted to determine the efficiency and affinity of an enzyme towards various substrates. This particular study used one enzyme with different substrates to generate the data presented in the table below. ## Data Table | Substrate | Intracellular Concentration | \( k_{\text{cat}} \) | \( K_M \) | \( k_{\text{cat}}/K_M \) | |--------------|-----------------------------|----------------------|------------------|---------------------| | Putrescine | \( 5 \times 10^{-6} \, \text{M} \) | 50000 | \( 5 \times 10^{-4} \, \text{M} \) | \( 1 \times 10^{8} \) | | Flavanol | \( 5 \times 10^{-5} \, \text{M} \) | 5000 | \( 5 \times 10^{-4} \, \text{M} \) | \( 1 \times 10^{7} \) | | Tryptophan | \( 5 \times 10^{-3} \, \text{M} \) | 500 | \( 5 \times 10^{-3} \, \text{M} \) | \( 1 \times 10^{5} \) | | Anthocyanin | \( 5 \times 10^{-4} \, \text{M} \) | 50 | \( 5 \times 10^{-3} \, \text{M} \) | \( 1 \times 10^{5} \) | | Auxin | \( 5 \times 10^{-5} \, \text{M} \) | 5 | \( 5 \times 10^{-2} \, \text{M} \) | \( 1 \times 10^{2} \) | ## Analysis Question Which is most likely the natural substrate for this enzyme? **Briefly justify your answer:** The natural substrate is typically the one with the highest \( k_{\text{cat}}/K_M \) ratio, indicating the most efficient catalysis relative to the affinity. Based on this table, **Putrescine
Expert Solution
Step 1

Enzyme efficiency can be best determined by a factor called catalytic efficiency, expressed as Kcat/Km.

Kcat is called turnover number which can be defined as the number of substrate molecules converted to product by one catalytic site of an enzyme per minute. Higher the turnover number, greater the efficiency.

Km is the substrate concentration at which rate of velocity is half maximal velocity. It can be correlated with affinity of substrate for the enzyme. Higher the Km, lesser the affinity.

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