Kinetic Parameters of Enzyme-Catalyzed Reactions TABLE 12-1 The Values of KM, Keat, and Keat/KM for Some Enzymes and Substrates Enzyme KM (M) 9.5 x 10-5 1.2 x 10-2 2.6 x 10-2 2.5 x 10-2 4.4 x 10-¹ 8.8 x 10-2 6.6 x 10-4 Acetylcholinesterase Carbonic anhydrase Catalase Chymotrypsin Fumarase Urease Substrate Acetylcholine CO₂ HCO3 H₂O₂ N-Acetylglycine ethyl ester N-Acetylvaline ethyl ester N-Acetyltyrosine ethyl ester Fumarate Malate Urea 5.0 x 10-6 2.5 x 10-5 2.5 x 10-2 Keat (S-¹) 1.4 x 104 1.0 X 106 4.0 X 105 1.0 x 107 5.1 x 10-² 1.7 x 10-1 1.9 X 10² 8.0 x 10² 9.0 × 10² 1.0 x 10¹ Keat/KM (M-¹.s-¹) 1.5 x 108 8.3 x 107 1.5 x 107 4.0 × 108 1.2 x 10-¹ 1.9 2.9 x 105 1.6 x 108 3.6 x 107 4.0 X 105 | Which enzyme is the most catalytically efficient? Which substrate does chymotrypsin bind to most tightly (assume k_₁ >> K₂)? -1 Is fumarate or malate a better substrate of fumarase? Is it possible to have a kcat/KM of greater than 1 x 10⁹ M-¹ s-¹? Why or why not?

Biochemistry
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Chapter1: Biochemistry: An Evolving Science
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**Kinetic Parameters of Enzyme-Catalyzed Reactions**

**TABLE 12-1:** The Values of \( K_M \), \( k_{cat} \), and \( \frac{k_{cat}}{K_M} \) for Some Enzymes and Substrates

| Enzyme            | Substrate                         | \( K_M \) (M)    | \( k_{cat} \) (s\(^{-1}\)) | \( \frac{k_{cat}}{K_M} \) (M\(^{-1}\) s\(^{-1}\)) |
|-------------------|-----------------------------------|-------------------|-------------------------|-------------------------|
| Acetylcholinesterase | Acetylcholine                    | \( 9.5 \times 10^{-5} \) | \( 1.4 \times 10^4 \)    | \( 1.5 \times 10^8 \)   |
| Carbonic anhydrase | \( \text{CO}_2 \)                | \( 1.2 \times 10^{-2} \) | \( 1.0 \times 10^6 \)    | \( 8.3 \times 10^7 \)   |
|                   | \( \text{HCO}_3^- \)              | \( 2.6 \times 10^{-2} \) | \( 4.0 \times 10^5 \)    | \( 1.5 \times 10^7 \)   |
| Catalase          | \( \text{H}_2\text{O}_2 \)       | \( 2.5 \times 10^{-2} \) | \( 4.0 \times 10^7 \)    | \( 1.6 \times 10^8 \)   |
| Chymotrypsin      | N-Acetylglycine ethyl ester       | \( 4.4 \times 10^{-1} \) | \( 5.1 \times 10^{0} \)  | \( 1.2 \times 10^1 \)   |
|                   | N-Acetylvaline ethyl ester        | \( 8.8 \times 10^{-1} \) | \( 5.7 \times 10^{0} \)  | \( 6
Transcribed Image Text:**Kinetic Parameters of Enzyme-Catalyzed Reactions** **TABLE 12-1:** The Values of \( K_M \), \( k_{cat} \), and \( \frac{k_{cat}}{K_M} \) for Some Enzymes and Substrates | Enzyme | Substrate | \( K_M \) (M) | \( k_{cat} \) (s\(^{-1}\)) | \( \frac{k_{cat}}{K_M} \) (M\(^{-1}\) s\(^{-1}\)) | |-------------------|-----------------------------------|-------------------|-------------------------|-------------------------| | Acetylcholinesterase | Acetylcholine | \( 9.5 \times 10^{-5} \) | \( 1.4 \times 10^4 \) | \( 1.5 \times 10^8 \) | | Carbonic anhydrase | \( \text{CO}_2 \) | \( 1.2 \times 10^{-2} \) | \( 1.0 \times 10^6 \) | \( 8.3 \times 10^7 \) | | | \( \text{HCO}_3^- \) | \( 2.6 \times 10^{-2} \) | \( 4.0 \times 10^5 \) | \( 1.5 \times 10^7 \) | | Catalase | \( \text{H}_2\text{O}_2 \) | \( 2.5 \times 10^{-2} \) | \( 4.0 \times 10^7 \) | \( 1.6 \times 10^8 \) | | Chymotrypsin | N-Acetylglycine ethyl ester | \( 4.4 \times 10^{-1} \) | \( 5.1 \times 10^{0} \) | \( 1.2 \times 10^1 \) | | | N-Acetylvaline ethyl ester | \( 8.8 \times 10^{-1} \) | \( 5.7 \times 10^{0} \) | \( 6
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