14. Calculate v, and the degree of inhibition caused by a competitive inhibitor under the following conditions: (a) [S] = 2 x 10-3 M and [I] = 2 x 103 M (b) [S] = 4 x 104 M and [I] = 2 x 10-3 M (c) [S] = 7.5 x 10-3 M and [I]= 10-$ M Assume that Km = 2 x 10-3 M, K; = 1.5 x 104 M and Vmax = 270 nmoles x liter x min-. The degree of inhibition is the percent of the uninhibited velocity reached in the presence of the inhibitor. %3D

Biochemistry
9th Edition
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Chapter15: The Importance Of Energy Changes And Electron Transfer In Metabolism
Section: Chapter Questions
Problem 15RE: MATHEMATICAL If a reaction can be written AB, and the G is 20kJmol1, what would the...
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**Problems 14 and 15: Some of the exponents are unclear. Here they are:**

14. Calculate \( v_i \) and the degree of inhibition caused by a competitive inhibitor under the following conditions:
   
   (a) \([S] = 2 \times 10^{-3} \, \text{M and} \, [I] = 2 \times 10^{-3} \, \text{M}\)
   
   (b) \([S] = 4 \times 10^{-4} \, \text{M and} \, [I] = 2 \times 10^{-3} \, \text{M}\)
   
   (c) \([S] = 7.5 \times 10^{-3} \, \text{M and} \, [I] = 10^{-5} \, \text{M}\)

Assume that \( K_m = 2 \times 10^{-3} \, \text{M}, \, K_i = 1.5 \times 10^{-4} \, \text{M} \) and \( V_{max} = 270 \, \text{nmoles} \times \text{liter}^{-1} \times \text{min}^{-1} \).
   
The degree of inhibition is the percent of the uninhibited velocity reached in the presence of the inhibitor.

15. (a) What concentration of competitive inhibitor is required to yield 75% inhibition at a substrate concentration of \( 1.5 \times 10^{-3} \, \text{M} \) if \( K_m = 2.9 \times 10^{-4} \, \text{M} \) and \( K_i = 2 \times 10^{-5} \, \text{M} \)?

(b) To what concentration must the substrate be increased to reestablish the velocity at the original uninhibited value?

**Note:** The questions are designed to test understanding of enzyme kinetics, focusing on competitive inhibition, the Michaelis-Menten equation, and the concept of \( K_i \), the inhibition constant.
Transcribed Image Text:**Problems 14 and 15: Some of the exponents are unclear. Here they are:** 14. Calculate \( v_i \) and the degree of inhibition caused by a competitive inhibitor under the following conditions: (a) \([S] = 2 \times 10^{-3} \, \text{M and} \, [I] = 2 \times 10^{-3} \, \text{M}\) (b) \([S] = 4 \times 10^{-4} \, \text{M and} \, [I] = 2 \times 10^{-3} \, \text{M}\) (c) \([S] = 7.5 \times 10^{-3} \, \text{M and} \, [I] = 10^{-5} \, \text{M}\) Assume that \( K_m = 2 \times 10^{-3} \, \text{M}, \, K_i = 1.5 \times 10^{-4} \, \text{M} \) and \( V_{max} = 270 \, \text{nmoles} \times \text{liter}^{-1} \times \text{min}^{-1} \). The degree of inhibition is the percent of the uninhibited velocity reached in the presence of the inhibitor. 15. (a) What concentration of competitive inhibitor is required to yield 75% inhibition at a substrate concentration of \( 1.5 \times 10^{-3} \, \text{M} \) if \( K_m = 2.9 \times 10^{-4} \, \text{M} \) and \( K_i = 2 \times 10^{-5} \, \text{M} \)? (b) To what concentration must the substrate be increased to reestablish the velocity at the original uninhibited value? **Note:** The questions are designed to test understanding of enzyme kinetics, focusing on competitive inhibition, the Michaelis-Menten equation, and the concept of \( K_i \), the inhibition constant.
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