Exhibit 6A This is a reaction going on in your muscle cells right this very minute: The enzyme triose phosphate isomerase catalyzes this reaction in the forward direction as part of the glycolytic pathway. It follows simple Michaelis-Menten kinetics: Typical cellular concentrations: triose phosphate isomerase = 0.1 nM?dihydroxyacetone phosphate = 5 µM glyceraldehyde-3-phosphate = 2 µM $k_{1}=10^{8} \mathrm{M}^{-1} \mathrm{~s}^{-1}, k_{-1}=100 \mathrm{~s}^{-1}, k_{2}=900 \mathrm{~s}^{-1}$ -Refer to Exhibit 6A. "Restrainin" is an inhibitor of triose phosphate isomerase. When it is added to cells at a concentration of 0.4 nM, the enzyme's apparent K_M for the substrate is altered to 100 µM, but the V_max is unchanged.

Question

Quizplus · Accepted Answer

The unchanged Vmax and increased apparent Km indicate that "Restrainin" is a competitive inhibitor. Competitive inhibitors increase the apparent Km without affecting Vmax.

Exhibit 6A This Is a Reaction Going on in Your k1=108M−1 s−1,k−1=100 s−1,k2=900 s−1k_{1}=10^{8} \mathrm{M}^{-1} \mathrm{~s}^{-1}, k_{-1}=100 \mathrm{~s}^{-1}, k_{2}=900 \mathrm{~s}^{-1}k1​=108M−1 s−1,k−1​=100 s−1,k2​=900 s−1

Exhibit 6A This Is a Reaction Going on in Your $k_{1}=10^{8} \mathrm{M}^{-1} \mathrm{~s}^{-1}, k_{-1}=100 \mathrm{~s}^{-1}, k_{2}=900 \mathrm{~s}^{-1}$