Exhibit 6A This is a reaction going on in your muscle cells right this very minute: $Exhibit 6A This is a reaction going on in your muscle cells right this very minute: The enzyme triose phosphate isomerase catalyzes this reaction in the forward direction as part of the glycolytic pathway. It follows simple Michaelis-Menten kinetics: Typical cellular concentrations: triose phosphate isomerase = 0.1 nM Dihydroxyacetone phosphate = 5 µM glyceraldehyde-3-phosphate = 2 µM Refer to Exhibit 6A. Hindrate is an inhibitor of triose phosphate isomerase. When it is added to cells at a concentration of 0.1 nM, the enzyme's KM for the substrate is unchanged, but the apparent Vmax is altered to 50 nM\sec. A) This is a competitive inhibitor. B) This is an uncompetitive inhibitor. C) This is a noncompetitive inhibitor. D) This is an irreversible inhibitor.$ The enzyme triose phosphate isomerase catalyzes this reaction in the forward direction as part of the glycolytic pathway. It follows simple Michaelis-Menten kinetics: $Exhibit 6A This is a reaction going on in your muscle cells right this very minute: The enzyme triose phosphate isomerase catalyzes this reaction in the forward direction as part of the glycolytic pathway. It follows simple Michaelis-Menten kinetics: Typical cellular concentrations: triose phosphate isomerase = 0.1 nM Dihydroxyacetone phosphate = 5 µM glyceraldehyde-3-phosphate = 2 µM Refer to Exhibit 6A. Hindrate is an inhibitor of triose phosphate isomerase. When it is added to cells at a concentration of 0.1 nM, the enzyme's KM for the substrate is unchanged, but the apparent Vmax is altered to 50 nM\sec. A) This is a competitive inhibitor. B) This is an uncompetitive inhibitor. C) This is a noncompetitive inhibitor. D) This is an irreversible inhibitor.$
Typical cellular concentrations: triose phosphate isomerase = 0.1 nM
Dihydroxyacetone phosphate = 5 µM glyceraldehyde-3-phosphate = 2 µM
Refer to Exhibit 6A. "Hindrate" is an inhibitor of triose phosphate isomerase. When it is added to cells at a concentration of 0.1 nM, the enzyme's K_M for the substrate is unchanged, but the apparent V_max is altered to 50 nM\sec.
A) This is a competitive inhibitor.
B) This is an uncompetitive inhibitor.
C) This is a noncompetitive inhibitor.
D) This is an irreversible inhibitor.

Enzymatic Activity Has an Optimum Temperature Because

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