The reaction is catalyzed by an enzyme called triose phosphate isomerase (TPI). This enzyme accelerates both the forward and reverse reactions using either DHAP or GAP as a substrate. Both reactions follow Michaelis-Menten kinetics, with kinetic perameters K_M= 1.2x 10^-3M. and k_cat=6.5x 10⁴min^-1.

A.) Assuming that TPI binds and releases its substrates rapidly (compared to the isomerization chemistry), which substrate binds to the enzyme with higher affinity?

B.) Under the following conditions: [TPI]=1x10^-6M, [DHAP]=2x10^-3M, and [GAP]=0M. What is the initial reaction velocity (v₀) for the forward reaction?

Question

The reaction is catalyzed by an enzyme called triose phosphate isomerase (TPI). This enzyme accelerates both the forward and reverse reactions using either DHAP or GAP as a substrate. Both reactions follow Michaelis-Menten kinetics, with kinetic perameters K_M= 1.2x 10^-3M. and k_cat=6.5x 10⁴min^-1.

A.) Assuming that TPI binds and releases its substrates rapidly (compared to the isomerization chemistry), which substrate binds to the enzyme with higher affinity?

B.) Under the following conditions: [TPI]=1x10^-6M, [DHAP]=2x10^-3M, and [GAP]=0M. What is the initial reaction velocity (v₀) for the forward reaction?

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