Final answer:
When 1 mM fructose 1,6-bisphosphate is incubated with aldolase under standard conditions, it cleaves into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate, with equilibrium concentrations of approximately 1 mM for each, assuming sufficient enzyme presence and that the reaction has reached equilibrium.
Step-by-step explanation:
The equilibrium concentrations of fructose 1,6-bisphosphate, dihydroxyacetone phosphate (DHAP), and glyceraldehyde 3-phosphate (G-3-P) when 1 mM fructose 1,6-bisphosphate is incubated with aldolase under standard conditions are determined by the action of aldolase in glycolysis. During this reaction, fructose 1,6-bisphosphate is cleaved by the enzyme aldolase into DHAP and G-3-P.
These two three-carbon isomers usually reach an equilibrium due to their interconversion by the enzyme triosephosphate isomerase.
The reaction is reversible and highly regulated, and the equilibrium concentrations will depend on several factors, including enzyme activity, temperature, and the presence of other substrates or inhibitors. However, the stoichiometry of the reaction suggests that for every molecule of fructose 1,6-bisphosphate, one molecule of DHAP and one molecule of G-3-P are produced.
Given that the initial concentration of fructose 1,6-bisphosphate is 1 mM and that the reaction proceeds with a 1:1 stoichiometry, we would expect the equilibrium concentrations of DHAP and G-3-P to also be approximately 1 mM if the enzyme aldolase is present in sufficient quantity and the reaction has reached equilibrium.