And this glutamate molecule, the amino acid glutamate, essentially is responsible for this catalyzation process from transforming dihydroxy acetone phosphate into another isomer. Now, if we add bromoacetal phosphate, this molecule into the mixture, notice how this is almost exactly the same in structure as this original natural substrate. The only difference is, instead of this hydroxyl group, we have this bromide. And because of that, this will act as a substrate analog and affinity label. And what happens is this carbon here reacts with this oxygen to form a Covalent bond, a Covalent modification, and that kicks off that bromide in the process because we form the Covalent modification that essentially inactivates the active side of that enzyme, the trio's phosphate isomerase. And now this enzyme cannot convert this molecule, the dihydroxy acetone phosphate, into its isomeric form.