Tryptophan synthase is an enzyme that catalyzes the final two steps of tryptophan biosynthesis, after Phosphoribosyl anthranilate (PRAI) and Indole 3-glycerol-phosphate synthase (IGPS), in that order, catalyze the previous two steps. Many have questioned to what extent these three enzymes interact with each other during tryptophan biosynthesis. To help solve this query, we utilized sequence data to measure amino acid covariation and protein frustration in each enzyme to assess for similarities in residues with those identified in previous NMR studies as functionally important, which could be explained as a potential allosteric network between the proteins in a complex. Our analysis found that there were many similarities between the frustrated contacts, covarying amino acids, and functionally important residues identified in previous NMR studies. This could be explained as a potential allosteric network between the proteins, and warrants further investigation through the use of NMR.
