Nonetheless, 14C and 18O isotopic labeling experiments,[3][4] as well as structural studies,[1][5] support the mechanism shown here.

Most significantly, the central tunnel of pdxJ is hydrophilic in contrast to the hydrophobic central tunnel observed in most TIM barrel proteins, and pdxJ has three extra alpha helices compared to the classical TIM fold.

[7] However, there are also important similarities in function: like many TIM barrel proteins, pdxJ binds its substrates primarily by their phosphate moieties,[1][5] and the phosphate-binding site responsible for binding to HAP and pyridoxine 5'-phosphate is a conserved motif found in many TIM barrel proteins.

In each dimer, an arginine residue Arg20 forms part of the active site in the other monomer, where it helps bind both phosphate groups.

Other names in common use include pyridoxine 5-phosphate phospho lyase, PNP synthase, and PdxJ.

[12] pdxJ and more generally vitamin B6 metabolism in the microbiome have also been shown to alter the effects of certain compounds on animal hosts.