[3] The reactions catalyzed by these two types of riboflavin synthase proceed via "enantiomeric" intermediates.

[3] Two 6,7-dimethyl-8-ribityllumazine (synthesized by lumazine synthase) molecules are hydrogen bound to each monomer as the two domains are topologically similar.

Of the dyad, His102 is from the N-barrel and Thr148 is from the C-barrel, highlighting the importance of the proximity of the two subunits of the enzyme in the early stages of the reaction.

Interestingly, archeal riboflavin synthase creates an "enantiomeric" intermediate as opposed to eubacterial, fungal and plant riboflavin synthase, where the attack of one molecule proceeds from the opposite face compared to the other enzyme.

[3] Scientists have hypothesized that enzymes involved in the riboflavin biosynthesis pathway, including riboflavin synthase, can be used to develop antibacterial drugs in order to treat infections caused by Gram-negative bacteria and yeasts.

This hypothesis is based on the inability of Gram-negative bacteria, such as E. coli and S. typhimurium, to uptake riboflavin from the external environment.