1r52A:8-366 1r53A:8-366 1qxoB:1-366 Chorismate synthase catalyzes the last of the seven steps in the shikimate pathway which is used in prokaryotes, fungi and plants for the biosynthesis of aromatic amino acids.

For example, chorismate synthase is known to be essential to the survival of Mycobacterium tuberculosis, making the enzyme an attractive antibiotic target for control of this pathogen.

The active sites for FMN-binding are made up of clusters of flexible loops and the area around these regions have highly positive electromagnetic potential.

There are two histidine residues located at the active site which are thought to protonate the reduced flavin molecule and the leaving phosphate group of the substrate.

[7] Although the chorismate synthase reaction is FMN-dependent, there is no net redox change between substrate and product; the FMN merely acts as a catalyst.