It has been shown that the proton comes from the surrounding water and not from an intramolecular shift of a hydrogen atom on the substrates.

Gel filtration experiments reveal that the complex occurs as an α2β2 tetramer under native conditions, and as an αβ dimer under high salt concentrations.

The subunits of anthranilate synthase are encoded by the trpE and trpD genes in E. coli, both of which appear in the trp operon.

[1] This enzyme belongs to the family of lyases, to be specific the oxo-acid-lyases, which cleave carbon-carbon bonds.

This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and two-component system - general.