Tryptophan biosynthesis is a critical anabolic pathway in bacteria that starts from chorismate, an intermediate derived from the shikimate pathway. In this process, chorismate is first converted into anthranilate through a reaction with glutamine, catalyzed by anthranilate synthase, which also releases ammonia as a byproduct. Anthranilate is then activated and condensed with phosphoribosyl pyrophosphate (PRPP) to form N-(5'-phosphoribosyl)-anthranilate, which undergoes several enzyme-catalyzed rearrangements and cyclizations to produce indole-3-glycerol phosphate. This intermediate is subsequently cleaved to generate indole, which reacts with serine in a reaction catalyzed by tryptophan synthase to form tryptophan. The pathway highlights the importance of chorismate as a branching point for the biosynthesis of aromatic amino acids, and tryptophan itself serves as a key building block for protein synthesis and a precursor for bioactive molecules like auxins and indole derivatives.

Tryptophan Biosynthesis References