Recombinant E.coli Trp synthase (N-6His)

Recombinant E.coli Tryptophan Synthase is produced by our E.coli expression system and the target gene encoding Met1-Ser268&Thr2-Ile397 is expressed with a 6His tag at the N-terminus. Tryptophan synthase is a multienzyme alpha2beta2 complex composed of two protein subunit. Tryptophan synthase catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyzes cleavage of 3-indole-d-glycerol 3'-phosphate (IGP) to give indole and D-glyceraldehyde 3'-phosphate (G3P). Indole is then transferred through a 25-Å hydrophobic tunnel to the beta-subunit. The beta2 subunit contains pyridoxal 5'-phosphate and catalyzes several pyridoxal 5'-phosphate-dependent reactions, including/3-elimination reactions 6 and a thiol-dependent transamination reaction. This enzyme is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from Animalia. As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target. Protein Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate [The Uniprot Consortium]