| Type: | Conserved_site | Name: | Tryptophan synthase, beta chain, conserved site |
| Description: | Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan [, ]:L-serine + 1-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O It has two functional domains, each found in bacteria and plants on a separate subunit: alpha chain () is for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate and beta chain is for the synthesis of tryptophan fromindole and serine. In fungi the two domains are fused together on a single multifunctional protein [].The beta chain of the enzyme, represented here, requires pyridoxal-phosphate as a cofactor. The pyridoxal-phosphate group is attached to a lysine residue. The region around this lysine residue also contains two histidine residues which are part of the pyridoxal-phosphate binding site. | Short Name: | Trp_synth_b_CS |
