1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR018204 | Active_site | Tryptophan synthase, alpha chain, active site |
| Type: | Family | Name: | Tryptophan synthase, alpha chain |
| Description: | Tryptophan synthase () catalyzes the last step in the biosynthesisof 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. In Escherichia coli, the 2 subunits, A and B, are encoded by the trpA and trpB genes respectively. The alpha chain is for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate and the beta chain is for the synthesis of tryptophan from indole and serine. In fungi the two domains are fused together in a single multifunctional protein, in the order: (NH2-A-B-COOH) [, ]. The two domains of the Neurospora crassapolypeptide are linked by a connector of 54-amino acid residues that has less than 25% identity to the 45-residue connector of the Saccharomyces cerevisiae(Baker's yeast) polypeptide. Two acidic residues are believed to serve as proton donors/acceptors in the enzyme's catalytic mechanism. | Short Name: | Trp_synthase_suA |
| DB identifier | Type | Name |
|---|---|---|
| IPR018204 | Active_site | Tryptophan synthase, alpha chain, active site |
