CATH Classification

Domain Context

CATH Clusters

Functional Family Tryptophan synthase beta chain

Enzyme Information
Tryptophan synthase.
based on mapping to UniProt P0A2K1
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O.
-!- The alpha-subunit catalyzes the conversion of 1-C-(indol-3- yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was listed formerly as EC -!- The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. -!- In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC, EC, EC and EC -!- In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC -!- That enzyme cannot combine with the alpha unit of EC to form a complex.

UniProtKB Entries (1)

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Tryptophan synthase alpha chain

PDB Structure

External Links
Primary Citation
Allosteric Regulation of Substrate Channeling in Tryptophan Synthase: Modulation of the L-Serine Reaction in Stage I of the Beta-Reaction by Alpha-Site Ligands.
Ngo, H., Kimmich, N., Harris, R., Niks, D., Blumenstein, L., Kulik, V., Barends, T.R., Schlichting, I., Dunn, M.F.