CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.1100
Functional Family Tryptophan synthase beta chain

Enzyme Information

4.2.1.20
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 4.1.2.8). -!- 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 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 5.3.1.24. -!- 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 4.2.1.122). -!- That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex.

UniProtKB Entries (1)

P0A2K1
TRPB_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Tryptophan synthase beta chain

PDB Structure

PDB 1K8X
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
On the Role of AlphaThr183 in the Allosteric Regulation and Catalytic Mechanism of Tryptophan Synthase
Kulik, V., Weyand, M., Siedel, R., Niks, D., Arac, D., Dunn, M.F., Schlichting, I.
J.Mol.Biol.