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)

P00929
TRPA_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Tryptophan synthase alpha chain

PDB Structure

PDB 4XUG
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of Tryptophan Synthase from Salmonella typhimurium in complex with 2-({[4-(Trifluoromethoxy)Phenyl]Sulfonyl}Amino)Ethyl Dihydrogen Phosphate (F9F) inhibitor in the alpha site and ammonium ion in the metal coordination site.
Hilario, E., Caulkins, B.G., Young, R.P., Niks, D., Dunn, M.F., Mueller, L.J., Fan, L.
To Be Published