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 P0A879
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)

P0A879
TRPB_ECOLI
Escherichia coli K-12
Tryptophan synthase beta chain

PDB Structure

PDB 2DH5
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Large conformational changes in the Escherichia coli tryptophan synthase beta(2) subunit upon pyridoxal 5'-phosphate binding
Nishio, K., Ogasahara, K., Morimoto, Y., Tsukihara, T., Lee, S.J., Yutani, K.
Febs J.