×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily Aldolase class I
Functional Family Tryptophan synthase alpha chain

Enzyme Information

4.2.1.20
Tryptophan synthase.
based on mapping to UniProt Q8U094
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)

Q8U094
TRPA_PYRFU
Pyrococcus furiosus DSM 3638
Tryptophan synthase alpha chain

PDB Structure

PDB 2DZU
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structures of mutant tryptophan synthase alpha-subunits from a hyperthermophile, Pyrococcus furiosus
Ogasahara, K., Yamagata, Y., Yutani, K.
To be Published
CATH-Gene3D is a Global Biodata Core Resource Learn more...