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CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.1100
Functional Family Tryptophan synthase beta chain 1

Enzyme Information

4.2.1.20
Tryptophan synthase.
based on mapping to UniProt P50383
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)

P50383
TRPB1_SACS2
Saccharolobus solfataricus P2
Tryptophan synthase beta chain 1

PDB Structure

PDB 6HUL
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Evolutionary Morphing of Tryptophan Synthase: Functional Mechanisms for the Enzymatic Channeling of Indole.
Fleming, J.R., Schupfner, M., Busch, F., Basle, A., Ehrmann, A., Sterner, R., Mayans, O.
J.Mol.Biol.
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