CATH Classification
Level | CATH Code | Description |
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3 | Alpha Beta |
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3.20 | Alpha-Beta Barrel |
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3.20.20 | TIM Barrel |
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3.20.20.70 | Aldolase class I |
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 P00929
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.
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UniProtKB Entries (1)
P00929 |
TRPA_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Tryptophan synthase alpha chain
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PDB Structure
PDB | 4HN4 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states.
Biochemistry
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