Any feedback?
Literature summary for 4.2.1.20 extracted from
- Tryptophan synthase, structure, function, and protein engineering (1995), Subcell. Biochem., 24, 207-254.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structure and function of alpha subunit, beta subunit, alpha2beta2 complex | Salmonella enterica subsp. enterica serovar Typhimurium |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D60Y | mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling | Salmonella enterica subsp. enterica serovar Typhimurium |
| E109A | catalytic activity with beta-chloro-L-Ala, but negligible activity with L-Ser, beta subunit | Salmonella enterica subsp. enterica serovar Typhimurium |
| E109D | catalytic activity with beta-chloro-L-Ala, but reduced activity with L-Ser, beta subunit | Salmonella enterica subsp. enterica serovar Typhimurium |
| E49F | mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling | Salmonella enterica subsp. enterica serovar Typhimurium |
| G281R | reduced activity and weak association with alpha subunit | Escherichia coli |
| G51L | mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling | Salmonella enterica subsp. enterica serovar Typhimurium |
| K87T | Lys87 represents an essential catalytic residue as acceptor of the alpha-proton of L-Ser, alpha subunit | Salmonella enterica subsp. enterica serovar Typhimurium |
| P132A | increase of activity of the alpha2beta2 complex | Escherichia coli |
| P132G | increase of activity of the alpha2beta2 complex | Escherichia coli |
| P57A | increase of activity of the alpha2beta2 complex | Escherichia coli |
| R179L | mutation inhibits the ligand-induced transition of the alpha subunit from an open to a closed conformation that serves to block the tunnel for the metabolite chanelling | Salmonella enterica subsp. enterica serovar Typhimurium |
General Stability
| General Stability | Organism |
|---|---|
| pyridoxal 5'-phosphate strongly stabilizes beta2 subunit | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | mechanism | Salmonella enterica subsp. enterica serovar Typhimurium | |
| L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | mechanism | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1-(indol-3-yl)glycerol 3-phosphate + L-serine | - |
Salmonella enterica subsp. enterica serovar Typhimurium | L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
? |  |
| 1-(indol-3-yl)glycerol 3-phosphate + L-serine | - |
Escherichia coli | L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
| indole + D-glyceraldehyde 3-phosphate | r | Salmonella enterica subsp. enterica serovar Typhimurium | indole-3-glycerol phosphate | r | ? | |
| indole + D-glyceraldehyde 3-phosphate | r | Escherichia coli | indole-3-glycerol phosphate | r | ? | |
| indole + L-serine | - |
Salmonella enterica subsp. enterica serovar Typhimurium | L-tryptophan + H2O | - |
? | |
| indole + L-serine | - |
Escherichia coli | L-tryptophan + H2O | - |
? | |
| indole-3-glycerol phosphate | r | Salmonella enterica subsp. enterica serovar Typhimurium | indole + D-glyceraldehyde 3-phosphate | r | ? | |
| indole-3-glycerol phosphate | r | Escherichia coli | indole + D-glyceraldehyde 3-phosphate | r | ? | |
| indole-3-glycerol phosphate | mechanism | Salmonella enterica subsp. enterica serovar Typhimurium | indole + D-glyceraldehyde 3-phosphate | r | ? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | activities of alpha and beta subunits are coordinated by allosteric interactions | Salmonella enterica subsp. enterica serovar Typhimurium |
| More | activities of alpha and beta subunits are coordinated by allosteric interactions | Escherichia coli |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
pyridoxal 5'-phosphate stabilizes against thermal inactivation, Schiff-base forming amino acids destabilize holo beta subunit | Escherichia coli |
| additional information | - |
ligands that promote subunit association (L-Ser, L-Trp, D-Trp) raise the inactivation temperature of alpha subunit | Salmonella enterica subsp. enterica serovar Typhimurium |
| additional information | - |
denaturation temperatures of alpha subunit | Salmonella enterica subsp. enterica serovar Typhimurium |
| additional information | - |
denaturation temperatures of alpha subunit | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Escherichia coli | |
| pyridoxal 5'-phosphate | forms a Schiff base with the epsilon amino-group of Lys87 | Salmonella enterica subsp. enterica serovar Typhimurium | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
