Crystallization (Comment) | Organism |
---|---|
structure and function of alpha subunit, beta subunit, alpha2beta2 complex | Salmonella enterica subsp. enterica serovar Typhimurium |
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 | Organism |
---|---|
pyridoxal 5'-phosphate strongly stabilizes beta2 subunit | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
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 | 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 | 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 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 | 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 |