Cloned (Comment) | Organism |
---|---|
cloning of trpF mutants, expression in Escherichia coli BL21(DE3) | Thermotoga maritima |
Crystallization (Comment) | Organism |
---|---|
mutationally generated monomeric PRA isomerase, comparison to PRAI dimer | Thermotoga maritima |
Protein Variants | Comment | Organism |
---|---|---|
D126N/C7A | catalytically inactive double mutant | Thermotoga maritima |
additional information | mutationally generated monomers of dimeric PRAI are as active as the dimer, but far more thermolabile, Pro-52/Phe-53 deletion mutant and mutants with multiple point mutations | Thermotoga maritima |
General Stability | Organism |
---|---|
extremely stable enzyme | Thermotoga maritima |
extremely stable towards proteolytic attack | Thermotoga maritima |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00028 | - |
N-(5-phospho-beta-D-ribosyl)anthranilate | pH 7.5, 25°C, dimer | Thermotoga maritima |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
additional information | - |
MWs of PRAI variants | Thermotoga maritima |
23040 | - |
2 * 23040, calculated from the amino acid sequence | Thermotoga maritima |
30200 | - |
dimer, gel filtration | Thermotoga maritima |
49600 | - |
dimer, sedimentation equilibrium analysis | Thermotoga maritima |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-(5-phospho-beta-D-ribosyl)anthranilate | Thermotoga maritima | fourth step in tryptophan biosynthesis | 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | - |
monofunctional enzyme | - |
Purification (Comment) | Organism |
---|---|
mutationally generated monomeric PRA isomerase | Thermotoga maritima |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
values for PRAI variants | Thermotoga maritima |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-(5-phospho-beta-D-ribosyl)anthranilate | enzyme structure | Thermotoga maritima | 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate | - |
? | |
N-(5-phospho-beta-D-ribosyl)anthranilate | fourth step in tryptophan biosynthesis | Thermotoga maritima | 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 23040, calculated from the amino acid sequence | Thermotoga maritima |
homodimer | 2 identical (betaalpha)8-barrel subunits, which are associated back-to-back and locked together by a hydrophobic loop | Thermotoga maritima |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Thermotoga maritima |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
extremely thermostable | Thermotoga maritima |
additional information | - |
mutationally generated monomers of PRAI are as active as the dimer, but far more thermolabile | Thermotoga maritima |
85 | - |
monomeric variants, half-life: 3-5 min | Thermotoga maritima |
85 | - |
dimer, half-life: 310 min | Thermotoga maritima |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | values for PRAI variants | Thermotoga maritima | |
3.7 | - |
N-(5-phospho-beta-D-ribosyl)anthranilate | pH 7.5, 25°C, dimer | Thermotoga maritima |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Thermotoga maritima |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
extremely stable towards acidic pH | Thermotoga maritima |