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Literature summary extracted from
- Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima (2000), Structure, 8, 265-276.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.3.1.24 | cloning of trpF mutants, expression in Escherichia coli BL21(DE3) | Thermotoga maritima |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.3.1.24 | mutationally generated monomeric PRA isomerase, comparison to PRAI dimer | Thermotoga maritima |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.3.1.24 | D126N/C7A | catalytically inactive double mutant | Thermotoga maritima |
| 5.3.1.24 | 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
| EC Number | General Stability | Organism |
|---|---|---|
| 5.3.1.24 | extremely stable enzyme | Thermotoga maritima |
| 5.3.1.24 | extremely stable towards proteolytic attack | Thermotoga maritima |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.1.24 | 0.00028 | - |
N-(5-phospho-beta-D-ribosyl)anthranilate | pH 7.5, 25°C, dimer | Thermotoga maritima |  |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.24 | additional information | - |
MWs of PRAI variants | Thermotoga maritima |
| 5.3.1.24 | 23040 | - |
2 * 23040, calculated from the amino acid sequence | Thermotoga maritima |
| 5.3.1.24 | 30200 | - |
dimer, gel filtration | Thermotoga maritima |
| 5.3.1.24 | 49600 | - |
dimer, sedimentation equilibrium analysis | Thermotoga maritima |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.24 | N-(5-phospho-beta-D-ribosyl)anthranilate | Thermotoga maritima | fourth step in tryptophan biosynthesis | 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.1.24 | Thermotoga maritima | - |
monofunctional enzyme | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.3.1.24 | mutationally generated monomeric PRA isomerase | Thermotoga maritima |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.24 | additional information | - |
values for PRAI variants | Thermotoga maritima |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.24 | N-(5-phospho-beta-D-ribosyl)anthranilate | enzyme structure | Thermotoga maritima | 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate | - |
? | |
| 5.3.1.24 | N-(5-phospho-beta-D-ribosyl)anthranilate | fourth step in tryptophan biosynthesis | Thermotoga maritima | 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.3.1.24 | homodimer | 2 * 23040, calculated from the amino acid sequence | Thermotoga maritima |
| 5.3.1.24 | 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]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.24 | 25 | - |
assay at | Thermotoga maritima |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.24 | additional information | - |
extremely thermostable | Thermotoga maritima |
| 5.3.1.24 | additional information | - |
mutationally generated monomers of PRAI are as active as the dimer, but far more thermolabile | Thermotoga maritima |
| 5.3.1.24 | 85 | - |
monomeric variants, half-life: 3-5 min | Thermotoga maritima |
| 5.3.1.24 | 85 | - |
dimer, half-life: 310 min | Thermotoga maritima |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.1.24 | additional information | - |
additional information | values for PRAI variants | Thermotoga maritima | |
| 5.3.1.24 | 3.7 | - |
N-(5-phospho-beta-D-ribosyl)anthranilate | pH 7.5, 25°C, dimer | Thermotoga maritima | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.24 | 7.5 | - |
assay at | Thermotoga maritima |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.3.1.24 | additional information | - |
extremely stable towards acidic pH | Thermotoga maritima |
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