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Literature summary for 5.4.3.9 extracted from
- Glutamate 2,3-aminomutase: a new member of the radical SAM superfamily of enzymes (2007), Biochim. Biophys. Acta, 1774, 286-296.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene eam, DNA and amio acid sequence determination and analysis, functional expression in Escherichia coli BL21 (DE3) CodonPlus RILP cells | Clostridioides difficile |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| O2 | glutamate-specific 2,3-aminomutases is sensitive to molecular oxygen which oxidizes the [4Fe-4S]1+ cluster required for catalysis to [4Fe4S]2+ | Clostridioides difficile |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | required, iron-sulfide cluster [4Fe-4S], the iron-sulfur cluster in glutamate 2,3-aminomutase is labile duirng purification | Clostridioides difficile | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-glutamate | Clostridioides difficile | - |
3-aminopentanedioate | - |
? | |
| L-glutamate | Clostridioides difficile | - |
3-aminopentanedioate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridioides difficile | - |
gene eam | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli by ammonium sulfate fractuionation, hydrophobic interaction chromatography, anion exchange chromatography, another step of ammonium sulfate fractionation, centrifugation, and gel filtration | Clostridioides difficile |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-glutamate | - |
Clostridioides difficile | 3-aminopentanedioate | - |
? | |
| L-glutamate | - |
Clostridioides difficile | 3-aminopentanedioate | - |
? | |
| additional information | no activity with L-lysine by the recombinant enzyme | Clostridioides difficile | ? | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Clostridioides difficile |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Clostridioides difficile |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | enzyme-bound, one molecule per subunit | Clostridioides difficile | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | glutamate 2,3-aminomutase is a member of the radical SAM superfamily of enzymes. The highly active glutamate 2,3-aminomutase that is homologous with lysine 2,3-aminomutase | Clostridioides difficile |
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