EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.15 | ammonium sulfate | at 1.8 M | Levilactobacillus brevis | |
4.1.1.15 | additional information | sodium glutamate is essential for tetramer formation and its activation | Levilactobacillus brevis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.15 | gene gadB, DNA and amin acid sequence determination and analysis, expression of the His-tagged enzyme in Escherichia coli strains Rosetta-gami B (DE3) ad JM109 | Levilactobacillus brevis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.15 | 1 | - |
L-glutamate | pH 4.6, 37°C, native enzyme | Levilactobacillus brevis | |
4.1.1.15 | 1.4 | - |
L-glutamate | pH 4.6, 37°C, recombinant enzyme | Levilactobacillus brevis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.1.1.15 | 54000 | - |
2 * 54000, inactive, recombinant His-tagged enzyme, SDS-PAGE | Levilactobacillus brevis |
4.1.1.15 | 54000 | - |
4 * 54000, ammonium sulfate-activated, recombinant His-tagged enzyme, SDS-PAGE | Levilactobacillus brevis |
4.1.1.15 | 110000 | - |
recombinant enzyme, pH 7.0, gel filtration | Levilactobacillus brevis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.15 | L-glutamate | Levilactobacillus brevis | - |
4-aminobutanoate + CO2 | - |
? | |
4.1.1.15 | L-glutamate | Levilactobacillus brevis IFO 12005 | - |
4-aminobutanoate + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.15 | Levilactobacillus brevis | A9ZM78 | gene gadB | - |
4.1.1.15 | Levilactobacillus brevis IFO 12005 | A9ZM78 | gene gadB | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.15 | recombinant His-tagged enzyme from Escherichia coli strain Rosetta-gami B (DE3) by nickel affinity chromatography | Levilactobacillus brevis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.15 | L-glutamate | - |
Levilactobacillus brevis | 4-aminobutanoate + CO2 | - |
? | |
4.1.1.15 | L-glutamate | - |
Levilactobacillus brevis IFO 12005 | 4-aminobutanoate + CO2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.15 | dimer | 2 * 54000, inactive, recombinant His-tagged enzyme, SDS-PAGE | Levilactobacillus brevis |
4.1.1.15 | More | sodium glutamate is essential for tetramer formation and its activation | Levilactobacillus brevis |
4.1.1.15 | tetramer | 4 * 54000, ammonium sulfate-activated, recombinant His-tagged enzyme, SDS-PAGE | Levilactobacillus brevis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.15 | GAD | - |
Levilactobacillus brevis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.15 | 30 | - |
native enzyme | Levilactobacillus brevis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.15 | 4.2 | 4.6 | native enzyme | Levilactobacillus brevis |
4.1.1.15 | 4.5 | 5 | recombinant His-tagged enzyme | Levilactobacillus brevis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.15 | pyridoxal 5'-phosphate | - |
Levilactobacillus brevis |