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Literature summary for 4.1.1.15 extracted from
- Expanding the active pH range of Escherichia coli glutamate decarboxylase by breaking the cooperativeness (2013), J. Biosci. Bioeng., 115, 154-158.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene gad, cloning in Escherichia coli strain DH5alpha, overexpression of His-tagged wild-type and mutant in Escherichia coli strain BL21(DE3) | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E89A | site-directed mutagenesis | Escherichia coli |
| E89A/H465A | site-directed mutagenesis, the double mutation not only brakes the cooperativity in the activity change but also yields a mutant enzyme that retains the activity at neutral pH. The resulting mutant enzyme, that is active at neutral pH, inhibits the cell growth in a glycerol medium by converting intracellular Glu into 4-aminobutanoate in an uncontrolled manner | Escherichia coli |
| E89Q | site-directed mutagenesis, double mutation Glu89Gln/DELTA452-466 strongly inhibits the cell growth and shows higher activity than mutant Glu89Gln/His465Ala | Escherichia coli |
| E89Q/H465A | site-directed mutagenesis, the double mutation not only brakes the cooperativity in the activity change but also yields a mutant enzyme that retains the activity at neutral pH. The resulting mutant enzyme, that is active at neutral pH, inhibits the cell growth in a glycerol medium by converting intracellular Glu into 4-aminobutanoate in an uncontrolled manner | Escherichia coli |
| H465A | site-directed mutagenesis | Escherichia coli |
| additional information | expanding the active pH range of the enzyme by breaking the cooperativeness | Escherichia coli |
| additional information | generation of a DELTA452-466 deletion mutant, the mutant can convert glycerol into 4-aminobutanoate with minimal growth inhibition to maximize its space-time yield. Double mutation Glu89Gln/DELTA452-466 strongly inhibits the cell growth and shows higher activity than mutant Glu89Gln/His465Ala | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | cooperativeness is kept intact by residues Glu89 and His465 in the cooperativity system of GAD | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate | Escherichia coli | - |
4-aminobutanoate + CO2 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate | - |
Escherichia coli | 4-aminobutanoate + CO2 | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Escherichia coli | |
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Release 2023.1 (January 2023)
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