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Literature summary for 4.1.1.15 extracted from
- Characterization of glutamate decarboxylase from a high gamma-aminobutyric acid (GABA)-producer, Lactobacillus paracasei (2008), Biosci. Biotechnol. Biochem., 72, 278-285.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene gadB, DNA and amin acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha | Lacticaseibacillus paracasei |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NaCl | 61.5% inhibition at 10 mM | Lacticaseibacillus paracasei |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 5 | - |
L-glutamate | pH 5.0, 37°C | Lacticaseibacillus paracasei | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates to 114% activity at 10 mM | Lacticaseibacillus paracasei | |
| NH4+ | activates to 132% activity at 10 mM | Lacticaseibacillus paracasei | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 57000 | - |
2 * 57000, SDS-PAGE | Lacticaseibacillus paracasei |
| 110000 | - |
gel filtration | Lacticaseibacillus paracasei |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate | Lacticaseibacillus paracasei | - |
4-aminobutanoate + CO2 | - |
? | |
| L-glutamate | Lacticaseibacillus paracasei NFRI 7415 | - |
4-aminobutanoate + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lacticaseibacillus paracasei | B1B389 | gene gadB; gene gadB | - |
| Lacticaseibacillus paracasei NFRI 7415 | B1B389 | gene gadB; gene gadB | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme 27fold from Escherichia coli strain DH5alpha by ammoniumn sulfate fractionation, hydrophobic interaction and anion exchange chromatography | Lacticaseibacillus paracasei |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 16.7 | - |
purified recombinant enzyme | Lacticaseibacillus paracasei |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate | - |
Lacticaseibacillus paracasei | 4-aminobutanoate + CO2 | - |
? | |
| L-glutamate | - |
Lacticaseibacillus paracasei NFRI 7415 | 4-aminobutanoate + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 57000, SDS-PAGE | Lacticaseibacillus paracasei |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GAD | - |
Lacticaseibacillus paracasei |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Lacticaseibacillus paracasei |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 40 | purified recombinant enzyme, stable | Lacticaseibacillus paracasei |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
- |
Lacticaseibacillus paracasei |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 6 | - |
Lacticaseibacillus paracasei |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 6 | purified recombinant enzyme, the enzyme is stable within a pH range of pH 4.5 to pH 5.0, but is unstable below pH 4.0 and above pH 5.5 | Lacticaseibacillus paracasei |
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Release 2023.1 (January 2023)
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