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Literature summary for 4.1.1.15 extracted from
- Characterization of glutamate decarboxylase (GAD) from Lactobacillus sakei A156 isolated from Jeot-gal (2015), J. Microbiol. Biotechnol., 25, 696-703 .
Application
| Application | Comment | Organism |
|---|---|---|
| food industry | Lactobacillus sakei strain A156 and its gadB gene might be useful when GABA-enriched foods are attempted to be produced, serving as a source of strain and gene | Latilactobacillus sakei |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene gadB, DNA and amino acid sequence determination and analysis, sequence comparisons, operon structure of gadCB, RT-PCR expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3). The gadC gene is amplified from the genomic DNA by using a primer set based on gadC from Lactobacillus brevis strain ATCC 367 | Latilactobacillus sakei |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| (NH4)2SO4 | 92% inhibition at 2 mM | Latilactobacillus sakei |  |
| AgNO3 | 79% inhibition at 2 mM | Latilactobacillus sakei | |
| MgCl2 | 84% inhibition at 2 mM | Latilactobacillus sakei | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 16 | - |
L-glutamate | pH 4.5, 37°C, recombinant His-tagged enzyme | Latilactobacillus sakei | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| CaCl2 | activates to 113% activity at 2 mM | Latilactobacillus sakei | |
| CoCl2 | activates to 118% activity at 2 mM | Latilactobacillus sakei | |
| MnCl2 | activates to 152% activity at 2 mM | Latilactobacillus sakei | |
| ZnCl2 | activates to 115% activity at 2 mM | Latilactobacillus sakei | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate | Latilactobacillus sakei | - |
4-aminobutanoate + CO2 | - |
? | |
| L-glutamate | Latilactobacillus sakei A156 | - |
4-aminobutanoate + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Latilactobacillus sakei | A0A0D3R1A0 | isolated from Jeot-gal, a Korean fermented seafood | - |
| Latilactobacillus sakei A156 | A0A0D3R1A0 | isolated from Jeot-gal, a Korean fermented seafood | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Latilactobacillus sakei |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
Lactobacillus sakei strain A156 produces 15.81 mg GABA per ml culture supernatant as determined by GABase assay | Latilactobacillus sakei |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate | - |
Latilactobacillus sakei | 4-aminobutanoate + CO2 | - |
? | |
| L-glutamate | - |
Latilactobacillus sakei A156 | 4-aminobutanoate + CO2 | - |
? | |
| additional information | enzyme activity determination by GABase assay, overview | Latilactobacillus sakei | ? | - |
? | |
| additional information | enzyme activity determination by GABase assay, overview | Latilactobacillus sakei A156 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 53540, sequence calculation, x * 54400, recombinant His-tagged enzyme, SDS-PAGE | Latilactobacillus sakei |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GAD | - |
Latilactobacillus sakei |
| GadB | - |
Latilactobacillus sakei |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
recombinant His-tagged enzyme | Latilactobacillus sakei |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
recombinant His-tagged enzyme | Latilactobacillus sakei |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | the GAD from Lactobacillus sakei strain A156 contains a highly conserved catalytic domain that belongs to the pyridoxal 5'-phosphate-dependent decarboxylase superfamily. The domain includes a lysine residue essential for pyridoxal 5'-phosphate binding, designated as PLP lysine | Latilactobacillus sakei | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Latilactobacillus sakei | sequence calculation | - |
4.91 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the GAD from Lactobacillus sakei strain A156 contains a highly conserved catalytic domain that belongs to the pyridoxal 5'-phosphate-dependent decarboxylase superfamily. The domain includes a lysine residue essential for pyridoxal 5'-phosphate binding, designated as PLP lysine | Latilactobacillus sakei |
| physiological function | enzyme GAD is involved in the maintainence of the cellular pH near neutral values under the acidic environments and its role is especially important for lactic acid bacteria (LAB) | Latilactobacillus sakei |
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