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Literature summary for 4.1.1.15 extracted from
- Study on oligomerization of glutamate decarboxylase from Lactobacillus brevis using asymmetrical flow field-flow fractionation (AF4) with light scattering techniques (2018), Anal. Bioanal. Chem., 410, 451-458 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene gad, DNA and amino acid sequence determination and analysis, the protein sequence is identical to the LbGadB of the strain ATCC 367, recombinant expression of His-tagged enzyme in Escherichia coli strain Origami 2 (DE3) | Levilactobacillus brevis |
General Stability
| General Stability | Organism |
|---|---|
| the hexameric form of LbGadB is most stable at pH 6 and in presence of NaCl or KCl | Levilactobacillus brevis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
asymmetrical flow field-flow fractionation (AF4) coupled with UV/Vis, multi-angle light scattering (MALS), and differential refractive index (dRI) detectors (AF4-UV-MALS-dRI) is employed for analysis of glutamate decarboxylase molecular weight and aggregation | Levilactobacillus brevis |
| 110000 | - |
dimeric enzyme, AF4-UV-MALS-dRI and molecular modeling | Levilactobacillus brevis |
| 330000 | - |
hexameric enzyme, molecular modeling | Levilactobacillus brevis |
| 350000 | - |
hexameric enzyme, AF4-UV-MALS-dRI | Levilactobacillus brevis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate | Levilactobacillus brevis | - |
4-aminobutanoate + CO2 | - |
? |  |
| L-glutamate | Levilactobacillus brevis DSM 1269 | - |
4-aminobutanoate + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Levilactobacillus brevis | A0A1U9Y677 | the protein sequence is identical to the LbGadB of the strain ATCC 367 | - |
| Levilactobacillus brevis DSM 1269 | A0A1U9Y677 | the protein sequence is identical to the LbGadB of the strain ATCC 367 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme of Escherichia coli strain Origami 2 (DE3) by nickel affinity chromatography and dialysis | Levilactobacillus brevis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamate | - |
Levilactobacillus brevis | 4-aminobutanoate + CO2 | - |
? | |
| L-glutamate | - |
Levilactobacillus brevis DSM 1269 | 4-aminobutanoate + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 54500, recombinant enzyme, SDS-PAGE | Levilactobacillus brevis |
| hexamer | - |
Levilactobacillus brevis |
| More | asymmetrical flow field-flow fractionation (AF4) provides molecular weight (MW) (or size)-based separation of dimer, hexamer, and aggregates of LbGadB, molecular modeling | Levilactobacillus brevis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GAD | - |
Levilactobacillus brevis |
| LbGadB | - |
Levilactobacillus brevis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Levilactobacillus brevis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | structure molecular modeling | Levilactobacillus brevis |
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Release 2023.1 (January 2023)
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