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Literature summary for 4.1.1.15 extracted from
- C-terminal truncation of glutamate decarboxylase from Lactobacillus brevis CGMCC 1306 extends its activity toward near-neutral pH (2012), Enzyme Microb. Technol., 50, 263-269.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | glutamate decarboxylase from Lactobacillus brevis is a very promising candidate for biosynthesis of gamma-aminobutanoate and various other bulk chemicals that can be derived from it. The enzyme mutant with deletion the C-terminal residues can be be useful in a bioreactor for continuous production of gamma-aminobutanoate | Levilactobacillus brevis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene gad, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Levilactobacillus brevis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| more | | deletion the C-terminal residues of GAD to generate a mutant, designated as GADDELTAC, which exhibits extended activity toward near-neutral pH compared to the wild-type. The microenvironment of the mutant active site is changed, the substrate entrance of the mutant is probably enlarged, homology modeling, overview. The enzyme deletion mutant GADDELTAC exhibits 4.8fold higher activity at pH 6.0 compared to the wild-type enzyme | Levilactobacillus brevis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Levilactobacillus brevis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 57000 | - |
1 * 57000, about, sequence calculation | Levilactobacillus brevis |
| 57200 | - |
gel filtration, recombinant enzyme | 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 CGMCC 1306 | - |
4-aminobutanoate + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Levilactobacillus brevis | - |
- |
- |
| Levilactobacillus brevis CGMCC 1306 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatograpyh | 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 CGMCC 1306 | 4-aminobutanoate + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 57000, about, sequence calculation | Levilactobacillus brevis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GAD | - |
Levilactobacillus brevis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4.8 | - |
wild-type and C-terminal deletion mutant enzymes | Levilactobacillus brevis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
the deletion mutant GADDELTAC is more active above pH 5.6. At pH 6.0, the mutant enzyme still retains 12% of its maximum activity while the wild-type enzyme almost loses all its activity. The enzyme deletion mutant GADDELTAC exhibits 4.8fold higher activity at pH 6.0 compared to the wild-type enzyme | Levilactobacillus brevis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | the pyridine ring of pyridoxal 5'-phosphate is sandwiched between residues Ala248 and Gln166. Residues Lys279 and His278 are required for the binding of cofactor pyridoxal 5'-phosphate to form a Schiff base as in many other pyridoxal 5'-phosphate-dependent enzymes | Levilactobacillus brevis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | important role of C-terminal region in the pH-dependent regulation of enzyme activity. Enzyme molecular homology modeling | Levilactobacillus brevis |
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