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Literature summary for 4.1.1.15 extracted from

  • Fan, E.; Huang, J.; Hu, S.; Mei, L.; Yu, K.
    Cloning, sequencing and expression of a glutamate decarboxylase gene from the GABA-producing strain Lactobacillus brevis CGMCC 1306 (2011), Ann. Microbiol., 62, 689-698.
No PubMed abstract available
Search for more literature for 4.1.1.15

Cloned(Commentary)

Cloned (Comment) Organism
gene gad, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in Escherichia coli strains BL21 and JM109 Levilactobacillus brevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
 x * 53000, recombinant enzyme, SDS-PAGE 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 D6PXK5 gene gad
-
Levilactobacillus brevis CGMCC 1306 D6PXK5 gene gad
-

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
? x * 53000, recombinant enzyme, SDS-PAGE Levilactobacillus brevis

Synonyms

Synonyms Comment Organism
GAD
-
 Levilactobacillus brevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
48
-
-
 Levilactobacillus brevis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
15 65 activity range, profile overview Levilactobacillus brevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.8
-
-
 Levilactobacillus brevis

pH Range

pH Minimum pH Maximum Comment Organism
3 6 activity range, profile overview Levilactobacillus brevis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate binding of pyridoxal 5'-phosphate as well as to the active site residues Thr215 and Asp246 that promote decarboxylation Levilactobacillus brevis

General Information

General Information Comment Organism
additional information binding of pyridoxal 5'-phosphate as well as to the active site residues Thr215 and Asp246 that promote decarboxylation Levilactobacillus brevis