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Literature summary for 4.1.1.15 extracted from

  • Lee, J.Y.; Jeon, S.J.
    Characterization and immobilization on nickel-chelated Sepharose of a glutamate decarboxylase A from Lactobacillus brevis BH2 and its application for production of GABA (2014), Biosci. Biotechnol. Biochem., 78, 1656-1661 .
    View publication on PubMed
Search for more literature for 4.1.1.15

Cloned(Commentary)

Cloned (Comment) Organism
gene gadA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3) Levilactobacillus brevis

Protein Variants

Protein Variants Comment Organism
additional information immobilization of recombinant GadA on a nickel affinity Sepharose resin for usage in L-glutamate conversions in a packed-bed reactor, method evaluation. The immobilization yield of GadA on the resin reaches 95.8% when the conditions are as follows: coupling time of 1 h at 25°C in working buffer, containing 50 mM sodium acetate, pH 4.0, 50 mM ammonium sulfate, and 0.1 mM pyridoxal 5'-phosphate, and enzyme loading of 42 mgGadA/g wet resin Levilactobacillus brevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
110000
-
 sedimentation equilibrium analytical centrifugation 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
-
 ir
L-glutamate Levilactobacillus brevis BH2
-
 4-aminobutanoate + CO2
-
 ir

Organism

Organism UniProt Comment Textmining
Levilactobacillus brevis A7UMP3 isolated from traditional Korean fermented food, kimchi
-
Levilactobacillus brevis BH2 A7UMP3 isolated from traditional Korean fermented food, kimchi
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3) by nickel affinity chromatography, elution with imidazol and ammonium szúlfate in the buffer, followed by ultrafiltration and dialysis Levilactobacillus brevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
-
 Levilactobacillus brevis 4-aminobutanoate + CO2
-
 ir
L-glutamate irreversible alpha-decarboxylation of L-glutamate in the presence of a pyridoxal 5'-phosphate (PLP) as coenzyme Levilactobacillus brevis 4-aminobutanoate + CO2
-
 ir
L-glutamate
-
 Levilactobacillus brevis BH2 4-aminobutanoate + CO2
-
 ir
L-glutamate irreversible alpha-decarboxylation of L-glutamate in the presence of a pyridoxal 5'-phosphate (PLP) as coenzyme Levilactobacillus brevis BH2 4-aminobutanoate + CO2
-
 ir

Subunits

Subunits Comment Organism
homodimer 2 * 53000, recombinant His-tagged enzyme, SDS-PAGE Levilactobacillus brevis

Synonyms

Synonyms Comment Organism
GadA
-
 Levilactobacillus brevis
glutamate decarboxylase A
-
 Levilactobacillus brevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 optimum temperature of recombinant free enzyme Levilactobacillus brevis
55
-
 optimum temperature of recombinant immobilized enzyme Levilactobacillus brevis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 the recombinant immobilized enzyme retains about 70% of its initial activity after incubation for 1 h, while the recombinant free enzyme loses all activity Levilactobacillus brevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
 optimum pH of recombinant free and immobilized enzyme Levilactobacillus brevis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Levilactobacillus brevis