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Literature summary extracted from

  • Sa, H.D.; Park, J.Y.; Jeong, S.J.; Lee, K.W.; Kim, J.H.
    Characterization of glutamate decarboxylase (GAD) from Lactobacillus sakei A156 isolated from Jeot-gal (2015), J. Microbiol. Biotechnol., 25, 696-703 .
    View publication on PubMed

Application

EC Number Application Comment Organism
4.1.1.15 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)

EC Number Cloned (Comment) Organism
4.1.1.15 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

EC Number Inhibitors Comment Organism Structure
4.1.1.15 (NH4)2SO4 92% inhibition at 2 mM Latilactobacillus sakei
4.1.1.15 AgNO3 79% inhibition at 2 mM Latilactobacillus sakei
4.1.1.15 MgCl2 84% inhibition at 2 mM Latilactobacillus sakei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.15 16
-
L-glutamate pH 4.5, 37°C, recombinant His-tagged enzyme Latilactobacillus sakei

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.15 CaCl2 activates to 113% activity at 2 mM Latilactobacillus sakei
4.1.1.15 CoCl2 activates to 118% activity at 2 mM Latilactobacillus sakei
4.1.1.15 MnCl2 activates to 152% activity at 2 mM Latilactobacillus sakei
4.1.1.15 ZnCl2 activates to 115% activity at 2 mM Latilactobacillus sakei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.15 L-glutamate Latilactobacillus sakei
-
4-aminobutanoate + CO2
-
?
4.1.1.15 L-glutamate Latilactobacillus sakei A156
-
4-aminobutanoate + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.15 Latilactobacillus sakei A0A0D3R1A0 isolated from Jeot-gal, a Korean fermented seafood
-
4.1.1.15 Latilactobacillus sakei A156 A0A0D3R1A0 isolated from Jeot-gal, a Korean fermented seafood
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.15 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Latilactobacillus sakei

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.15 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.15 L-glutamate
-
Latilactobacillus sakei 4-aminobutanoate + CO2
-
?
4.1.1.15 L-glutamate
-
Latilactobacillus sakei A156 4-aminobutanoate + CO2
-
?
4.1.1.15 additional information enzyme activity determination by GABase assay, overview Latilactobacillus sakei ?
-
?
4.1.1.15 additional information enzyme activity determination by GABase assay, overview Latilactobacillus sakei A156 ?
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.15 ? x * 53540, sequence calculation, x * 54400, recombinant His-tagged enzyme, SDS-PAGE Latilactobacillus sakei

Synonyms

EC Number Synonyms Comment Organism
4.1.1.15 GAD
-
Latilactobacillus sakei
4.1.1.15 GadB
-
Latilactobacillus sakei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.15 55
-
recombinant His-tagged enzyme Latilactobacillus sakei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.15 5
-
recombinant His-tagged enzyme Latilactobacillus sakei

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.15 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

EC Number Organism Comment pI Value Maximum pI Value
4.1.1.15 Latilactobacillus sakei sequence calculation
-
4.91

General Information

EC Number General Information Comment Organism
4.1.1.15 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
4.1.1.15 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