Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.1.15 extracted from

  • Shin, S.M.; Kim, H.; Joo, Y.; Lee, S.J.; Lee, Y.J.; Lee, S.J.; Lee, D.W.
    Characterization of glutamate decarboxylase from Lactobacillus plantarum and its C-terminal function for the pH dependence of activity (2014), J. Agric. Food Chem., 62, 12186-12193 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene gadB, sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3). The expression level of both truncated mutants in Escherichia coli at 25°C is much higher than that at 37°C Lactiplantibacillus plantarum subsp. plantarum

Protein Variants

Protein Variants Comment Organism
additional information generation of C-terminally truncated (DELTA3 and DELTA11 residues) mutants, their enzyme activities are compared with that of the wild-type enzyme at different pH values. Unlike the wild-type GAD, the mutants show pronounced catalytic activity in a broad pH range of 4.0-8.0, suggesting that the C-terminal region is involved in the pH dependence of GAD activity Lactiplantibacillus plantarum subsp. plantarum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Lactiplantibacillus plantarum subsp. plantarum
22.8
-
L-glutamate pH 5.0, 37°C, recombinant wild-type enzyme Lactiplantibacillus plantarum subsp. plantarum
33.8
-
L-glutamate pH 5.0, 37°C, recombinant enzyme mutant DELTA11 Lactiplantibacillus plantarum subsp. plantarum
122.1
-
L-glutamate pH 7.0, 37°C, recombinant wild-type enzyme Lactiplantibacillus plantarum subsp. plantarum
137.1
-
L-glutamate pH 7.0, 37°C, recombinant enzyme mutant DELTA11 Lactiplantibacillus plantarum subsp. plantarum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate Lactiplantibacillus plantarum subsp. plantarum
-
4-aminobutanoate + CO2
-
?
L-glutamate Lactiplantibacillus plantarum subsp. plantarum ATCC 14917 / JCM 1149 / CGMCC 1.2437
-
4-aminobutanoate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Lactiplantibacillus plantarum subsp. plantarum D7VEX3
-
-
Lactiplantibacillus plantarum subsp. plantarum ATCC 14917 / JCM 1149 / CGMCC 1.2437 D7VEX3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage through thrombin, and dialysis, followed by gel filtration Lactiplantibacillus plantarum subsp. plantarum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
-
Lactiplantibacillus plantarum subsp. plantarum 4-aminobutanoate + CO2
-
?
L-glutamate
-
Lactiplantibacillus plantarum subsp. plantarum ATCC 14917 / JCM 1149 / CGMCC 1.2437 4-aminobutanoate + CO2
-
?

Synonyms

Synonyms Comment Organism
GAD
-
Lactiplantibacillus plantarum subsp. plantarum
GadB
-
Lactiplantibacillus plantarum subsp. plantarum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
Lactiplantibacillus plantarum subsp. plantarum

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 60 over 60% activity within this range Lactiplantibacillus plantarum subsp. plantarum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70 90 the recombinant enzyme with a thermal half-life of 46 min at 90°C retains approximately 70% of initial activity after incubation at 70°C for 9 h, whereas the enzyme is rapidly inactivated at 100°C Lactiplantibacillus plantarum subsp. plantarum
90
-
irreversible thermal unfolding of the purified recombinant detagged enzyme Lactiplantibacillus plantarum subsp. plantarum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.015
-
L-glutamate pH 7.0, 37°C, recombinant wild-type enzyme Lactiplantibacillus plantarum subsp. plantarum
0.485
-
L-glutamate pH 7.0, 37°C, recombinant enzyme mutant DELTA11 Lactiplantibacillus plantarum subsp. plantarum
21.75
-
L-glutamate pH 5.0, 37°C, recombinant wild-type enzyme Lactiplantibacillus plantarum subsp. plantarum
40.25
-
L-glutamate pH 5.0, 37°C, recombinant enzyme mutant DELTA11 Lactiplantibacillus plantarum subsp. plantarum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
Lactiplantibacillus plantarum subsp. plantarum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Lactiplantibacillus plantarum subsp. plantarum

General Information

General Information Comment Organism
additional information the GAD C-terminal region (Ile454-Thr468) plays an important role in the pH dependence of catalysis. Homology modeling of GAD Lactiplantibacillus plantarum subsp. plantarum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00012
-
L-glutamate pH 7.0, 37°C, recombinant wild-type enzyme Lactiplantibacillus plantarum subsp. plantarum
0.0035
-
L-glutamate pH 7.0, 37°C, recombinant enzyme mutant DELTA11 Lactiplantibacillus plantarum subsp. plantarum
0.954
-
L-glutamate pH 5.0, 37°C, recombinant wild-type enzyme Lactiplantibacillus plantarum subsp. plantarum
1.19
-
L-glutamate pH 5.0, 37°C, recombinant enzyme mutant DELTA11 Lactiplantibacillus plantarum subsp. plantarum