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Information on EC 4.1.1.15 - glutamate decarboxylase and Organism(s) Levilactobacillus brevis and UniProt Accession Q03U69
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4.1.1.15 glutamate decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein. The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.
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Word Map
- 4.1.1.15
-
gabaergic
-
gamma-aminobutyric
- autoimmune
- autoantibody
- islet
- mellitus
-
neurotransmitter
- synaptic
- hippocampus
-
interneurons
- cortical
- autoantigens
- choline
-
excitatory
-
dorsal
- striatum
-
insulin-dependent
-
ventral
- seizure
- parvalbumin
- epilepsy
- beta-cell
-
cholinergic
-
glutamatergic
- synapses
-
medial
-
neurotransmission
-
neurochemical
-
substantia
-
afferent
-
postsynaptic
- c-peptide
-
somata
-
chat
-
presynaptic
-
antibody-positive
-
autoreactive
- ketoacidosis
- bicuculline
- gaba-transaminase
- colliculus
-
preoptic
- gaba-t
-
calretinin
-
rostral
- muscimol
-
boutons
- reelin
- calbindin
- analysis
- synthesis
- pharmacology
- nutrition
- medicine
- food industry
- diagnostics
-
glycinergic
The taxonomic range for the selected organisms is: Levilactobacillus brevis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
glutamic acid decarboxylase, gad65, gad67, glutamate decarboxylase, glutamic acid decarboxylase 65, glutamic acid decarboxylase 67, gad-65, gad-67, glutamate decarboxylase 67, l-glutamate decarboxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
65 kDa glutamic acid decarboxylase
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-
-
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67 kDa glutamic acid decarboxylase
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-
-
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Aspartate 1-decarboxylase
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-
-
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Aspartic alpha-decarboxylase
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-
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Cysteic acid decarboxylase
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-
-
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Decarboxylase, glutamate
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-
-
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ERT D1
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-
-
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GAD
GAD-65
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-
-
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GAD-67
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-
-
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GAD-alpha
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-
-
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GAD-beta
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-
-
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GAD-gamma
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-
-
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GadB
GADCase
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-
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gamma-Glutamate decarboxylase
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-
-
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GDCase
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-
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Glutamic acid decarboxylase
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-
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Glutamic decarboxylase
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-
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L-Aspartate-alpha-decarboxylase
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-
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L-Glutamate alpha-decarboxylase
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-
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L-Glutamate decarboxylase
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L-Glutamic acid decarboxylase
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L-Glutamic decarboxylase
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-
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MGAD
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-
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GAD
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-glutamate 1-carboxy-lyase (4-aminobutanoate-forming)
A pyridoxal-phosphate protein. The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.
CAS REGISTRY NUMBER
COMMENTARY
9024-58-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutamate
4-aminobutanoate + CO2
the alpha-carboxyl group, leaving as CO2, is thus replaced by a cytoplasmic proton, yielding 4-aminobutanoate
-
-
?
L-glutamate
4-aminobutanoate + CO2
the alpha-carboxyl group, leaving as CO2, is replaced by a cytoplasmic proton, yielding 4-aminobutanoate
-
-
?
L-glutamate
4-aminobutanoate + CO2
irreversible alpha-decarboxylation of L-glutamate in the presence of a pyridoxal 5'-phosphate (PLP) as coenzyme
-
-
ir
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
binding of pyridoxal 5'-phosphate as well as to the active site residues Thr215 and Asp246 that promote decarboxylation
pyridoxal 5'-phosphate
residue K279 is essential for cofactor binding
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
no effect on activity by NaCl, MgCl2, and MnCl2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
sodium glutamate is essential for tetramer formation and its activation
-
additional information
-
sodium glutamate is essential for tetramer formation and its activation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics
-
1.9
L-glutamate
-
recombinant enzyme, in acetate buffer (20 mM, pH 4.8), at 40°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.3 - 5.8
-
pH 3.3: about 20% of maximal activity, pH 3.5: about 65% of maximal activity, pH 5.2: about 55% of maximal activity, pH 5.8: about 20% of maximal activity
additional information
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
additional information
-
the enzyme significantly loses activity at near-neutral pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
55
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 42
-
15°C: 65% of maximal activity, 42°C: about 55% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
strain 877G, isolated from traditional Korean fermented food kimchi, shows very high gamma-aminobutanoate production
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
clustal X-generated dendrogram of bacterial glutamate decarboxylases, overview
evolution
metabolism
glutamate decarboxylase is a key enzyme that catalyzes the irreversible alpha-decarboxylation of L-glutamate to 4-aminobutanoate, GABA
additional information
evolution
clustal X-generated dendrogram of bacterial glutamate decarboxylases, overview
evolution
the amino acid sequences of GADLbHYE1 shows 48% homology with the GadA family and 99% identity with the GadB family from Lactobacillus brevis
additional information
absence of a His residue near the C-terminus in Lactobacillus brevis GadB homologue LVIS_0079
additional information
absence of a His residue near the C-terminus in Lactobacillus brevis GadB homologue LVIS_0079
additional information
binding of pyridoxal 5'-phosphate as well as to the active site residues Thr215 and Asp246 that promote decarboxylation
additional information
-
important role of C-terminal region in the pH-dependent regulation of enzyme activity. Enzyme molecular homology modeling
additional information
residues T215 and D246 are involved in catalysis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
50000
x * 53522, sequence calculation, x * 50000, recombinant His-tagged enzyme, SDS-PAGE
53522
x * 53522, sequence calculation, x * 50000, recombinant His-tagged enzyme, SDS-PAGE
54000
additional information
110000
dimeric enzyme, AF4-UV-MALS-dRI and molecular modeling
54000
2 * 54000, inactive, recombinant His-tagged enzyme, SDS-PAGE
54000
4 * 54000, ammonium sulfate-activated, recombinant His-tagged enzyme, SDS-PAGE
additional information
asymmetrical flow field-flow fractionation (AF4) coupled with UV/Vis, multi-angle light scattering (MALS), and differential refractive index (dRI) detectors (AF4-UV-MALS-dRI) is employed for analysis of glutamate decarboxylase molecular weight and aggregation
additional information
-
asymmetrical flow field-flow fractionation (AF4) coupled with UV/Vis, multi-angle light scattering (MALS), and differential refractive index (dRI) detectors (AF4-UV-MALS-dRI) is employed for analysis of glutamate decarboxylase molecular weight and aggregation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
?
x * 53522, sequence calculation, x * 50000, recombinant His-tagged enzyme, SDS-PAGE
dimer
2 * 54000, inactive, recombinant His-tagged enzyme, SDS-PAGE
tetramer
4 * 54000, ammonium sulfate-activated, recombinant His-tagged enzyme, SDS-PAGE
tetramer
Lactobacillus brevis IFO12005 is dimeric in the inactive form and tetrameric in the active form
additional information
sodium glutamate is essential for tetramer formation and its activation
additional information
-
sodium glutamate is essential for tetramer formation and its activation
additional information
asymmetrical flow field-flow fractionation (AF4) provides molecular weight (MW) (or size)-based separation of dimer, hexamer, and aggregates of LbGadB, molecular modeling
additional information
-
asymmetrical flow field-flow fractionation (AF4) provides molecular weight (MW) (or size)-based separation of dimer, hexamer, and aggregates of LbGadB, molecular modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
T17I/D294G/Q346H
-
site-directed mutagenesis, the mutant has increased catalytic efficiency, showing 13.1 and 43.2fold of wild-type GadB1 activity at pH 4.6 and pH 6.0, respectively
additional information
additional information
-
directed evolution of GadB1 using site-specific mutagenesis, mutant screening
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
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
additional information
the production of gamma-aminobutyric acid in Escherichia coli BL21 harboring gadlbhye1/pET28a is increased by adding pyridoxine as a cheaper coenzyme
additional information
-
the production of gamma-aminobutyric acid in Escherichia coli BL21 harboring gadlbhye1/pET28a is increased by adding pyridoxine as a cheaper coenzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the hexameric form of LbGadB is most stable at pH 6 and in presence of NaCl or KCl
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain Rosetta-gami B (DE3) by nickel affinity chromatography
recombinant His-tagged enzyme of Escherichia coli strain Origami 2 (DE3) by nickel affinity chromatography and dialysis
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatograpyh
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gad, DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene gad, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in Escherichia coli strains BL21 and JM109
gene gad, DNA and amino acid sequence determination and analysis, the protein sequence is identical to the LbGadB of the strain ATCC 367, recombinant expression of His-tagged enzyme in Escherichia coli strain Origami 2 (DE3)
gene gad, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene gadA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)
gene gadB, DNA and amin acid sequence determination and analysis, expression of the His-tagged enzyme in Escherichia coli strains Rosetta-gami B (DE3) ad JM109
gene gadB1, expression of wild-type and mutant enzymes in Corynebacterium glutamicum strain ATCC 13032 leads to increased 4-aminobutanoate levels in the transgenic bacterium
-
gene gadlbhye1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
-
use of Bacillus subtilis strain expressing L-glutamate decarboxylase from Lactobacillus brevis for preparation of Korean fermented soybean product Chungkukjang results in significantly higher levels of gamma-aminobutanoate in products
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ueno, Y.; Hayakawa, K.; Takahashi, S.; Oda, K.
Purification and characterization of glutamate decarboxylase from Lactobacillus brevis IFO 12005
Biosci. Biotechnol. Biochem.
61
1168-1171
1997
Levilactobacillus brevis
Park, K.B.; Oh, S.H.
Enhancement of gamma-aminobutyric acid production in Chungkukjang by applying a Bacillus subtilis strain expressing glutamate decarboxylase from Lactobacillus brevis
Biotechnol. Lett.
28
1459-1463
2006
Levilactobacillus brevis
Hiraga, K.; Ueno, Y.; Oda, K.
Glutamate decarboxylase from Lactobacillus brevis: activation by ammonium sulfate
Biosci. Biotechnol. Biochem.
72
1299-1306
2008
Levilactobacillus brevis (A9ZM78), Levilactobacillus brevis, Levilactobacillus brevis IFO 12005 (A9ZM78)
Shi, F.; Li, Y.
Synthesis of gamma-aminobutyric acid by expressing Lactobacillus brevis-derived glutamate decarboxylase in the Corynebacterium glutamicum strain ATCC 13032
Biotechnol. Lett.
33
2469-2474
2011
Levilactobacillus brevis, Levilactobacillus brevis Lb85
Yu, K.; Hu, S.; Huang, J.; Mei, L.
A high-throughput colorimetric assay to measure the activity of glutamate decarboxylase
Enzyme Microb. Technol.
49
272-276
2011
Levilactobacillus brevis, Levilactobacillus brevis CGMCC
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
Ann. Microbiol.
62
689-698
2011
Levilactobacillus brevis (D6PXK5), Levilactobacillus brevis CGMCC 1306 (D6PXK5)
-
Seo, M.J.; Nam, Y.D.; Lee, S.Y.; Park, S.L.; Yi, S.H.; Lim, S.I.
Expression and characterization of a glutamate decarboxylase from Lactobacillus brevis 877G producing gamma-aminobutyric acid
Biosci. Biotechnol. Biochem.
77
853-856
2013
Levilactobacillus brevis (K4HXK6), Levilactobacillus brevis 877G (K4HXK6)
Yu, K.; Lin, L.; Hu, S.; Huang, J.; Mei, L.
C-terminal truncation of glutamate decarboxylase from Lactobacillus brevis CGMCC 1306 extends its activity toward near-neutral pH
Enzyme Microb. Technol.
50
263-269
2012
Levilactobacillus brevis, Levilactobacillus brevis CGMCC 1306
Shi, F.; Xie, Y.; Jiang, J.; Wang, N.; Li, Y.; Wang, X.
Directed evolution and mutagenesis of glutamate decarboxylase from Lactobacillus brevis Lb85 to broaden the range of its activity toward a near-neutral pH
Enzyme Microb. Technol.
61-62
35-43
2014
Levilactobacillus brevis, Levilactobacillus brevis Lb85
De Biase, D.; Pennacchietti, E.
Glutamate decarboxylase-dependent acid resistance in orally acquired bacteria: function, distribution and biomedical implications of the gadBC operon
Mol. Microbiol.
86
770-786
2012
Escherichia coli, Listeria monocytogenes, Levilactobacillus brevis (A9ZM78), Levilactobacillus brevis (Q03U69), Levilactobacillus brevis ATCC 367 (Q03U69), Levilactobacillus brevis FO12005 (A9ZM78)
Choi, J.; Lee, S.; Linares-Pasten, J.A.; Nilsson, L.
Study on oligomerization of glutamate decarboxylase from Lactobacillus brevis using asymmetrical flow field-flow fractionation (AF4) with light scattering techniques
Anal. Bioanal. Chem.
410
451-458
2018
Levilactobacillus brevis (A0A1U9Y677), Levilactobacillus brevis, Levilactobacillus brevis DSM 1269 (A0A1U9Y677)
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
Biosci. Biotechnol. Biochem.
78
1656-1661
2014
Levilactobacillus brevis (A7UMP3), Levilactobacillus brevis, Levilactobacillus brevis BH2 (A7UMP3)
Lim, H.S.; Seo, D.H.; Cha, I.T.; Lee, H.; Nam, Y.D.; Seo, M.J.
Expression and characterization of glutamate decarboxylase from Lactobacillus brevis HYE1 isolated from kimchi
World J. Microbiol. Biotechnol.
34
44
2018
Levilactobacillus brevis (A0A0B5CSE1), Levilactobacillus brevis, Levilactobacillus brevis HYE1 (A0A0B5CSE1)
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