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H465A
the mutant is active at pH well above 5.7 and shows 78% of wild type specific activity in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C in the presence of 0.1 mM pyridoxal 5'-phosphate
Q5D/V6I/T7E
site-directed mutagenesis the mutant shows higher thermostability and increased melting temperature compared to the wild-type, but shows no reduction of catalytic activity
A408F
virtual point mutation, modelling
D304A
virtual point mutation, modelling
D304C
virtual point mutation, modelling
D304I
virtual point mutation, modelling
D304M
virtual point mutation, modelling
D304P
virtual point mutation, modelling
D304S
virtual point mutation, modelling
D304T
virtual point mutation, modelling
D304V
virtual point mutation, modelling
E89A
-
site-directed mutagenesis
E89A/H465A
-
site-directed mutagenesis, the double mutation not only brakes the cooperativity in the activity change but also yields a mutant enzyme that retains the activity at neutral pH. The resulting mutant enzyme, that is active at neutral pH, inhibits the cell growth in a glycerol medium by converting intracellular Glu into 4-aminobutanoate in an uncontrolled manner
E89Q
-
site-directed mutagenesis, double mutation Glu89Gln/DELTA452-466 strongly inhibits the cell growth and shows higher activity than mutant Glu89Gln/His465Ala
E89Q/H465A
-
site-directed mutagenesis, the double mutation not only brakes the cooperativity in the activity change but also yields a mutant enzyme that retains the activity at neutral pH. The resulting mutant enzyme, that is active at neutral pH, inhibits the cell growth in a glycerol medium by converting intracellular Glu into 4-aminobutanoate in an uncontrolled manner
H465A
-
site-directed mutagenesis
I164D
virtual point mutation, modelling
I164E
virtual point mutation, modelling
I164L
virtual point mutation, modelling
I164P
virtual point mutation, modelling
I164Q
virtual point mutation, modelling
I164R
virtual point mutation, modelling
K168F
virtual point mutation, modelling
K168I
virtual point mutation, modelling
K168L
virtual point mutation, modelling
K276A
-
no decarboxylation of L-Glu. Transition temperature is 11°C higher than that of the wild-type enzyme. Limited proteolysis by trypsin shows that the mutant enzyme is more resistant to proteolytic degradation than the wild-type enzyme. Mutant enzyme contains very little pyridoxal 5'-phosphate
K276H
-
no decarboxylation of L-Glu. Transition temperature is 4°C higher than that of the wild-type enzyme. Mutant enzyme contains no pyridoxal 5'-phosphate
K87F
virtual point mutation, modelling
K87W
virtual point mutation, modelling
K87Y
virtual point mutation, modelling
L60F
virtual point mutation, modelling
L60W
virtual point mutation, modelling
N302A
virtual point mutation, modelling
N302C
virtual point mutation, modelling
N302F
virtual point mutation, modelling
N302I
virtual point mutation, modelling
N302L
virtual point mutation, modelling
N302M
virtual point mutation, modelling
N302P
virtual point mutation, modelling
N302S
virtual point mutation, modelling
N302T
virtual point mutation, modelling
N302V
virtual point mutation, modelling
N316F
virtual point mutation, modelling
N316W
virtual point mutation, modelling
N316Y
virtual point mutation, modelling
N83P
virtual point mutation, modelling
N83W
virtual point mutation, modelling
Q309C
virtual point mutation, modelling
Q309I
virtual point mutation, modelling
Q309K
virtual point mutation, modelling
Q309R
virtual point mutation, modelling
Q309S
virtual point mutation, modelling
Q309T
virtual point mutation, modelling
Q309V
virtual point mutation, modelling
Q5I/V6D/T7Q
mutant M6, site-directed mutagenesis, the mutant shows higher thermostability, with a 5.6times (560%) increase in half-life value at 45°C, 8.7°C rise in melting temperature (Tm) and a 14.3°C rise in the temperature at which 50% of the initial activity remained after 15 min incubation (T15/50), compared to wild-type enzyme. The induced new hydrogen bonds in the same polypeptide chain or between polypeptide chains in Escherichia coli GadB homohexamer may be responsible for the improved thermostability. Increased thermostability contributes to increased GABA conversion ability. After 12 h conversion of 3 mol/l glutamate, 297 g/l GABA is produced and 95% mole conversion rate is catalyzed by mtant M6 whole cells while those by wild-type GAD are 273.5 g/L and 86.2%, respectively
Q5N/V6Y/T7V
mutant M1, site-directed mutagenesis, the mutant shows improved thermostability and increased activity compared to the wild-type enzyme
Q5Y/V6R/T7K
mutant M8, site-directed mutagenesis, the mutant shows improved thermostability and increased activity compared to the wild-type enzyme
R319F
virtual point mutation, modelling
R319I
virtual point mutation, modelling
R319L
virtual point mutation, modelling
R319M
virtual point mutation, modelling
R319W
virtual point mutation, modelling
R319Y
virtual point mutation, modelling
R398F
virtual point mutation, modelling
R398I
virtual point mutation, modelling
R398L
virtual point mutation, modelling
R398M
virtual point mutation, modelling
R398W
virtual point mutation, modelling
R398Y
virtual point mutation, modelling
S246C
virtual point mutation, modelling
S246F
virtual point mutation, modelling
S246I
virtual point mutation, modelling
S246L
virtual point mutation, modelling
S246M
virtual point mutation, modelling
S246V
virtual point mutation, modelling
S246W
virtual point mutation, modelling
S246Y
virtual point mutation, modelling
S396C
virtual point mutation, modelling
S396F
virtual point mutation, modelling
S396I
virtual point mutation, modelling
S396L
virtual point mutation, modelling
S396M
virtual point mutation, modelling
S396R
virtual point mutation, modelling
S396V
virtual point mutation, modelling
S396W
virtual point mutation, modelling
S396Y
virtual point mutation, modelling
T214F
virtual point mutation, modelling
T214L
virtual point mutation, modelling
T410P
virtual point mutation, modelling
T410V
virtual point mutation, modelling
Y393E
virtual point mutation, modelling
Y393K
virtual point mutation, modelling
Y393Q
virtual point mutation, modelling
Y393R
virtual point mutation, modelling
additional information
the mutant GadBDELTAHT (His465 of GadB is deleted together with the last residue in the polypeptide chain, Thr466) is active at pH well above 5.7 and shows 52% of wild type specific activity in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C in the presence of 0.1 mM pyridoxal 5'-phosphate
additional information
-
the mutant GadBDELTAHT (His465 of GadB is deleted together with the last residue in the polypeptide chain, Thr466) is active at pH well above 5.7 and shows 52% of wild type specific activity in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C in the presence of 0.1 mM pyridoxal 5'-phosphate
additional information
improvement of the thermostability of GadB through structural optimization ofits N-terminal interdomain. Residues Gln5, Val6, and Thr7 are potential mutational target sites for the optimization of inter- and intra-molecular interactions of the triple-helix bundle. Generation of a deletion mutant of GadB lacking residues 1-14 at the N-terminus, GadBDELTA1-14
additional information
-
improvement of the thermostability of GadB through structural optimization ofits N-terminal interdomain. Residues Gln5, Val6, and Thr7 are potential mutational target sites for the optimization of inter- and intra-molecular interactions of the triple-helix bundle. Generation of a deletion mutant of GadB lacking residues 1-14 at the N-terminus, GadBDELTA1-14
additional information
cross-linked aggregation method is used in order to extend the active range of GAD toward alkaline pH. Cross-linked aggregation activate GAD even at neutral and alkaline pH values. It is a useful method capable of facilitating recovery and reuse of the enzyme as well as increasing the reaction conversion by extending the active pH range of GAD. GAD from Escherichia coli is prepared as cross-linked enzyme aggregate (CLEA) in which the enzyme is precipitated using ammonium sulfate (60% saturation) and then cross-linked with glutaraldehyde (2%) in sodium acetate buffer (0.2 mol/l, pH 4.6). The cross-linked aggregation extends an active pH-range of GAD from pH 5.5 up to pH 8.0. As a result, the reaction conversion of 1 mol/l monosodium L-glutamate into GABA is improved from 13% to 22%. Moreover, the CLEA of GAD is easily recovered after the reaction and reused retaining over 95% of its initial activity during the first four cycles and over 60% activity at the 10th cycle. Method evaluation and optimization, overview
additional information
enhanced production of recombinant Escherichia coli glutamate decarboxylase through optimization of induction strategy and addition of pyridoxine, different induction strategies are investigated, induction is optimal when the temperature is maintained at 30°C, the inducer lactose is fed at a rate of 0.2 g/l/h, and protein expression is induced when the cell density (OD600) reaches 50. Under these conditions, the GAD activity of 1273.8 U/ml is achieved. The supplementing the medium with 2 mM pyridoxine hydrochloride (PN), a cheap and stable PLP precursor, at the initiation of protein expression, and then again 10 h later, results in very high GAD activity of 3193.4 U/ml. Fed-batch cultivation in a 3.6-L fermentor at 37°C and pH 7.0
additional information
-
enhanced production of recombinant Escherichia coli glutamate decarboxylase through optimization of induction strategy and addition of pyridoxine, different induction strategies are investigated, induction is optimal when the temperature is maintained at 30°C, the inducer lactose is fed at a rate of 0.2 g/l/h, and protein expression is induced when the cell density (OD600) reaches 50. Under these conditions, the GAD activity of 1273.8 U/ml is achieved. The supplementing the medium with 2 mM pyridoxine hydrochloride (PN), a cheap and stable PLP precursor, at the initiation of protein expression, and then again 10 h later, results in very high GAD activity of 3193.4 U/ml. Fed-batch cultivation in a 3.6-L fermentor at 37°C and pH 7.0
additional information
GABA is produced from glutamate through decarboxylation catalyzed by the recombinant glutamate decarboxylase (GAD) expressed in Escherichia coli strain BL21(DE3), the GAD-catalyzed reaction is conducted in 0.2 mol/l sodium acetate buffer (pH 4.6) with 1 mol/l monosodium glutamate at 37°C, optimization of GABA production method, overview. When commercial cation-exchange resins as solid acids are simply added to the reaction medium, the conversion improves from 13% to 67% without salt formation. Even when water is used as the reaction medium, acidic ion-exchange resins enhance the reaction conversion significantly. In a salt-free manner, acidic resins suppress the pH rise during the reaction so that they can enhance the reaction conversion. In addition, they can be recovered and reused easily after the reaction. Heterogeneous solid acids make the GABA production processmore economical and eco-friendly
additional information
optimization of the reaction conditions for recombinant GABA production by the homogenously expressed enzyme from Escherichia coli. The activity for GAD produced in media supplemented with 0.05 mM soluble vitamin B6 analogue pyridoxine hydrochloride (GAD-V) is 154.8 U/l, 1.8fold higher than that of GAD obtained without supplementation (GAD-C). Purified GAD-V exhibits increased activity of 193.4 U/mg (1.5fold higher), superior thermostability (2.8fold greater), and higher kcat/Km (1.6fold higher) compared to GAD-C. Under optimal conditions in reactions mixtures lacking added pyridoxal 5'-phosphate, crude GAD-V converts 500 g/l monosodium glutamate to GABA with a yield of 100%, and 750 g/l monosodium glutamate with a yield of 88.7%. Effect of substrate concentration on GABA production by GAD-C and GAD-V, overview
additional information
production method optimization, overexpression of Escherichia coli gene gadB in strain BL21(DE3), overview. Some GadB proteins overexpressed in BL21(DE3)/pET20b-pelB-gadB might not be functional. The highest extracellular GadB activity (1.39 U/mL) is found in BL21(DE3)/pET20b-torAgadB with 0.7 mM IPTG induction
additional information
-
production method optimization, overexpression of Escherichia coli gene gadB in strain BL21(DE3), overview. Some GadB proteins overexpressed in BL21(DE3)/pET20b-pelB-gadB might not be functional. The highest extracellular GadB activity (1.39 U/mL) is found in BL21(DE3)/pET20b-torAgadB with 0.7 mM IPTG induction
additional information
-
construction of a synthetic protein complex to improve the 4-aminobutanoate conversion in engineered Escherichia coli strain XL1-Blue, by assembling a single protein-protein interaction domain SH3 to the glutamate decarboxylase (GadA and GadB) and attaching a cognate peptide ligand to the glutamate/4-aminobutanoate antiporter (GadC) at the N-terminus, C-terminus, and the 233rd amino acid residue
additional information
-
expanding the active pH range of the enzyme by breaking the cooperativeness
additional information
-
generation of a DELTA452-466 deletion mutant, the mutant can convert glycerol into 4-aminobutanoate with minimal growth inhibition to maximize its space-time yield. Double mutation Glu89Gln/DELTA452-466 strongly inhibits the cell growth and shows higher activity than mutant Glu89Gln/His465Ala
additional information
-
immobilization of the cellulose binding domain-enzyme fusion protein on a crystalline cellulose resin, with binding capacity of 33 nmol CBD-GAD/g resin, the immobilized enzymes retains 60% of initial activiy after 10 uses
additional information
application of site-directed saturation mutagenesis of the N-terminal residues of GadB from Escherichia coli to improve its thermostability. Among the mutants tested, M6 is the most thermostable one
additional information
-
application of site-directed saturation mutagenesis of the N-terminal residues of GadB from Escherichia coli to improve its thermostability. Among the mutants tested, M6 is the most thermostable one
additional information
-
Corynebacterium glutamicum, the major L-glutamate producing microorganism, has been engineered to achieve direct fermentative production of GABA from glucose, method optimization, overview. In the fed-batch cultivation at pH 5.0, which is not preferable condition for cell growth, much less glutamate might be synthesized, which results in much lower production of GABA compared with that of pH 6.0. In the culture at pH 6.0, increased GAD activity can be balanced for glutamate synthesis to result in high-level production of GABA of up to 38.6 g/l. Corynebacterium glutamicum expressing Escherichia coli GAD mutant under the strong PH36 promoter produces GABA to the concentration of 5.89 g/l in GP1 medium at pH 7.0, which is 17fold higher than that obtained by Corynebacterium glutamicum expressing wild-type Escherichia coli GAD in the same condition (0.34 g/l). Optimized fed-batch culture of Corynebacterium glutamicum expressing Escherichia coli GAD mutant in GP1 medium containing 0.05 mg/l of biotin at pH 6.0, 30°C, results in the highest GABA concentration of 38.6 g/l with the productivity of 0.536 g/l/h
additional information
expression of gadB2 produced more GABA in Corynebacterium glutamicum than expression of gadB1. Construction of gadB2 expression strains under different RBS sequence and promoters (tacM, sglB, hmp, ilvE, cg1417, gapA, dtsR, tuf, cspB, odhL, uspA, gdh, sod, and pqo), engineering of RBS sequence and promoter, evaluation of GABA production, overview. In recombinant Corynebacterium glutamicum, the optimal pH for cell growth and Glu biosynthesis is about 7.0, whereas that for GAD activity and conversion of Glu to GABA is 5.0-6.0
additional information
expression of gadB2 produced more GABA in Corynebacterium glutamicum than expression of gadB1. Construction of gadB2 expression strains under different RBS sequence and promoters (tacM, sglB, hmp, ilvE, cg1417, gapA, dtsR, tuf, cspB, odhL, uspA, gdh, sod, and pqo), engineering of RBS sequence and promoter, evaluation of GABA production, overview. In recombinant Corynebacterium glutamicum, the optimal pH for cell growth and Glu biosynthesis is about 7.0, whereas that for GAD activity and conversion of Glu to GABA is 5.0-6.0
additional information
point mutation is performed virtually in the active site of the Escherichia coli GAD in order to increase thermal stability and catalytic activity of the enzyme, overview. Molecular modelling results indicate that performing mutation separately at positions 164, 302, 304, 393, 396, 398 and 410 increase binding affinity to substrate. The enzyme is predicted to be more thermostable in all 7 mutants based on DDG value. Stabilizing mutations in the active site based on DDG value, and binding energy levels, overview. Cavity volume change analysis for selected mutants
additional information
-
point mutation is performed virtually in the active site of the Escherichia coli GAD in order to increase thermal stability and catalytic activity of the enzyme, overview. Molecular modelling results indicate that performing mutation separately at positions 164, 302, 304, 393, 396, 398 and 410 increase binding affinity to substrate. The enzyme is predicted to be more thermostable in all 7 mutants based on DDG value. Stabilizing mutations in the active site based on DDG value, and binding energy levels, overview. Cavity volume change analysis for selected mutants
additional information
the Escherichia coli glutamate decarboxylase is expressed in Corynebacterium glutamicum for production of gamma-aminobutyric acid (GABA), a building block of the biodegradable plastic polyamide 4. Disruption of gene pknG, encoding serine/threonine protein kinase G (EC 2.7.11.1), enhances recombinant production of gamma-aminobutyric acid through reduction of the 2-oxoglutarate dehydrogenase complex (ODHC) activity regulation, PknG catalyzes the phosphorylation of OdhI, a 15 kDa subunit of ODHC, which reverses the inhibition of the ODHC activity. Strain GAD produces 13.06 g/l of GABA in 120 hours, consuming 83.62 g/l of glucose, strain GADDELTApknG produces 0.272 g/l of GABA in 120 hours, consuming less glucose
additional information
-
the Escherichia coli glutamate decarboxylase is expressed in Corynebacterium glutamicum for production of gamma-aminobutyric acid (GABA), a building block of the biodegradable plastic polyamide 4. Disruption of gene pknG, encoding serine/threonine protein kinase G (EC 2.7.11.1), enhances recombinant production of gamma-aminobutyric acid through reduction of the 2-oxoglutarate dehydrogenase complex (ODHC) activity regulation, PknG catalyzes the phosphorylation of OdhI, a 15 kDa subunit of ODHC, which reverses the inhibition of the ODHC activity. Strain GAD produces 13.06 g/l of GABA in 120 hours, consuming 83.62 g/l of glucose, strain GADDELTApknG produces 0.272 g/l of GABA in 120 hours, consuming less glucose
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Fonda, M.L.
L-Glutamate decarboxylase from bacteria
Methods Enzymol.
113
11-16
1985
Clostridium perfringens, Escherichia coli
brenda
Fields, H.A.; Wheeler, C.M.; Davis, C.L.; Warner, T.N.; Bradley, D.W.; Maynard, J.E.
Purification and radiometric assay detection of glutamate decarboxylase
J. Appl. Biochem.
4
271-279
1982
Escherichia coli
-
brenda
Youngs, T.L.; Tunnicliff, G.
Substrate analogues and divalent cations as inhibitors of glutamate decarboxylase from Escherichia coli
Biochem. Int.
23
915-922
1991
Escherichia coli, Mus musculus
brenda
Bertoldi, M.; Carbone, V.; Borri Voltattorni, C.
Ornithine and glutamate decarboxylases catalyze an oxidative deamination of their a-methyl substrates
Biochem. J.
342
509-512
1999
Escherichia coli
-
brenda
McCormick, S.J.; Tunnicliff, G.
Kinetics of inactivation of glutamate decarboxylase by cysteine-specific reagents
Acta Biochim. Pol.
48
573-578
2001
Escherichia coli
brenda
Capitani, G.; De Biase, D.; Aurizi, C.; Gut, H.; Bossa, F.; Grutter, M.G.
Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase
EMBO J.
22
4027-4037
2003
Escherichia coli
brenda
Drsata, J.; Netopilova, M.; Tolman, V.
Stereoisomers of 4-fluoroglutamic acid. Influence on Escherichia coli glutamate decarboxylase
Pharmazie
54
713-714
1999
Escherichia coli
brenda
Dutyshev, D.I.; Darii, E.L.; Fomenkova, N.P.; Pechik, I.V.; Polyakov, K.M.; Nikonov, S.V.; Andreeva, N.S.; Sukhareva, B.S.
Structure of Escherichia coli glutamate decarboxylase (GADalpha) in complex with glutarate at 2.05 A resolution
Acta Crystallogr. Sect. D
61
230-235
2005
Escherichia coli
brenda
Matthews, C.C.; Zielke, H.R.; Fishman, P.S.; Remington, M.P.; Bowen, T.G.
Glutamate decarboxylase protects neurons against excitotoxic injury
J. Neurosci. Res.
85
855-859
2007
Escherichia coli
brenda
Pennacchietti, E.; Lammens, T.M.; Capitani, G.; Franssen, M.C.; John, R.A.; Bossa, F.; De Biase, D.
Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH
J. Biol. Chem.
284
31587-31596
2009
Escherichia coli (P69910), Escherichia coli
brenda
Yao, W.; Wu, X.; Zhu, J.; Sun, B.; Miller, C.
System establishment of ATPS for one-step purification of glutamate decarboxylase from E. coli after cell disruption
Appl. Biochem. Biotechnol.
164
1339-1349
2011
Escherichia coli
brenda
Wang, Q.; Xin, Y.; Zhang, F.; Feng, Z.; Fu, J.; Luo, L.; Yin, Z.
Enhanced ?-aminobutyric acid-forming activity of recombinant glutamate decarboxylase (gadA) from Escherichia coli
World J. Microbiol. Biotechnol.
27
693-700
2011
Escherichia coli
brenda
Park, H.; Ahn, J.; Lee, J.; Lee, H.; Kim, C.; Jung, J.K.; Lee, H.; Lee, E.G.
Expression, immobilization and enzymatic properties of glutamate decarboxylase fused to a cellulose-binding domain
Int. J. Mol. Sci.
13
358-368
2012
Escherichia coli
brenda
Thu Ho, N.A.; Hou, C.Y.; Kim, W.H.; Kang, T.J.
Expanding the active pH range of Escherichia coli glutamate decarboxylase by breaking the cooperativeness
J. Biosci. Bioeng.
115
154-158
2013
Escherichia coli
brenda
Jun, C.; Joo, J.C.; Lee, J.H.; Kim, Y.H.
Thermostabilization of glutamate decarboxylase B from Escherichia coli by structure-guided design of its pH-responsive N-terminal interdomain
J. Biotechnol.
174
22-28
2014
Escherichia coli (P69910), Escherichia coli
brenda
Le Vo, T.D.; Ko, J.S.; Park, S.J.; Lee, S.H.; Hong, S.H.
Efficient gamma-aminobutyric acid bioconversion by employing synthetic complex between glutamate decarboxylase and glutamate/GABA antiporter in engineered Escherichia coli
J. Ind. Microbiol. Biotechnol.
40
927-933
2013
Escherichia coli
brenda
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)
brenda
Okai, N.; Takahashi, C.; Hatada, K.; Ogino, C.; Kondo, A.
Disruption of pknG enhances production of gamma-aminobutyric acid by Corynebacterium glutamicum expressing glutamate decarboxylase
AMB Express
4
20
2014
Escherichia coli (A5YKJ2), Escherichia coli
brenda
Zhao, A.; Hu, X.; Li, Y.; Chen, C.; Wang, X.
Extracellular expression of glutamate decarboxylase B in Escherichia coli to improve gamma-aminobutyric acid production
AMB Express
6
55
2016
Escherichia coli (P69910), Escherichia coli, Escherichia coli K-12 / W3110 (P69910)
brenda
Shi, F.; Luan, M.; Li, Y.
Ribosomal binding site sequences and promoters for expressing glutamate decarboxylase and producing gamma-aminobutyrate in Corynebacterium glutamicum
AMB Express
8
61
2018
Escherichia coli (A0A0J2E2M6), Escherichia coli (A0A2Y0HLE8)
brenda
Su, L.; Huang, Y.; Wu, J.
Enhanced production of recombinant Escherichia coli glutamate decarboxylase through optimization of induction strategy and addition of pyridoxine
Biores. Technol.
198
63-69
2015
Escherichia coli (P69910), Escherichia coli
brenda
Tavakoli, Y.; Esmaeili, A.; Saber, H.
Increasing thermal stability and catalytic activity of glutamate decarboxylase in E. coli an in silico study
Comput. Biol. Chem.
64
74-81
2016
Escherichia coli (P69908), Escherichia coli
brenda
Fan, L.Q.; Li, M.W.; Qiu, Y.J.; Chen, Q.M.; Jiang, S.J.; Shang, Y.J.; Zhao, L.M.
Increasing thermal stability of glutamate decarboxylase from Escherichia coli by site-directed saturation mutagenesis and its application in GABA production
J. Biotechnol.
278
1-9
2018
Escherichia coli (A5YKJ2), Escherichia coli
brenda
Dinh, T.; Ho, N.; Kang, T.; Mcdonald, K.; Won, K.
Salt-free production of gamma-aminobutyric acid from glutamate using glutamate decarboxylase separated from Escherichia coli
J. Chem. Technol. Biotechnol.
89
1432-1436
2014
Escherichia coli (P69910)
-
brenda
Dinh, T.; Jang, N.; Mcdonald, K.; Won, K.
Cross-linked aggregation of glutamate decarboxylase to extend its activity range toward alkaline pH
J. Chem. Technol. Biotechnol.
90
2100-2105
2015
Escherichia coli (P69910)
-
brenda
Choi, J.W.; Yim, S.S.; Lee, S.H.; Kang, T.J.; Park, S.J.; Jeong, K.J.
Enhanced production of gamma-aminobutyrate (GABA) in recombinant Corynebacterium glutamicum by expressing glutamate decarboxylase active in expanded pH range
Microb. Cell Fact.
14
21
2015
Escherichia coli
brenda
Huang, Y.; Su, L.; Wu, J.
Pyridoxine supplementation improves the activity of recombinant glutamate decarboxylase and the enzymatic production of gama-aminobutyric acid
PLoS ONE
11
e0157466
2016
Escherichia coli (P69910), Escherichia coli K-12 / MG1655 (P69910)
brenda
Giovannercole, F.; Merigoux, C.; Zamparelli, C.; Verzili, D.; Grassini, G.; Buckle, M.; Vachette, P.; De Biase, D.
On the effect of alkaline pH and cofactor availability in the conformational and oligomeric state of Escherichia coli glutamate decarboxylase
Protein Eng. Des. Sel.
30
235-244
2017
Escherichia coli (P69910), Escherichia coli
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