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( Sivachandiran Somasundaram ),( Murali Kannan Maruthamuthu ),( Irisappan Ganesh ),( Gyeong Tae Eom ),( Soon Ho Hong ) 한국미생물생명공학회(구 한국산업미생물학회) 2017 Journal of microbiology and biotechnology Vol.27 No.9
Gamma-aminobutyric acid is a precursor of nylon-4, which is a promising heat-resistant biopolymer. GABA can be produced from the decarboxylation of glutamate by glutamate decarboxylase. In this study, a synthetic scaffold complex strategy was employed involving the Neurospora crassa glutamate decarboxylase (GadB) and Escherichia coli GABA antiporter (GadC) to improve GABA production. To construct the complex, the SH3 domain was attached to the N. crassa GadB, and the SH3 ligand was attached to the N-terminus, middle, and C-terminus of E. coli GadC. In the C-terminus model, 5.8 g/l of GABA concentration was obtained from 10 g/l glutamate. When a competing pathway engineered strain was used, the final GABA concentration was further increased to 5.94 g/l, which corresponds to 97.5% of GABA yield. With the introduction of the scaffold complex, the GABA productivity increased by 2.9 folds during the initial culture period.
Andreoni, Francesca,Mastrogiacomo, Anna Rita,Serafini, Giordano,Carancini, Gionmattia,Magnani, Mauro The Korean Society for Microbiology and Biotechnol 2019 한국미생물·생명공학회지 Vol.47 No.1
Glutamate decarboxylase catalyzes the conversion of glutamate to gamma-aminobutyric acid (GABA), contributing to pH homeostasis through proton consumption. The reaction is the first step toward the GABA shunt. To date, the enzymes involved in the glutamate metabolism of Photobacterium damselae subsp. piscicida have not been elucidated. In this study, an open reading frame of P. damselae subsp. piscicida, showing homology to the glutamate decarboxylase or putative pyridoxal-dependent aspartate 1-decarboxylase genes, was isolated and cloned into an expression vector to produce the recombinant enzyme. Preliminary gas chromatography-mass spectrometry characterization of the purified recombinant enzyme revealed that it catalyzed not only the decarboxylation of glutamate but also the transamination of GABA. This enzyme of P. damselae subsp. piscicida could be bifunctional, combining decarboxylase and transaminase activities in a single polypeptide chain.
Hong, Sung-Jun,Ullah, Ihsan,Park, Gun-Seok,Lee, Chang-Hee,Shin, Jae-Ho The Korean Society for Applied Biological Chemisty 2012 Applied Biological Chemistry (Appl Biol Chem) Vol.55 No.2
Glutamate decarboxylase (GAD) (EC 4.1.1.15) catalyzes decarboxylation of glutamic acid to produce gamma-aminobutyric acid (GABA). A putative gad gene (tk1814) from an archaeon Thermococcus kodakaraensis KOD1 was cloned and transformed into Escherichia coli to produce a bulk amount of recombinant GAD. Activity of the purified GAD was optimal at $90^{\circ}C$ and pH 8.0. Optimal concentration of substrate for conversion into gamma-aminobutyric acid by recombinant GAD was 50 mM monosodium glutamate. Recombinant GAD was confirmed to be monomeric, and its activity was greatly inhibited by various salts such as sodium chloride, Tris-HCl, and sodium phosphate. $K_m$, $V_{max}$, and $K_{cat}$ values were 9.92 mM, 153.8 ${\mu}mol\;min^{-1}\;mg^{-1}$, and $6.613{\times}10^3\;min^{-1}$ respectively.
Francesca Andreoni,Anna Rita Mastrogiacomo,Giordano Serafini,Gionmattia Cara,Mauro Magnani 한국미생물·생명공학회 2019 한국미생물·생명공학회지 Vol.47 No.1
Glutamate decarboxylase catalyzes the conversion of glutamate to gamma-aminobutyric acid (GABA), contributing to pH homeostasis through proton consumption. The reaction is the first step toward the GABA shunt. To date, the enzymes involved in the glutamate metabolism of Photobacterium damselae subsp. piscicida have not been elucidated. In this study, an open reading frame of P. damselae subsp. piscicida, showing homology to the glutamate decarboxylase or putative pyridoxal-dependent aspartate 1-decarboxylase genes, was isolated and cloned into an expression vector to produce the recombinant enzyme. Preliminary gas chromatography-mass spectrometry characterization of the purified recombinant enzyme revealed that it catalyzed not only the decarboxylation of glutamate but also the transamination of GABA. This enzyme of P. damselae subsp. piscicida could be bifunctional, combining decarboxylase and transaminase activities in a single polypeptide chain.
( Hyun Deok Sa ),( Ji Yeong Park ),( Seon Ju Jeong ),( Kang Wook Lee ),( Jeong Hwan Kim ) 한국미생물 · 생명공학회 2015 Journal of microbiology and biotechnology Vol.25 No.5
A gamma-aminobutyric acid (GABA)-producing microorganism was isolated from jeot-gal (anchovy), a Korean fermented seafood. The isolate, A156, produced GABA profusely when incubated in MRS broth with monosodium glutamate (3% (w/v)) at 37°C for 48 h. A156 was identified as Lactobacillus sakei by 16S rRNA gene sequencing. The GABA conversion yield was 86% as determined by GABase enzyme assay. The gadB gene encoding glutamate decarboxylase (GAD) was cloned by PCR. gadC encoding a glutamate/GABA antiporter was located immediately upstream of gadB. The operon structure of gadCB was confirmed by RT-PCR. gadB was overexpressed in Escherichia coli BL21(DE3) and recombinant GAD was purified. The purified GAD was 54.4 kDa in size by SDS-PAGE. Maximum GAD activity was observed at pH 5.0 and 55°C and the activity was dependent on pyridoxal 5’-phosphate. The Km and Vmax of GAD were 0.045 mM and 0.011 mM/min, respectively, when glutamate was used as the substrate.
( Jeong A Kim ),( Ji Yeong Park ),( Jeong Hwan Kim ) 한국미생물생명공학회(구 한국산업미생물학회) 2021 한국미생물·생명공학회지 Vol.49 No.1
A γ-aminobutyric acid (GABA)-producing microorganism was isolated from galchi (hairtail fish, Trichiurus lepturus) jeotgal, a Korean salted and fermented seafood. The G144 isolate produced GABA excessively when incubated in MRS broth containing monosodium glutamate (MSG, 3%, w/v). G144 was identified as Lactobacillus brevis through 16S rRNA and recA gene sequencing. gadB and gadC encoding glutamate decarboxylase (GAD) and glutamate/GABA antiporter, respectively, were cloned and gadB was located downstream of gadC. The operon structure of gadCB was confirmed by reverse transcription (RT)-polymerase chain reaction. gadB was overexpressed in Escherichia coli and recombinant GAD was purified and its size was 54.4 kDa as evidenced by SDS-PAGE results. Maximum GAD activity was observed at pH 5.0 and 40℃ and the activity was dependent on pyridoxal 5'-phophate. The K<sub>m</sub> and V<sub>max</sub> of GAD were 8.6 mM and 0.01 mM/min, respectively.
전기경련충격이 부신절제 백서 해마의 Glutamate Decarboxylase와 Glutamine Synthetase의 활성도에 미치는 영향
김용식,김형래,주연호 大韓神經精神醫學會 1992 신경정신의학 Vol.31 No.4
The authors measured the activities of Glutamate Decarboxylase(GAD) and Glutamine Synthetase(GS), the essential enzymes in GABA and glutamate system which are closely linked to the mechanism of convulsion to determine whether the anticonvulsant action of consecutive electroconvulsive shock(ECS) can explain the therapeutic effects of ECS on psychiatric illnesses such as depression, mania and schizophrenia. We performed adrenalectomy on rats to exclude nonspecific endocrine reaction to stress produced by ECS. From fourteenth day after adrenalectomy. we administered ECS to those rats for ten days. then they are victimized 24hrs after the last ECS. The sample were obtained from hippocampus. and the activities of GAD and GS were compared with those of adequate control cases. Significant results are the reduced activities of GAD in adrenalectomized rat hippocampus after 10 consecutive ECS(p<0.05) and the reduced activities of GS in hippocampus by adrenalectomy(p<0.001). This study indicates that the mechanism of ECS are closely linked to GABA and Glutamate metabolism and we think that further studies are needed including moleculer biology technique.
홍성준,Ihsan Ullah,박건석,이창희,JAE-HO SHIN 한국응용생명화학회 2012 Applied Biological Chemistry (Appl Biol Chem) Vol.55 No.2
Glutamate decarboxylase (GAD) (EC 4.1.1.15)catalyzes decarboxylation of glutamic acid to produce gammaaminobutyric acid (GABA). A putative gad gene (tk1814) from an archaeon Thermococcus kodakaraensis KOD1 was cloned and transformed into Escherichia coli to produce a bulk amount of recombinant GAD. Activity of the purified GAD was optimal at 90oC and pH 8.0. Optimal concentration of substrate for conversion into gamma-aminobutyric acid by recombinant GAD was 50 mM monosodium glutamate. Recombinant GAD was confirmed to be monomeric, and its activity was greatly inhibited by various salts such as sodium chloride, Tris-HCl, and sodium phosphate. Km, Vmax, and Kcat values were 9.92 mM, 153.8 μmol min−1 mg−1, and 6.613×103 min−1 respectively.
이세진,Zhuang Yao,Yu Meng,Huong Giang Le,전혜성,유지연,김정환 경상국립대학교 농업생명과학연구원 2020 농업생명과학연구 Vol.54 No.4
A γ-aminobutyric acid (GABA) producing microorganism was isolated from Sun-Tae Jeotgal, a Korean traditional fermented seafood. Two thousand presumptive lactic acid bacteria (LAB) isolates were screened for GABA production by thin layer chromatography. One isolate, T118, produced GABA profusely, and identified as Lactobacillus brevis. Growth of Lb. brevis T118 was examined during 120 h cultivation in MRS broth under different conditions. Lb. brevis T118 grew well at 30-37℃, initial pH of 4-7, and up to 5% NaCl (w/v). A gene, gadB, encoding glutamate decarboxylase (GAD) was cloned by PCR. gadC encoding a glutamate/GABA antiporter was cloned and gadC located immediately upstream of gadB, indicating gadCB operon structure. The operon structure was confirmed by reverse transcription (RT)-PCR. gadB was overexpressed in Escherichia coli BL21 (DE3) and recombinant GAD was purified. The size of recombinant GAD was 54.4 kDa by SDS-PAGE, which matched well with the calculated size from the nucleotide sequence.