Identification, Expression and Preliminary Characterization of a Recombinant Bifunctional Enzyme of Photobacterium damselae subsp. piscicida with Glutamate Decarboxylase/Transaminase Activity
| العنوان: | Identification, Expression and Preliminary Characterization of a Recombinant Bifunctional Enzyme of Photobacterium damselae subsp. piscicida with Glutamate Decarboxylase/Transaminase Activity |
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| المؤلفون: | Giordano Serafini, Gionmattia Carancini, Mauro Magnani, Francesca Andreoni, A. R. Mastrogiacomo |
| المصدر: | Microbiology and Biotechnology Letters. 47:139-147 |
| بيانات النشر: | Korean Society for Microbiology and Biotechnology, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | chemistry.chemical_classification, Transamination, Glutamate decarboxylase, Glutamate receptor, Applied Microbiology and Biotechnology, Microbiology, Transaminase, law.invention, Enzyme, Photobacterium damselae, chemistry, Biochemistry, law, Recombinant DNA, Phosphofructokinase 2, Biotechnology |
| الوصف: | 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. |
| تدمد: | 2234-7305 1598-642X |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_________::654d312cc810b5b2a9a093729d5a1e53Test https://doi.org/10.4014/mbl.1804.04006Test |
| رقم الانضمام: | edsair.doi...........654d312cc810b5b2a9a093729d5a1e53 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 22347305 1598642X |
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