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Pivotal Enzyme in Glutamate Metabolism of Poly-γ-Glutamate-Producing Microbes

The extremely halophilic archaeon Natrialba aegyptiaca secretes the L-homo type of poly-γ-glutamate (PGA) as an extremolyte. We examined the enzymes involved in glutamate metabolism and verified the presence of L-glutamate dehydrogenases, L-aspartate aminotransferase, and L-glutamate synthase. Howev...

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Autores principales: Ashiuchi, Makoto, Yamamoto, Takashi, Kamei, Tohru
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4187202/
https://www.ncbi.nlm.nih.gov/pubmed/25371338
http://dx.doi.org/10.3390/life3010181
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author Ashiuchi, Makoto
Yamamoto, Takashi
Kamei, Tohru
author_facet Ashiuchi, Makoto
Yamamoto, Takashi
Kamei, Tohru
author_sort Ashiuchi, Makoto
collection PubMed
description The extremely halophilic archaeon Natrialba aegyptiaca secretes the L-homo type of poly-γ-glutamate (PGA) as an extremolyte. We examined the enzymes involved in glutamate metabolism and verified the presence of L-glutamate dehydrogenases, L-aspartate aminotransferase, and L-glutamate synthase. However, neither glutamate racemase nor D-amino acid aminotransferase activity was detected, suggesting the absence of sources of D-glutamate. In contrast, D-glutamate-rich PGA producers mostly possess such intracellular sources of D-glutamate. The results of our present study indicate that the D-glutamate-anabolic enzyme “glutamate racemase” is pivotal in the biosynthesis of PGA.
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spelling pubmed-41872022014-10-27 Pivotal Enzyme in Glutamate Metabolism of Poly-γ-Glutamate-Producing Microbes Ashiuchi, Makoto Yamamoto, Takashi Kamei, Tohru Life (Basel) Communication The extremely halophilic archaeon Natrialba aegyptiaca secretes the L-homo type of poly-γ-glutamate (PGA) as an extremolyte. We examined the enzymes involved in glutamate metabolism and verified the presence of L-glutamate dehydrogenases, L-aspartate aminotransferase, and L-glutamate synthase. However, neither glutamate racemase nor D-amino acid aminotransferase activity was detected, suggesting the absence of sources of D-glutamate. In contrast, D-glutamate-rich PGA producers mostly possess such intracellular sources of D-glutamate. The results of our present study indicate that the D-glutamate-anabolic enzyme “glutamate racemase” is pivotal in the biosynthesis of PGA. MDPI 2013-02-06 /pmc/articles/PMC4187202/ /pubmed/25371338 http://dx.doi.org/10.3390/life3010181 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Communication
Ashiuchi, Makoto
Yamamoto, Takashi
Kamei, Tohru
Pivotal Enzyme in Glutamate Metabolism of Poly-γ-Glutamate-Producing Microbes
title Pivotal Enzyme in Glutamate Metabolism of Poly-γ-Glutamate-Producing Microbes
title_full Pivotal Enzyme in Glutamate Metabolism of Poly-γ-Glutamate-Producing Microbes
title_fullStr Pivotal Enzyme in Glutamate Metabolism of Poly-γ-Glutamate-Producing Microbes
title_full_unstemmed Pivotal Enzyme in Glutamate Metabolism of Poly-γ-Glutamate-Producing Microbes
title_short Pivotal Enzyme in Glutamate Metabolism of Poly-γ-Glutamate-Producing Microbes
title_sort pivotal enzyme in glutamate metabolism of poly-γ-glutamate-producing microbes
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4187202/
https://www.ncbi.nlm.nih.gov/pubmed/25371338
http://dx.doi.org/10.3390/life3010181
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