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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
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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. |
format | Online Article Text |
id | pubmed-4187202 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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