ArticleExtremophiles : life under extreme conditions2014
Ferredoxin-dependent glutamate synthase: involvement in ammonium assimilation in Haloferax mediterranei.
Article in Extremophiles : life under extreme conditions, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Soil water limitation intensity alters nitrogen cycling at the plant-soil interface in Scots pine mesocosms.Plant and soil · 2025Article
- Transcriptome analysis of nitrogen assimilation preferences inFrontiers in microbiology · 2025Article
- Analysis of Lsm Protein-Mediated Regulation in the HaloarchaeonInternational journal of molecular sciences · 2024Article
- Novel Glutamate-Putrescine Ligase Activity inBiomolecules · 2021Article
- Microorganisms and Their Metabolic Capabilities in the Context of the Biogeochemical Nitrogen Cycle at Extreme Environments.International journal of molecular sciences · 2020Review
- Essentiality of the glnA gene in Haloferax mediterranei: gene conversion and transcriptional analysis.Extremophiles : life under extreme conditions · 2020Article
- Purification and characterization of a novel glutamate dehydrogenase from Geotrichum candidum with higher alcohol and amino acid activity.AMB Express · 2017Article
- Nitrate reduction in Haloferax alexandrinus: the case of assimilatory nitrate reductase.Extremophiles : life under extreme conditions · 2017Article
- Environmental selection pressures related to iron utilization are involved in the loss of the flavodoxin gene from the plant genome.Genome biology and evolution · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutamate synthase (GOGAT) is one of the two important enzymes involved in the ammonium assimilation pathway glutamine synthetase (GS)/GOGAT, which enables Hfx. mediterranei to thrive in media with low ammonium concentration or containing just nitrate as single nitrogen source. The gene coding for this enzyme, gltS, has been sequenced, analysed and compared with other GOGATs from different organisms from the three domains of life. According to its amino acid sequence, Hfx. mediterranei GOGAT displays high homology with those from other archaeal halophilic organisms and with the bacterial alpha-like subunit. Hfx. mediterranei GOGAT and GS expression was induced under conditions of ammonium restriction. The GOGAT protein was found to be a monomer with a molecular mass of 163.78 kDa, which is consistent with that estimated by gel filtration, 198 ± 30 kDa. The enzyme is highly ferredoxin dependent: activity was only observed with one of the two different 2Fe-2S ferredoxins chromatographically isolated from Hfx. mediterranei. The enzyme also displayed typical halophilic behaviour, being fully stable, and producing maximal activity, at salt concentrations from 3 to 4 M NaCl, pH 7.5 and a temperature of 50 °C.
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