The Experts below are selected from a list of 9 Experts worldwide ranked by ideXlab platform
J. Esclapez - One of the best experts on this subject based on the ideXlab platform.
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novel glutamate putrescine Ligase activity in haloferax mediterranei a new function for glna 2 gene
Biomolecules, 2021Co-Authors: Veronica Rodriguezherrero, Monica Camacho, Vanesa Bautista, Arnau Peris, J. EsclapezAbstract:The genome of the halophilic archaea Haloferax mediterranei contains three ORFs that show homology with glutamine synthetase (GS) (glnA-1, glnA-2, and glnA-3). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of Ligases, including 20 subclasses of other different enzymes, such as Aspartate–Ammonia Ligase (EC 6.3.1.1), glutamate–ethylamine Ligase (EC 6.3.1.6), and glutamate–putrescine Ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine Ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine Ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine Ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine Ligase’s activity and the analysis of the transcriptional and translational expression of the glnA-2 gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the Archaea domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain.
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Novel Glutamate–Putrescine Ligase Activity in Haloferax mediterranei: A New Function for glnA-2 Gene
'MDPI AG', 2021Co-Authors: Verónica Rodríguez-herrero, Monica Camacho, J. Esclapez, Vanesa Bautista, Arnau Peris, María-josé BoneteAbstract:The genome of the halophilic archaea Haloferax mediterranei contains three ORFs that show homology with glutamine synthetase (GS) (glnA-1, glnA-2, and glnA-3). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of Ligases, including 20 subclasses of other different enzymes, such as Aspartate–Ammonia Ligase (EC 6.3.1.1), glutamate–ethylamine Ligase (EC 6.3.1.6), and glutamate–putrescine Ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine Ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine Ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine Ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine Ligase’s activity and the analysis of the transcriptional and translational expression of the glnA-2 gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the Archaea domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain
Veronica Rodriguezherrero - One of the best experts on this subject based on the ideXlab platform.
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novel glutamate putrescine Ligase activity in haloferax mediterranei a new function for glna 2 gene
Biomolecules, 2021Co-Authors: Veronica Rodriguezherrero, Monica Camacho, Vanesa Bautista, Arnau Peris, J. EsclapezAbstract:The genome of the halophilic archaea Haloferax mediterranei contains three ORFs that show homology with glutamine synthetase (GS) (glnA-1, glnA-2, and glnA-3). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of Ligases, including 20 subclasses of other different enzymes, such as Aspartate–Ammonia Ligase (EC 6.3.1.1), glutamate–ethylamine Ligase (EC 6.3.1.6), and glutamate–putrescine Ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine Ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine Ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine Ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine Ligase’s activity and the analysis of the transcriptional and translational expression of the glnA-2 gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the Archaea domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain.
Monica Camacho - One of the best experts on this subject based on the ideXlab platform.
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novel glutamate putrescine Ligase activity in haloferax mediterranei a new function for glna 2 gene
Biomolecules, 2021Co-Authors: Veronica Rodriguezherrero, Monica Camacho, Vanesa Bautista, Arnau Peris, J. EsclapezAbstract:The genome of the halophilic archaea Haloferax mediterranei contains three ORFs that show homology with glutamine synthetase (GS) (glnA-1, glnA-2, and glnA-3). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of Ligases, including 20 subclasses of other different enzymes, such as Aspartate–Ammonia Ligase (EC 6.3.1.1), glutamate–ethylamine Ligase (EC 6.3.1.6), and glutamate–putrescine Ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine Ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine Ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine Ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine Ligase’s activity and the analysis of the transcriptional and translational expression of the glnA-2 gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the Archaea domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain.
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Novel Glutamate–Putrescine Ligase Activity in Haloferax mediterranei: A New Function for glnA-2 Gene
'MDPI AG', 2021Co-Authors: Verónica Rodríguez-herrero, Monica Camacho, J. Esclapez, Vanesa Bautista, Arnau Peris, María-josé BoneteAbstract:The genome of the halophilic archaea Haloferax mediterranei contains three ORFs that show homology with glutamine synthetase (GS) (glnA-1, glnA-2, and glnA-3). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of Ligases, including 20 subclasses of other different enzymes, such as Aspartate–Ammonia Ligase (EC 6.3.1.1), glutamate–ethylamine Ligase (EC 6.3.1.6), and glutamate–putrescine Ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine Ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine Ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine Ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine Ligase’s activity and the analysis of the transcriptional and translational expression of the glnA-2 gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the Archaea domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain
Vanesa Bautista - One of the best experts on this subject based on the ideXlab platform.
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novel glutamate putrescine Ligase activity in haloferax mediterranei a new function for glna 2 gene
Biomolecules, 2021Co-Authors: Veronica Rodriguezherrero, Monica Camacho, Vanesa Bautista, Arnau Peris, J. EsclapezAbstract:The genome of the halophilic archaea Haloferax mediterranei contains three ORFs that show homology with glutamine synthetase (GS) (glnA-1, glnA-2, and glnA-3). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of Ligases, including 20 subclasses of other different enzymes, such as Aspartate–Ammonia Ligase (EC 6.3.1.1), glutamate–ethylamine Ligase (EC 6.3.1.6), and glutamate–putrescine Ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine Ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine Ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine Ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine Ligase’s activity and the analysis of the transcriptional and translational expression of the glnA-2 gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the Archaea domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain.
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Novel Glutamate–Putrescine Ligase Activity in Haloferax mediterranei: A New Function for glnA-2 Gene
'MDPI AG', 2021Co-Authors: Verónica Rodríguez-herrero, Monica Camacho, J. Esclapez, Vanesa Bautista, Arnau Peris, María-josé BoneteAbstract:The genome of the halophilic archaea Haloferax mediterranei contains three ORFs that show homology with glutamine synthetase (GS) (glnA-1, glnA-2, and glnA-3). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of Ligases, including 20 subclasses of other different enzymes, such as Aspartate–Ammonia Ligase (EC 6.3.1.1), glutamate–ethylamine Ligase (EC 6.3.1.6), and glutamate–putrescine Ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine Ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine Ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine Ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine Ligase’s activity and the analysis of the transcriptional and translational expression of the glnA-2 gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the Archaea domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain
Arnau Peris - One of the best experts on this subject based on the ideXlab platform.
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novel glutamate putrescine Ligase activity in haloferax mediterranei a new function for glna 2 gene
Biomolecules, 2021Co-Authors: Veronica Rodriguezherrero, Monica Camacho, Vanesa Bautista, Arnau Peris, J. EsclapezAbstract:The genome of the halophilic archaea Haloferax mediterranei contains three ORFs that show homology with glutamine synthetase (GS) (glnA-1, glnA-2, and glnA-3). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of Ligases, including 20 subclasses of other different enzymes, such as Aspartate–Ammonia Ligase (EC 6.3.1.1), glutamate–ethylamine Ligase (EC 6.3.1.6), and glutamate–putrescine Ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine Ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine Ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine Ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine Ligase’s activity and the analysis of the transcriptional and translational expression of the glnA-2 gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the Archaea domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain.
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Novel Glutamate–Putrescine Ligase Activity in Haloferax mediterranei: A New Function for glnA-2 Gene
'MDPI AG', 2021Co-Authors: Verónica Rodríguez-herrero, Monica Camacho, J. Esclapez, Vanesa Bautista, Arnau Peris, María-josé BoneteAbstract:The genome of the halophilic archaea Haloferax mediterranei contains three ORFs that show homology with glutamine synthetase (GS) (glnA-1, glnA-2, and glnA-3). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of Ligases, including 20 subclasses of other different enzymes, such as Aspartate–Ammonia Ligase (EC 6.3.1.1), glutamate–ethylamine Ligase (EC 6.3.1.6), and glutamate–putrescine Ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine Ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine Ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine Ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine Ligase’s activity and the analysis of the transcriptional and translational expression of the glnA-2 gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the Archaea domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain
