ArticleJournal of bacteriology2010
Functional roles of the conserved Glu304 loop of Bacillus subtilis glutamine synthetase.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Systems metabolic engineering ofSynthetic and systems biotechnology · 2025Article
- The metabolic engineering of Escherichia coli for the high-yield production of hypoxanthine.Microbial cell factories · 2024Article
- Engineering of Shikimate Pathway and Terminal Branch for Efficient Production of L-Tryptophan inInternational journal of molecular sciences · 2023Article
- Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.Nature communications · 2022Article
- Novel Glutamate-Putrescine Ligase Activity inBiomolecules · 2021Article
- Role of GlnR in Controlling Expression of Nitrogen Metabolism Genes inJournal of bacteriology · 2020Article
- EngineeringSynthetic and systems biotechnology · 2020Article
- Phosphorylation of Glutamine Synthetase on Threonine 301 Contributes to Its Inactivation During Epilepsy.Frontiers in molecular neuroscience · 2019Article
- The Molecular Basis of TnrA Control by Glutamine Synthetase in Bacillus subtilis.The Journal of biological chemistry · 2016Article
- The structures of cytosolic and plastid-located glutamine synthetases from Medicago truncatula reveal a common and dynamic architecture.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Structures of the Bacillus subtilis glutamine synthetase dodecamer reveal large intersubunit catalytic conformational changes linked to a unique feedback inhibition mechanism.The Journal of biological chemistry · 2013Article
- A sensing role of the glutamine synthetase in the nitrogen regulation network in Fusarium fujikuroi.PloS one · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
The enzymatic activity of Bacillus subtilis glutamine synthetase (GS), which catalyzes the synthesis of glutamine from ammonium and glutamate, is regulated by glutamine feedback inhibition. The feedback-inhibited form of B. subtilis GS regulates the DNA-binding activities of the TnrA and GlnR nitrogen transcriptional factors. Bacterial GS proteins contain a flexible seven-residue loop, the Glu304 flap, that closes over the glutamate entrance to the active site. Amino acid substitutions in Glu304 flap residues were examined for their effects on gene regulation, enzymatic activity, and feedback inhibition. Substitutions in five of the Glu304 loop residues resulted in constitutive expression of both TnrA- and GlnR-regulated genes, indicating that this flap is important for regulating the activity of these transcription factors. The residues in the highly conserved Glu304 flap appear to be optimized for glutamate binding because mutant enzymes with substitutions in five of the flap residues had increased glutamate Km values compared to that for wild-type GS. The E304A and E304D substitutions increased the ammonium Km values compared to that for wild-type GS and conferred high-level resistance to inhibition by glutamine, glycine, and methionine sulfoximine. A model for the role of the Glu304 residue in glutamine feedback inhibition is proposed.
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