ArticleInternational journal of molecular sciences2022
Structural Basis for the Binding of Allosteric Activators Leucine and ADP to Mammalian Glutamate Dehydrogenase.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- RIMKLA promotes hypertension by activating PKM2 to trigger VSMC phenotype switch.Military Medical Research · 2026Article
- Review
- Neanderthal and Denisovan Glutamate Dehydrogenase 2 Evolution and Clinical Significance.International journal of molecular sciences · 2025Article
- Enzymatic Synthesis of Biologically ActiveBiomolecules · 2024Article
- Mitolnc controls cardiac BCAA metabolism and heart hypertrophy by allosteric activation of BCKDH.Nucleic acids research · 2024Article
- Evolutionary Changes in Primate Glutamate Dehydrogenases 1 and 2 Influence the Protein Regulation by Ligands, Targeting and Posttranslational Modifications.International journal of molecular sciences · 2024Review
- The Mitochondrial Protein MitoNEET as a Probe for the Allostery of Glutamate Dehydrogenase.Molecules (Basel, Switzerland) · 2022Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Glutamate dehydrogenase (GDH) plays a key role in the metabolism of glutamate, an important compound at a cross-road of carbon and nitrogen metabolism and a relevant neurotransmitter. Despite being one of the first discovered allosteric enzymes, GDH still poses challenges for structural characterization of its allosteric sites. Only the structures with ADP, and at low (3.5 Å) resolution, are available for mammalian GDH complexes with allosteric activators. Here, we aim at deciphering a structural basis for the GDH allosteric activation using bovine GDH as a model. For the first time, we report a mammalian GDH structure in a ternary complex with the activators leucine and ADP, co-crystallized with potassium ion, resolved to 2.45 Å. An improved 2.4-angstrom resolution of the GDH complex with ADP is also presented. The ternary complex with leucine and ADP differs from the binary complex with ADP by the conformation of GDH C-terminus, involved in the leucine binding and subunit interactions. The potassium site, identified in this work, may mediate interactions between the leucine and ADP binding sites. Our data provide novel insights into the mechanisms of GDH activation by leucine and ADP, linked to the enzyme regulation by (de)acetylation.
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Registered trials
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