ArticleProtein science : a publication of the Protein Society2019
Allosteric discrimination at the NADH/ADP regulatory site of glutamate dehydrogenase.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- MitCOM-based prognostic model identifies GLUD1 as a key suppressor of glioblastoma growth and invasion through regulation of mitochondrial structure and metabolism.Cancer cell international · 2025Article
- The role of glutamate dehydrogenase in the ageing brain.Frontiers in pharmacology · 2025Review
- GLUD1 inhibits hepatocellular carcinoma progression via ROS-mediated p38/JNK MAPK pathway activation and mitochondrial apoptosis.Discover oncology · 2024Article
- Glutamate dehydrogenase hyperinsulinism: mechanisms, diagnosis, and treatment.Orphanet journal of rare diseases · 2023Review
- Allosteric discrimination at the NADH/ADP regulatory site of glutamate dehydrogenase.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Glutamate dehydrogenase (GDH) is a target for treating insulin-related disorders, such as hyperinsulinism hyperammonemia syndrome. Modeling native ligand binding has shown promise in designing GDH inhibitors and activators. Our computational investigation of the nicotinamide adenine diphosphate hydride (NADH)/adenosine diphosphate (ADP) site presented in this paper provides insight into the opposite allosteric effects induced at a single site of binding inhibitor NADH versus activator ADP to GDH. The computed binding free-energy difference between NADH and ADP using thermodynamic integration is -0.3 kcal/mol, which is within the -0.275 and -1.7 kcal/mol experimental binding free-energy difference range. Our simulations show an interesting model of ADP with dissimilar binding conformations at each NADH/ADP site in the GDH trimer, which explains the poorly understood strong binding but weak activation shown in experimental studies. In contrast, NADH showed similar inhibitory binding conformations at each NADH/ADP site. The structural analysis of the important residues in the NADH/ADP binding site presented in this paper may provide potential targets for mutation studies for allosteric drug design.
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