ArticleProtein science : a publication of the Protein Society2025
Allosteric regulation of L-lactate dehydrogenase: Beyond effector-mediated tetramerization.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Allosteric regulation of L-lactate dehydrogenase: Beyond effector-mediated tetramerization.Protein science : a publication of the Protein Society · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
The activity of allosterically regulated enzyme is modulated through structural changes induced by effectors. L-lactate dehydrogenase from Geobacillus stearothermophilus (GsLDH) catalyzes the reversible conversion between pyruvate and lactate using NAD(H), and its activity is known to be activated by fructose 1,6-bisphosphate (FBP). However, the molecular basis of this regulation has not been explored using molecular dynamics (MD) simulations. In this study, we integrated MD simulations with biochemical assays to investigate the impact of FBP on GsLDH structure and function. MD revealed that FBP stabilizes the tetrameric form, reduces residue flexibility, and enhances pyruvate interactions with active site residues, despite a 23 Å distance between binding sites. Using MDavocado, we identified three P-axis-related dimer interface regions critical for stability and structural integrity. Microcalorimetry titration revealed that NADH binding (K
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