ArticleMolecular biotechnology2026
Evaluation of ADP Glucose Pyrophosphorylase Subunit Interaction in Wheat by Binding Free Energy Calculations.
Article in Molecular biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
ADP-glucose pyrophosphorylase (AGPase; E.C. 2.7.7.27) is the rate-limiting enzyme catalyzing the first committed step of starch biosynthesis in higher plants. The enzyme functions as a heterotetramer comprising two large (LS) and two small (SS) subunits that share 47.02% sequence identity in wheat. To elucidate the structural mechanism underlying heterotetramer assembly, we generated six possible dimeric conformations based on two-fold symmetry, three side-by-side (D1, D2, D3), and three upside-down (D4, D5, D6) orientations and evaluated their stability through all-atom molecular dynamics (MD) simulations combined with MM-GBSA and MM-PBSA free energy analyses. Among all configurations, the D2 heterodimer emerged as the most stable, exhibiting the lowest binding free energy (-15.2 kcal·mol⁻
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