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Structure
Rabbit muscle aldolase 1ADO (Blom N & Sygusch J, Nat Struct Biol 1997, PMID:8989320); human ALDOA is highly homologous (Lys229 conserved).
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① F1,6BP docks onto Lys229
[schematic] Fructose-1,6-BP slides in with its C2 carbonyl facing the catalytic Lys229, which will form the Schiff base (no crystalline Michaelis complex exists; PubChem 3D geometry docked, marked schematic).
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② Schiff base → C3–C4 cleavage
[schematic] Lys229 ε-NH₂ attacks the C2 carbonyl to give a protonated imine (Schiff base); the electrophilic C3–C4 bond then breaks (retro-aldol). Covalent-intermediate step drawn schematically.
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③ DHAP out — G3P remains
[schematic] Dihydroxyacetone phosphate is released; G3P remains transiently Schiff-bound, then dissociates toward the GapDH step.
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Sequence
DNA/gene NCBI Gene 226 · protein UniProt P04075
› Backbones and ligand poses are taken directly from the listed PDB entries,
superposed into one common frame. Where no crystalline state exists for a step
(e.g., Michaelis geometry), the pose is drawn schematically using PubChem 3D
geometries and is labeled as such in the narration.