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Structure
Human ENO1 scaffold 2PSN (the entry has no standalone PMID, i.e. "to be published").
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Metal-site mechanism
Mg²⁺ octahedral coordination at the enolase high-affinity metal site: Wedekind JE, Reed GH & Rayment I, Biochemistry 1995, PMID:7703246 (1EBH, yeast enolase — enolase metal/mechanism is highly conserved).
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② 2PG chelates Mg²⁺
[schematic] 2-phosphoglycerate docks with its carboxylate and C2-OH chelating the Mg²⁺ ions (PubChem geometry, schematic), which polarize the substrate and sharpen the C2 proton toward the catalytic lysine.
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③ Anti-elimination of water
[schematic] Conserved Lys342 abstracts the C2 proton while conserved Glu209 protonates the departing C3-OH, eliminating water anti; the Mg²⁺-stabilized enolate gives PEP.
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④ PEP released
[schematic] PEP exits toward pyruvate kinase; its phosphate hydrolysis ΔG is nearly double that of ATP — the high-energy molecule metabolized by PK.
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Sequence
DNA/gene NCBI Gene 2023 · protein UniProt P06733
› 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.