page_title: Isocitrate lyase
hierarchical_section_title: Isocitrate lyase
caption_attribution_description: English: This file shows the hometetrameric structure of isocitrate lyase. Each chain is in a different color. In chain A (the blue chain), amino acid residues corresponding to catalytic residues have been highlighted.
context_page_description: Isocitrate lyase, or ICL, is an enzyme in the glyoxylate cycle that catalyzes the cleavage of isocitrate to succinate and glyoxylate. Together with malate synthase, it bypasses the two decarboxylation steps of the tricarboxylic acid cycle and is used by bacteria, fungi, and plants.
  The systematic name of this enzyme class is isocitrate glyoxylate-lyase. Other names in common use include isocitrase, isocitritase, isocitratase, threo-Ds-isocitrate glyoxylate-lyase, and isocitrate glyoxylate-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
context_section_description: Isocitrate lyase (EC 4.1.3.1), or ICL, is an enzyme in the glyoxylate cycle that catalyzes the cleavage of isocitrate to succinate and glyoxylate. Together with malate synthase, it bypasses the two decarboxylation steps of the tricarboxylic acid cycle (TCA cycle) and is used by bacteria, fungi, and plants.
  The systematic name of this enzyme class is isocitrate glyoxylate-lyase (succinate-forming). Other names in common use include isocitrase, isocitritase, isocitratase, threo-Ds-isocitrate glyoxylate-lyase, and isocitrate glyoxylate-lyase.  This enzyme participates in glyoxylate and dicarboxylate metabolism.
caption: Homotetrameric structure of Isocitrate lyase from E. coli.  Based on PDB 1IGW.[1]
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