Methylisocitrate lyase

In enzymology, a methylisocitrate lyase is an enzyme that catalyzes the chemical reaction


 * (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate $$\rightleftharpoons$$ succinate + pyruvate

Hence, this enzyme has one substrate, (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate, and two products, succinate and pyruvate.

This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase (succinate-forming). Other names in common use include 2-methylisocitrate lyase, MICL, and (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase. This enzyme participates in propanoate metabolism.

Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes, , , , , and.