Lactoylglutathione lyase

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


 * (R)-S-lactoylglutathione $$\rightleftharpoons$$ glutathione + methylglyoxal

Hence, this enzyme has one substrate, (R)-S-lactoylglutathione, and two products, glutathione and methylglyoxal.

This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing glutathione-forming). Other names in common use include methylglyoxalase, aldoketomutase, ketone-aldehyde mutase, glyoxylase I, and (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing). This enzyme participates in pyruvate metabolism. At least one compound, S-(N-Hydroxy-N-methylcarbamoyl)glutathione is known to inhibit this enzyme. The human version of this enzyme is GLO1.

Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , and.