Methylglyoxal (MGO) is generated as a by-product of glycolysis (~0.1% - 0.4% of the total glycolytic flux). Under physiologic conditions, MGO is detoxified by the glyoxalase system, which is comprised of two enzymes (glyoxalase 1, GLO1, and GLO2). When this system is compromised (e.g. diabetes, cancer), concentrations of MGO are elevated, resulting in protein and DNA modifications. As a result, systems are in place to remove these potentially damaging modifications. We have shown that the deglycase, DJ-1, is capable of repairing modified Arg residues. We are interested in fully understanding these enzymatic reactions and elucidating the consequences of MGO modifications in disease. Enzymatic reactions are shown in green.  

Recently, we have identified a novel lysine modification derived from the glyoxalase cycle intermediate, lactoylglutathione. Read about it here!