The oxidation of methylglyoxal by mammalian pyruvate dehydrogenase

Mammalian pyruvate dehydrogenase actively catalyzed the oxidation of methylglyoxal to acetyl-CoA. The reaction was fully enzymatic with an estimated Km of 1.89 mM. On the other hand, methylglyoxal was a competitive inhibitor of the enzyme for pyruvate, the Ki being in the 1 mM range. The reaction was inhibited in the presence of HgCl2. The reaction products were quantitatively identified as acetyl-CoA and formic acid. A mechanism for the reaction is proposed.