Abstract
Mammalian pyruvate dehydrogenase actively catalyzed the oxidation of methylglyoxal to acetyl-CoA. The reaction was fully enzymatic with an estimated K m of 1.89 m m. On the other hand, methylglyoxal was a competitive inhibitor of the enzyme for pyruvate, the K i being in the 1 m m range. The reaction was inhibited in the presence of HgCl 2. The reaction products were quantitatively identified as acetyl-CoA and formic acid. A mechanism for the reaction is proposed.
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