An enzyme which catalyzes the oxidation of methylglyoxal to pyruvic acid was partially purified from aqueous extracts of sheep liver acetone powders.NAD+ or NADP+ was necessary for the oxidation.Changes in methylglyoxal, pyruvate, and pyridine nucleotide were stoichiometrically equivalent.Of various carbonyl-containing compounds tested, only oc-keto aldehydes were substrates.Enzyme activity was found only in the supernatant fraction of liver cells.Evidence is presented that the conversion of methylglyoxal to pyruvate was direct and did not involve its preliminary conversion to lactate.Activity increased up to pH 10.4 with no indication of a pH optimum.
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Carl Monder (1967) studied this question.
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