Abstract
Malonic semialdehyde dehydrogenase, which catalyzes the diphosphopyridine nucleotide oxidation of malonic semialdehyde to malonate according to the reaction: malonic semialdehyde + DPN + + H 2O → malonic acid + DPNH + H + has been partially purified from soluble extracts of Pseudomonas aeruginosa. The best preparation obtained has been purified approximately 200 fold. The pH optimum is near 8.7 and the Michaelis constant for the malonic semialdehydee is 4·3 10 −5 M and that for the diphosphopyridine nucleotide 1.1·10 −4, both with the standard assay system. Purification procedures and some properties of the enzyme are described.
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