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- W1570473787 abstract "Abstract Methylmalonate semialdehyde dehydrogenase, an inducible enzyme from Pseudomonas aeruginosa which catalyzes the oxidation of methylmalonate semialdehyde to propionyl coenzyme A, was purified to the extent that a preparation was obtained which was homogenous by the criterion of disc gel electrophoresis. The molecular weight of the native enzyme was estimated to be 132,000 by gel filtration. Methylmalonate semialdehyde dehydrogenase dissociated into subunits in urea or sodium dodecyl sulfate solutions. The molecular weight of the subunit was estimated at between 58,000 and 69,000 by the techniques of gel electrophoresis and gel filtration in sodium dodecyl sulfate, respectively, which means that the native enzyme is composed of at least two subunits. The purified enzyme catalyzed the reduction of NAD with methylmalonate semialdehyde and propionaldehyde. In the presence of CoA, propionyl-CoA was a product of methylmalonate semialdehyde oxidation. The enzyme was active when mercaptoethanol replaced CoA and an active propionyl derivative was formed then as well. The stoichiometry between NADH and propionyl-CoA was 1:1. 3-Hydroxyisobutyrate dehydrogenase and 3-hydroxyisobutyrate-1-14C were used to generate methylmalonate semialdehyde-1-14C, and radioactive carbon dioxide was produced when methylmalonate semialdehyde dehydrogenase was present in the reaction mixture. The Michaelis constants for methylmalonate semialdehyde, NAD, CoA, mercaptoethanol, and propionaldehyde were determined. The proposal is made that the physiological role of methylmalonate semialdehyde dehydrogenase in cell metabolism is to catalyze the oxidation of methylmalonate semialdehyde to propionyl-CoA in the catabolism of valine." @default.
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- W1570473787 date "1970-04-01" @default.
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- W1570473787 title "Properties of Purified Methylmalonate Semialdehyde Dehydrogenase of Pseudomonas aeruginosa" @default.
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- W1570473787 doi "https://doi.org/10.1016/s0021-9258(19)77166-x" @default.
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