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Metabolism of Pipecolic Acid in a Pseudomonas Species

III. l--AMINOADIPATE -SEMIALDEHYDE:NICOTINAMIDE ADENINE DINUCLEOTIDE OXIDOREDUCTASE

From the ¹ From the Department of Biochemistry, Medical School, University of California, San Francisco Medical Center, San Francisco, California 94122

A highly specific soluble enzyme catalyzing essentially irreversibly the nicotinamide adenine dinucleotide (phosphate)-dependent oxidation of l--aminoadipate -semialdehyde to l--aminoadipate is induced in Pseudomonas P2 by growth on dl-pipecolate. This enzyme has been purified 20-fold to a specific activity of 4.9 units per mg, at pH 7.0, in five steps, with an over-all recovery of 46%.

The enzyme, which is optimally active at pH 8.2, shows a high degree of substrate specificity and does not act on glutamate -semialdehyde (¹-pyrroline-5-carboxylate). Kinetic constants for the substrate and for several coenzyme analogues are presented, together with evidence that the open chain aminoaldehyde form of the substrate may be the species bound initially to the enzyme.

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