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Saccharopine, an Intermediate of the Aminoadipic Acid Pathway of Lysine Biosynthesis

IV. SACCHAROPINE DEHYDROGENASE

From the ¹ From the Laboratory of Biochemistry, Department of Dairy Science, University of Illinois, Urbana, Illinois 61803

The -amino group of lysine arises in yeast and Neurospora from glutamate in a unique transamination between -aminoadipic -semialdehyde and glutamate involving the stable intermediate saccharopine.

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The enzyme catalyzing the terminal reaction, saccharopine dehydrogenase (-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming)) has been purified and shown to be a sulfhydryl enzyme having an approximate molecular weight of 49,000. Two distinct pH optima (approximately 10 and 7) exist for the forward and reverse directions of the enzyme-catalyzed reaction. The enzyme is stabilized in the presence of relatively high salt concentrations and has been shown to display a high degree of specificity with respect to the coenzyme and substrates. The Michaelis constants for lysine, oxoglutarate, and reduced nicotinamide adenine dinucleotide have been found to be 1.2 x 10^-2 M, 4.4 x 10^-4 M, and 4.6 x 10^-5 M, respectively.

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