Glutarate semialdehyde dehydrogenase of Pseudomonas. Purification, properties, and relation to L-lysine catabolism.

Abstract

The lysine-induced glutarate semialdehyde dehydrogenase of Pseudomonas was purified to electrophoretic homogeneity from a mutant strain lacking delta-aminovalerate transaminase. The properties of the enzyme, including molecular weight, amino acid composition, electrophoretic behavior, and kinetic features, distinguish it from similar dehydrogenases induced… (More)

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