A soluble enzyme which catalyzes the oxidation of 2-aminoadipic semialdehyde to 2-aminoadipate has been partially purified from rat liver cytoplasm. The enzyme, which exhibits a sharp optimum activity at pH 7.5, requires NAD+ and shows a high degree of substrate specificity. It is more sensitive to heat than is the common nonspecific aldehyde dehydrogenase, which does not act on 2-aminoadipic semialdehyde. The apparent Km values for NAD+ and 2-aminoadipic semialdehyde were estimated to be 0.2 mm and 0.02 mm, respectively. The molecular weight of the enzyme was estimated to be 250,000.
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Tsai et al. (1974) studied this question.
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