An NAD-specific succinic semialdehyde dehydrogenase from a Pseudomonas species has been purified. The enzyme has been shown to have low activity toward aminoaldehydes (3-aminopropanal or 4-aminobutanal) as substrate. It contains 24 sulfhydryls per molecule (164,000 daltons). The kinetic constants and the pH profiles with different substrates are documented.
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Callewaert et al. (1973) studied this question.
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