Abstract
Pure preparations of the high- k m aldehyde reductase from rat brain catalyse the NADPH-dependent reduction of succinic semialdehyde to γ-hydroxybutyrate. The high-speed supernatant fraction from rat brain contains a second enzyme, succinic semialdehyde reductase. that will catalyse this reaction using either NADPH or NADH but, unlike the high- k m aldehyde reductase, is insensitive to inhibition by barbiturates. Alcohol dehydrogenase is also able to catalyse the reversible NAD −-dependent oxidation of γ-hydroxybutyrate. The kinetic parameters of these enzymes have been compared and indicate that only the succinic semialdehyde reductase is likely to play a significant role in the metabolism of this compound in vitro.
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