In intact rat liver mitochondria acetaldehyde is oxidazed by three functionally distinct dehydrogenase systems. Two of these reduce intramitochondrial nicotinamide adenine dinucleotide (NAD): one is operative with micromolar acetaldehyde concentrations and is stimulated by Mg^2+, the other is operative with millimolar acetaldehyde concentrations and is stimulated by adenosine 5'-triphosphate (ATP). The third system reduces added NAD and is stimulated by rotenone. Connected to these systems, three aldehyde dehydrogenase isozymes (ALDH) have been purified: a low-K(m) ALDH activated by Mg^2+, a high-K(m) ALDH activated by ATP and Mg^2+, a high-Km ALDH activated by rotenone. The properties of some isozymes are affected by detergents. Thus, deoxycholate augments the stimulation of low-K isozyme by Mg^2+ and confers sensitivity to Mg^2+ and ATP on one of the high-K(m) isozymes. A fourth isozyme has been purified. Its affinity for acetaldehyde is so low that it is very unlikely that acetaldehyde is the physiological substrate.

Keywords:
Aldehyde dehydrogenase, Acetaldehyde oxidation, Mg^2 + effect, ATP effect, Rotenone effect
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1988
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