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/lp/karger/acetaldehyde-oxidation-in-rat-liver-mitochondria-action-of-mg-2-atp-yRZv3xwwl8
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- Publisher
- Karger
- Copyright
- © 1988 S. Karger AG, Basel
- ISSN
- 0013-9432
- eISSN
- 2504-2564
- DOI
- 10.1159/000469091
- Publisher site
- See Article on Publisher Site
Abstract
In intact rat liver mitochondria acetaldehyde is oxidazed by three functionallydistinct dehydrogenase systems. Two of these reduce intramitochondrial nicotinamide adeninedinucleotide (NAD): one is operative with micromolar acetaldehyde concentrations andis stimulated by Mg^2+, the other is operative with millimolar acetaldehyde concentrationsand is stimulated by adenosine 5'-triphosphate (ATP). The third system reduces added NADand is stimulated by rotenone. Connected to these systems, three aldehyde dehydrogenaseisozymes (ALDH) have been purified: a low-K(m) ALDH activated by Mg^2+, a high-K(m) ALDHactivated by ATP and Mg^2+, a high-Km ALDH activated by rotenone. The properties of someisozymes are affected by detergents. Thus, deoxycholate augments the stimulation of low-Kisozyme 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 veryunlikely that acetaldehyde is the physiological substrate.
Journal
Enzyme – Karger
Published: Jan 1, 2017
Keywords: Aldehyde dehydrogenase; Acetaldehyde oxidation; Mg^2 + effect; ATP effect; Rotenone effect