Activation of aldehyde dehydrogenase at physiological temperatures

The release of NADH from the enzyme·NADH complexes was rate limiting at 37°, for the oxidation of propionaldehyde by sheep liver cytosolic aldehyde dehydrogenase. Marked substrate activation was observed at this temperature as was activation by p-(chloromercuri)benzoate. Activation of enzymic activi...

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Veröffentlicht in:	Biochemical pharmacology 1992-12, Vol.44 (12), p.2425-2426
Hauptverfasser:	Hill, Jeremy P., Buckley, Paul D., Blackwell, Leonard F., Sime, Richard M., Kingston, Richard L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alcoholism and acute alcohol poisoning Aldehyde Dehydrogenase - metabolism Aldehydes - metabolism Animals Biological and medical sciences Body Temperature Cytosol - enzymology Enzyme Activation Liver - enzymology Medical sciences NAD - metabolism Sheep Toxicology
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Beschreibung
Zusammenfassung:	The release of NADH from the enzyme·NADH complexes was rate limiting at 37°, for the oxidation of propionaldehyde by sheep liver cytosolic aldehyde dehydrogenase. Marked substrate activation was observed at this temperature as was activation by p-(chloromercuri)benzoate. Activation of enzymic activity may be of importance in vivo.
ISSN:	0006-2952 1873-2968
DOI:	10.1016/0006-2952(92)90692-C