title: Activation of aldehyde dehydrogenase at physiological temperatures.
abstract: The release of NADH from the enzyme.NADH complexes was rate limiting at 37 degrees, 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.
authors: Department of Chemistry and Biochemistry, Massey University, Palmerston North, New Zealand.
authors: J P
authors: JP
authors: Hill
authors: P D
authors: PD
authors: Buckley
authors: L F
authors: LF
authors: Blackwell
authors: R M
authors: RM
authors: Sime
authors: R L
authors: RL
authors: Kingston
mesh_terms: D000444:Aldehyde Dehydrogenase / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism; D000818:Animals; D001831:Body Temperature; D003600:Cytosol / Q000201:enzymology; D004789:Enzyme Activation; D008099:Liver / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D012756:Sheep
chemical_list: D000447:Aldehydes; D009243:NAD; C005556:propionaldehyde; D000444:Aldehyde Dehydrogenase