Effect of pyrophosphate ions and alkaline pH on the kinetics of propionaldehyde oxidation by sheep liver cytosolic aldehyde dehydrogenase.
Pyrophosphate ions activate the steady-state rate of oxidation of propionaldehyde by sheep liver cytosolic aldehyde dehydrogenase at alkaline pH values. The steps in the mechanism governing the release of NADH from terminal enzyme. NADH complexes have been shown to be rate-limiting at pH 7.6 [MacGibbon, Buckley & Blackwell (1977) Biochem J. 165, 455-462]. These steps are shown to be also rate-limiting at more alkaline pH values, and it is through an acceleration of these steps that pyrophosphate ions exert their activation effect.
Hill
J P
JP
Department of Chemistry and Biochemistry, Massey University, Palmerston North, New Zealand.
Buckley
P D
PD
Blackwell
L F
LF
Motion
R L
RL
D000444:Aldehyde Dehydrogenase / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism*; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D011756:Diphosphates / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010084:Oxidation-Reduction; D012756:Sheep; D013379:Substrate Specificity
D000447:Aldehydes; D011756:Diphosphates; C005556:propionaldehyde; D000444:Aldehyde Dehydrogenase