S. Francis, B. P. Meriwether, J. H. Park
Sep 10, 1971
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Journal
The Journal of biological chemistry
Abstract
Abstract The interaction of 3-phosphoglyceraldehyde dehydrogenase with NAD and adenine nucleotides has been studied. The effects of these compounds on the individual steps in several catalytic activities of this multifunctional enzyme have been determined. The results may be tabulated as follows In general, the NAD interacts with the dehydrogenase to promote substrate oxidation and to protect the enzyme against inactivation. At physiological concentrations, ATP inhibits almost every step in the above reactions except the acetylation of the dehydrogenase with p-nitrophenyl acetate. The present findings further characterize the active center of the dehydrogenase. ATP inhibition could contribute to metabolic control and the Pasteur effect in vivo.