Adenylate as a Metabolic Regulator
Year: 1964
Type: article
Abstract: A possible mechanism for the frequently proposed involvement of phosphofructokinase in regulation of the rate of carbohydrate metabolism was suggested by the finding of Lardy and Parks (1) that this enzyme is inhibited by excess adenosine triphosphate. Mansour and Mansour (2) showed phosphofructokinase of the liver fluke to be stimulated by cyclic adenosine 3’,5’-monophosphate. Inhibition of the corresponding enzyme from guinea pig heart by ATP is overcome by 3’, 5’-AMP, 5’-AMP, or ADP (3). Similar properties of phosphofructokinase from skeletal muscle were suggested as a possible explanation of the Pasteur effect (4). Since 3’,5’-AMP seems to be generally associated with hormonal control mechanisms, we investigated the properties of phosphofructokinase from yeast, the classical organism for study of the Pasteur effect and one presumably lacking hormones. The effect of 5’-AMP on the kinetics of yeast DPN-specific isocitrate dehydrogenase (5) had led us to suspect that this nucleotide may play an important role in the control of energy metabolism in yeast. The results presented here suggest that the ratio of the concentrations of AMP and ATP may regulate the activity of phosphofructokinase in yeast.
Source: Journal of Biological Chemistry
Institution: University of California, Los Angeles
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W2135512849