Abstract
Pyruvate kinase (EC 2.7.1.40) from Azotobacter vinelandii responds sharply to the adenylate energy charge, with a decrease in activity at high values of charge, as expected for an enzyme of an adenosine triphosphate-regenerating sequence. Glycolytic intermediates, especially glucose 6-phosphate, fructose 6-phosphate, and fructose-1,6-diphosphate, strongly stimulate the reaction and overcome the inhibition caused by high values of energy charge. Thus, the properties of this enzyme depend on interaction between energy charge and the concentrations of hexose phosphates. The properties of pyruvate kinase, together with those of phosphoenolpyruvate carboxylase, aspartokinase, and citrate synthase, seem adapted to provide appropriate partitioning of phosphoenolpyruvate between competing pathways in response to metabolic need.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Atkinson D. E. Citrate and the citrate cycle in the regulation of energy metabolism. Biochem Soc Symp. 1968;27:23–40. [PubMed] [Google Scholar]
- Atkinson D. E. Regulation of enzyme function. Annu Rev Microbiol. 1969;23:47–68. doi: 10.1146/annurev.mi.23.100169.000403. [DOI] [PubMed] [Google Scholar]
- Atkinson D. E. The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers. Biochemistry. 1968 Nov;7(11):4030–4034. doi: 10.1021/bi00851a033. [DOI] [PubMed] [Google Scholar]
- Atkinson D. E., Walton G. M. Adenosine triphosphate conservation in metabolic regulation. Rat liver citrate cleavage enzyme. J Biol Chem. 1967 Jul 10;242(13):3239–3241. [PubMed] [Google Scholar]
- Cánovas J. L., Kornberg H. L. Properties and regulation of phosphopyruvate carboxylase activity in Escherichia coli. Proc R Soc Lond B Biol Sci. 1966 Aug 16;165(999):189–205. doi: 10.1098/rspb.1966.0064. [DOI] [PubMed] [Google Scholar]
- DAVIDSON E. A. Specificity of pyruvate kinase. Biochim Biophys Acta. 1959 May;33(1):238–240. doi: 10.1016/0006-3002(59)90520-7. [DOI] [PubMed] [Google Scholar]
- Hess B., Haeckel R., Brand K. FDP-activation of yeast pyruvate kinase. Biochem Biophys Res Commun. 1966 Sep 22;24(6):824–831. doi: 10.1016/0006-291x(66)90322-6. [DOI] [PubMed] [Google Scholar]
- KREBS H. A., SPEAKE R. N., HEMS R. ACCELERATION OF RENAL GLUCONEOGENESIS BY KETONE BODIES AND FATTY ACIDS. Biochem J. 1965 Mar;94:712–720. doi: 10.1042/bj0940712. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Klungsoyr L., Hagemen J. H., Fall L., Atkinson D. E. Interaction between energy charge and product feedback in the regulation of biosynthetic enzymes. Aspartokinase, phosphoribosyladenosine triphosphate synthetase, and phosphoribosyl pyrophosphate synthetase. Biochemistry. 1968 Nov;7(11):4035–4040. doi: 10.1021/bi00851a034. [DOI] [PubMed] [Google Scholar]
- Li Y. T., Li S. C. Studies on the glycosidases in jack bean meal. II. Sepation of various glycosidases by isoelectric focusing. J Biol Chem. 1968 Jul 25;243(14):3994–3996. [PubMed] [Google Scholar]
- Liao C. L., Atkinson D. E. Regulation at the phosphoenolpyruvate branchpoint in Azotobacter vinelandii: phosphoenolpyruvate carboxylase. J Bacteriol. 1971 Apr;106(1):31–36. doi: 10.1128/jb.106.1.31-36.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Maeba P., Sanwal B. D. The regulation of pyruvate kinase of Escherichia coli by fructose diphosphate and adenylic acid. J Biol Chem. 1968 Jan 25;243(2):448–450. [PubMed] [Google Scholar]
- Ozaki H., Shiio I. Regulation of the TCA and glyoxylate cycles in Brevibacterium flavum. II. Regulation of phosphoenolpyruvate carboxylase and pyruvate kinase. J Biochem. 1969 Sep;66(3):297–311. doi: 10.1093/oxfordjournals.jbchem.a129148. [DOI] [PubMed] [Google Scholar]
- Utter M. F., Keech D. B., Scrutton M. C. A possible role for acetyl CoA in the control of gluconeogenesis. Adv Enzyme Regul. 1964;2:49–68. doi: 10.1016/s0065-2571(64)80005-4. [DOI] [PubMed] [Google Scholar]