Abstract
Phosphoenolpyruvate carboxykinase from rat liver cytosol is activated by Fe2+ ions in either direction of catalysis. Preincubation of the purified enzyme with Fe2+ ions causes a time-dependent irreversible loss of activity; this is not seen with unpurified enzyme. Purified enzyme can be protected from inactivation by Fe2+ ions by partially purified protein fractions from liver (ferroactivator fractions). The possible role of ferroactivator and Fe2+ ions in regulating phosphoenolpyruvate carboxykinase is discussed.
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Selected References
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- Ballard F. J., Hanson R. W. Phosphoenolpyruvate carboxykinase and pyruvate carboxylase in developing rat liver. Biochem J. 1967 Sep;104(3):866–871. doi: 10.1042/bj1040866. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ballard F. J., Hanson R. W. Purification of phosphoenolpyruvate carboxykinase from the cytosol fraction of rat liver and the immunochemical demonstration of differences between this enzyme and the mitochondrial phosphoenolpyruvate carboxykinase. J Biol Chem. 1969 Oct 25;244(20):5625–5630. [PubMed] [Google Scholar]
- Bentle L. A., Lardy H. A. Interaction of anions and divalent metal ions with phosphoenolpyruvate carboxykinase. J Biol Chem. 1976 May 25;251(10):2916–2921. [PubMed] [Google Scholar]
- Bentle L. A., Lardy H. A. P-enolpyruvate carboxykinase ferroactivator. Purification and some properties. J Biol Chem. 1977 Feb 25;252(4):1431–1440. [PubMed] [Google Scholar]
- Bentle L. A., Snoke R. E., Lardy H. A. A protein factor required for activation of phosphoenolpyruvate carboxykinase by ferrous ions. J Biol Chem. 1976 May 25;251(10):2922–2928. [PubMed] [Google Scholar]
- Colombo G., Carlson G. M., Lardy H. A. Phosphoenolpyruvate carboxykinase (guanosine triphosphate) from rat liver cytosol. Separation of homogeneous forms of the enzyme with high and low activity by chromatography on agarose-hexane-guanosine triphosphate. Biochemistry. 1978 Dec 12;17(25):5321–5329. doi: 10.1021/bi00618a001. [DOI] [PubMed] [Google Scholar]
- Hammond K. D., Balinsky D. Kinetic studies on phosphoenolpyruvate carboxykinase purified from the mitochondrial and cytosol fractions of monkey liver. Int J Biochem. 1978;9(3):199–211. doi: 10.1016/0020-711x(78)90150-7. [DOI] [PubMed] [Google Scholar]
- MacDonald M. J., Bentle L. A., Lardy H. A. P-enolpyruvate carboxykinase ferroactivator. Distribution, and the influence of diabetes and starvation. J Biol Chem. 1978 Jan 10;253(1):116–124. [PubMed] [Google Scholar]
- MacDonald M. J., Lardy H. A. 3-Aminopicolinate: a synthetic metal-complexing activator of phosphoenolpyruvate carboxykinase. J Biol Chem. 1978 Apr 10;253(7):2300–2307. [PubMed] [Google Scholar]
- Philippidis H., Hanson R. W., Reshef L., Hopgood M. F., Ballard F. J. The initial synthesis of proteins during development. Phosphoenolpyruvate carboxylase in rat liver at birth. Biochem J. 1972 Mar;126(5):1127–1134. doi: 10.1042/bj1261127. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pogson C. I., Smith S. A. The activity of phosphoenolpyruvate carboxykinase in rat tissues. Assay techniques and effects of dietary and hormonal changes. Biochem J. 1975 Nov;152(2):401–408. doi: 10.1042/bj1520401. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Snoke R. E., Johnston J. B., Lardy H. A. Response of phosphopyruvate carboxylase to tryptophan metabolites and metal ions. Eur J Biochem. 1971 Dec;24(2):342–346. doi: 10.1111/j.1432-1033.1971.tb19692.x. [DOI] [PubMed] [Google Scholar]