Humphrey, S. J., James, D. E. & Mann, M. Protein phosphorylation: a major switch mechanism for metabolic regulation. Trends Endocrinol. Metab. 26, 676–687 (2015).
Marín-Hernández, Á., Rodríguez-Zavala, J. S., Jasso-Chávez, R., Saavedra, E. & Moreno-Sánchez, R. Protein acetylation effects on enzyme activity and metabolic pathway fluxes. J. Cell. Biochem. 123, 701–718 (2022).
Sabari, B. R., Zhang, D., Allis, C. D. & Zhao, Y. Metabolic regulation of gene expression through histone acylations. Nat. Rev. Mol. Cell Biol. 18, 90–101 (2017).
Wu, Q., Schapira, M., Arrowsmith, C. H. & Barsyte-Lovejoy, D. Protein arginine methylation: from enigmatic functions to therapeutic targeting. Nat. Rev. Drug. Discov. 20, 509–530 (2021).
Murn, J. & Shi, Y. The winding path of protein methylation research: milestones and new frontiers. Nat. Rev. Mol. Cell Biol. 18, 517–527 (2017).
Husted, A. S., Trauelsen, M., Rudenko, O., Hjorth, S. A. & Schwartz, T. W. GPCR-mediated signaling of metabolites. Cell Metab. 25, 777–796 (2017).
Krebs, H. A. The history of the tricarboxylic acid cycle. Perspect. Biol. Med. 14, 154–172 (1970).
Barnett, J. A. A history of research on yeasts 5: the fermentation pathway. Yeast 20, 509–543 (2003).
Houten, S. M. & Wanders, R. J. A. A general introduction to the biochemistry of mitochondrial fatty acid β-oxidation. J. Inherit. Metab. Dis. 33, 469–477 (2010).
Lowry, O. H. & Passonneau, J. V. Kinetic evidence for multiple binding sites on phosphofructokinase. J. Biol. Chem. 241, 2268–2279 (1966).
Kemp, R. G. & Foe, L. G. Allosteric regulatory properties of muscle phosphofructokinase. Mol. Cell. Biochem. 57, 147–154 (1983).
Hue, L. & Taegtmeyer, H. The Randle cycle revisited: a new head for an old hat. Am. J. Physiol. Endocrinol. Metab. 297, E578–E591 (2009).
Icard, P. et al. Why may citrate sodium significantly increase the effectiveness of transarterial chemoembolization in hepatocellular carcinoma? Drug. Resist. Updat. 59, 100790 (2021).
Van Schaftingen, E., Hue, L. & Hers, H. G. Fructose 2,6-bisphosphate, the probably structure of the glucose- and glucagon-sensitive stimulator of phosphofructokinase. Biochem. J. 192, 897–901 (1980).
Hers, H. G. & Van Schaftingen, E. Fructose 2,6-bisphosphate 2 years after its discovery. Biochem. J. 206, 1–12 (1982). An insightful history of the discovery and characterization of F2,6BP. It includes reproductions of plots from early experiments.
Uyeda, K., Furuya, E. & Luby, L. The effect of natural and synthetic d-fructose 2,6-bisphosphate on the regulatory kinetic properties of liver and muscle phosphofructokinases. J. Biol. Chem. 256, 8394–8399 (1981).
Hers, H. G. & Van Schaftingen, E. Fructose 2,6-bisphosphate 2 years after its discovery. Biochem. J. 206, 1–12 (1982).
Christophe, J. Glucagon receptors: from genetic structure and expression to effector coupling and biological responses. Biochim. Biophys. Acta 1241, 45–57 (1995).
el-Maghrabi, M. R., Claus, T. H., Pilkis, J. & Pilkis, S. J. Regulation of 6-phosphofructo-2-kinase activity by cyclic AMP-dependent phosphorylation. Proc. Natl Acad. Sci. USA 79, 315–319 (1982).
Pilkis, S. J., El-Maghrabi, M. R. & Claus, T. H. Fructose-2,6-bisphosphate in control of hepatic gluconeogenesis: from metabolites to molecular genetics. Diabetes Care 13, 582–599 (1990).
Muller, A., Unthan-Fechner, K. & Probst, I. Activation of phosphofructokinase 2 by insulin in cultured hepatocytes without accompanying changes of effector levels or cAMP-stimulated protein kinase activity ratios. Eur. J. Biochem. 176, 415–420 (1988).
Nishimura, M. & Uyeda, K. Purification and characterization of a novel xylulose 5-phosphate-activated protein phosphatase catalyzing dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. J. Biol. Chem. 270, 26341–26346 (1995).
Morimoto, Y. et al. Insulin pretreatment protects the liver from ischemic damage during Pringle’s maneuver. Surgery 120, 808–815 (1996).
Mokrasch, L. C. & McGilvery, R. W. Purification and properties of fructose-1,6-diphosphatase. J. Biol. Chem. 221, 909–917 (1956).
Van Schaftingen, E. & Hers, H. G. Inhibition of fructose-1,6-bisphosphatase by fructose 2,6-biphosphate. Proc. Natl Acad. Sci. USA 78, 2861–2863 (1981).
Bricker Daniel, K. et al. A mitochondrial pyruvate carrier required for pyruvate uptake in yeast, Drosophila, and humans. Science 337, 96–100 (2012).
Jagannathan, V. & Schweet, R. Pyruvic oxidase of pigeon breast muscle. I. Purification and properties of the enzyme. J. Biol. Chem. 196, 551–562 (1952).
Gudi, R., Melissa, M. B.-K., Kedishvili, N. Y., Zhao, Y. & Popov, K. M. Diversity of the pyruvate dehydrogenase kinase gene family in humans. J. Biol. Chem. 270, 28989–28994 (1995).
Kerbey, A. L. et al. Regulation of pyruvate dehydrogenase in rat heart. Mechanism of regulation of proportions of dephosphorylated and phosphorylated enzyme by oxidation of fatty acids and ketone bodies and of effects of diabetes: role of coenzyme A, acetyl-coenzyme A and reduced and oxidized nicotinamide-adenine dinucleotide. Biochem. J. 154, 327–348 (1976).
Bowker-Kinley, M. M., Davis, I. W., Wu, P., Harris, A. R. & Popov, M. K. Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex. Biochem. J. 329, 191–196 (1998).
Sharma, P., Walsh, K. T., Kerr-Knott, K. A., Karaian, J. E. & Mongan, P. D. Pyruvate modulates hepatic mitochondrial functions and reduces apoptosis indicators during hemorrhagic shock in rats. Anesthesiology 103, 65–73 (2005).
Woods, M. & Burk, D. Inhibition of tumor cell glycolysis by DPNH2, and reversal of the inhibition by DPN, pyruvate or methylene blue. Z. f.ür. Naturforsch. B 18, 731–748 (1963).
Huckabee, W. E. Relationships of pyruvate and lactate during anaerobic metabolism. I. Effects of infusion of pyruvate or glucose and of hyperventilation. J. Clin. Invest. 37, 244–254 (1958).
Baumberger, J. P., Jürgensen, J. J. & Bardwell, K. The coupled redox potential of the lactate–enzyme–pyruvate system. J. Gen. Physiol. 16, 961–976 (1933).
O’Carra, P. & Mulcahy, P. Tissue distribution of mammalian lactate dehydrogenase isoenzymes. Biochem. Soc. Trans. 18, 272–274 (1990).
Wang, C.-S. Inhibition of human erythrocyte lactate dehydrogenase by high concentrations of pyruvate. Eur. J. Biochem. 78, 569–574 (1977). Experiments demonstrating the inhibition of high levels of pyruvate on human LDHA. The mechanism involves competition with NADH for binding within the active site.
Rao, Y. et al. Excess exogenous pyruvate inhibits lactate dehydrogenase activity in live cells in an MCT1-dependent manner. J. Biol. Chem. 297, (2021).
DeBerardinis Ralph, J. et al. Beyond aerobic glycolysis: transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis. Proc. Natl Acad. Sci. USA 104, 19345–19350 (2007).
Cohen, P. F. & Colman, R. F. Diphosphopyridine nucleotide dependent isocitrate dehydrogenase from pig heart. Characterization of active substrate and modes of regulation. Biochemistry 11, 1501–1508 (1972).
Gabriel, J. L. & Plaut, G. W. E. Inhibition of bovine heart NAD-specific isocitrate dehydrogenase by reduced pyridine nucleotides: modulation of inhibition by ADP, NAD+, calcium2+, citrate, and isocitrate. Biochemistry 23, 2773–2778 (1984).
Chen, R. F. & Plaut, G. W. E. Activation and inhibition of DPN-linked isocitrate dehydrogenase of heart by certain nucleotides. Biochemistry 2, 1023–1032 (1963).
Roche, T. E. & Lawlis, V. B. Structure and regulation of α-ketoglutarate dehydrogenase of bovine kidney. Ann. N. Y. Acad. Sci. 378, 236–249 (1982).
Smith, C., Bryla, J. & Williamson, J. Regulation of mitochondrial α-ketoglutarate metabolism by product inhibition at α-ketoglutarate dehydrogenase. J. Biol. Chem. 249, 1497–1505 (1974).
Fang, J. et al. Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem. J. 363, 81–87 (2002).
Smith, T. J., Peterson, P. E., Schmidt, T., Fang, J. & Stanley, C. A. Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. J. Mol. Biol. 307, 707–720 (2001).
留言 (0)