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Chemical Compound Review

MgAtp     magnesium[(2R,3S,4R,5R)-5-(6- aminopurin-9...

Synonyms: Magnesium ATP, CHEMBL2364734, LS-15179, AKOS016009253, AC1L257T, ...
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Disease relevance of Adenosine triphosphate

  • The role of calcium and magnesium-ATP on the structure and contractility in motile extracts of Amoeba proteus and plasmalemma-ectoplasm "ghosts" of Chaos carolinensis has been investigated by correlating light and electron microscope observations with turbidity and birefringence measurements [1].
  • Cytosolic free magnesium, ATP and blebbing during chemical hypoxia in cultured rat hepatocytes [2].
  • Use of magnesium-ATP following liver ischemia [3].

High impact information on Adenosine triphosphate

  • The pharmacological characteristics of LmrA and P-glycoprotein-expressing lung fibroblasts were very similar, and the affinities of both proteins for vinblastine and magnesium-ATP were indistinguishable [4].
  • Resealed ghosts, prepared by dialyzing erythrocytes in narrow membrane tubing against low ionic strength buffer that was supplemented with magnesium ATP, were as susceptible to parasite infection as were normal erythrocytes [5].
  • Human erthrocyte membranes in isotonic medium change shape from crenated spheres to biconcave disks and cup-forms when incubated at 37 degrees C in the presence of MgATP (M. P. Sheetz and S. J. Singer, 1977, J. Cell Biol. 73:638-646) [6].
  • In the absence of magnesium, ATP bound to three independent catalytic sites, each with Kd = 76 microM [7].
  • When this was done an analysis of the previously postulated rate law for histone phosphorylation c atalyzed by protein kinase I gave a binding constant for the magnesium-ATP complex which was in agreement with that expected for this complex on the basis of various binding constants available in the literature [8].

Anatomical context of Adenosine triphosphate


Gene context of Adenosine triphosphate


  1. The contractile basis of ameboid movement. II. Structure and contractility of motile extracts and plasmalemma-ectoplasm ghosts. Taylor, D.L., Rhodes, J.A., Hammond, S.A. J. Cell Biol. (1976) [Pubmed]
  2. Cytosolic free magnesium, ATP and blebbing during chemical hypoxia in cultured rat hepatocytes. Harman, A.W., Nieminen, A.L., Lemasters, J.J., Herman, B. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  3. Use of magnesium-ATP following liver ischemia. Chaudry, I.H., Stephan, R.N., Dean, R.E., Clemens, M.G., Baue, A.E. Magnesium. (1988) [Pubmed]
  4. A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene. van Veen, H.W., Callaghan, R., Soceneantu, L., Sardini, A., Konings, W.N., Higgins, C.F. Nature (1998) [Pubmed]
  5. Involvement of spectrin and ATP in infection of resealed erythrocyte ghosts by the human malarial parasite, Plasmodium falciparum. Olson, J.A., Kilejian, A. J. Cell Biol. (1982) [Pubmed]
  6. Spectrin phosphorylation and shape change of human erythrocyte ghosts. Patel, V.P., Fairbanks, G. J. Cell Biol. (1981) [Pubmed]
  7. Cooperativity and stoichiometry of substrate binding to the catalytic sites of Escherichia coli F1-ATPase. Effects of magnesium, inhibitors, and mutation. Weber, J., Wilke-Mounts, S., Senior, A.E. J. Biol. Chem. (1994) [Pubmed]
  8. Ionic inhibition of catalytic phosphorylation of histone by bovine brain protein kinase. Moll, G.W., Kaiser, E.T. J. Biol. Chem. (1977) [Pubmed]
  9. Effect of intra-erythrocytic magnesium ions on invasion by Plasmodium falciparum. Field, S.J., Rangachari, K., Dluzewski, A.R., Wilson, R.J., Gratzer, W.B. Parasitology (1992) [Pubmed]
  10. Haemodynamics and myocardial metabolism of phosphorus depleted dogs: effects of catecholamines and angiotensin II. Kreusser, W., Vetter, H.O., Mittmann, U., Hörl, W.H., Ritz, E. Eur. J. Clin. Invest. (1982) [Pubmed]
  11. Regulation of release from isolated adrenergic secretory vesicles by ATP-mediated changes in transmembrane potential and anion permeability. Pollard, H.B., Pazoles, C.J., Hoffman, P.G., Zinder, O., Nikodijevik, O. Prog. Clin. Biol. Res. (1977) [Pubmed]
  12. The DNA-dependent protein kinase interacts with DNA to form a protein-DNA complex that is disrupted by phosphorylation. Merkle, D., Douglas, P., Moorhead, G.B., Leonenko, Z., Yu, Y., Cramb, D., Bazett-Jones, D.P., Lees-Miller, S.P. Biochemistry (2002) [Pubmed]
  13. Role of the divalent cation in topoisomerase II mediated reactions. Osheroff, N. Biochemistry (1987) [Pubmed]
  14. Regulation of binding of myosin subfragments with regulated actin by calcium ions in the presence of magnesium ATP. Inoue, A., Tonomura, Y. J. Biochem. (1982) [Pubmed]
  15. Inhibition of axoneme and dynein ATPase from sea urchin sperm by free ATP. Hayashi, M. Biochim. Biophys. Acta (1976) [Pubmed]
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