The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

CHEBI:13711     (hydroxy-oxido-phosphoryl) ethanoate

Synonyms: AC1O7462, acetyl hydrogen phosphate
This record was replaced with 186.
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of acetyloxyphosphonic acid


High impact information on acetyloxyphosphonic acid

  • Cyclopiazonic acid also inhibited the Ca2+-dependent acetylphosphate, p-nitrophenylphosphate and carbamylphosphate hydrolysis by sarcoplasmic reticulum [4].
  • This mechanism includes a phosphoenzyme intermediate and requires enzyme-bount MgADP for phosphorylation of the enzyme by acetylphosphate [5].
  • The activation of PhoB by acetylphosphate [6].
  • During 30 min of anaerobic dark or light incubation with sodium pyrivate, crude extracts from fermentatively grown cells produced about 6 micronmol of acetylphosphate and formate per mg of protein in reactions performed at pH 8 [7].
  • Although these comparative analyses revealed several common differences, thus suggesting possible interactions between these regulatory mechanisms, i.e. H-NS, Lrp (leucine-responsive regulatory protein) and acetylphosphate, the most extensive modifications occurred in an hns mutant [8].

Chemical compound and disease context of acetyloxyphosphonic acid

  • Cell-free extracts of Clostridium sporogenes catalyse the water elimination from (2R)-phenyllactate in the presence of one of the energy-rich compounds acetyl-CoA, acetylphosphate or ATP and coenzyme A. Water is eliminated from (2R)-phenyllactoyl-CoA without any of the aforementioned additions [9].

Biological context of acetyloxyphosphonic acid

  • This effect, which is attributed to occupancy of the phosphorylation domain of the catalytic site, is distinct from the known secondary activation of enzyme turnover which is produced by ATP and by inactive nucleotide analogs, but not by acetylphosphate [10].
  • The linkage in the active site of the phosphorylated intermediate of (Na+,K+)-ATPase appeared to be equivalent to the non-hydrated state of the model compound acetylphosphate [11].

Anatomical context of acetyloxyphosphonic acid


Associations of acetyloxyphosphonic acid with other chemical compounds


Analytical, diagnostic and therapeutic context of acetyloxyphosphonic acid


  1. Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. Muller, Y.A., Schulz, G.E. Science (1993) [Pubmed]
  2. Purification of five components from Clostridium thermoaceticum which catalyze synthesis of acetate from pyruvate and methyltetrahydrofolate. Properties of phosphotransacetylase. Drake, H.L., Hu, S.I., Wood, H.G. J. Biol. Chem. (1981) [Pubmed]
  3. Binding sites of VanRB and sigma70 RNA polymerase in the vanB vancomycin resistance operon of Enterococcus faecium BM4524. Depardieu, F., Courvalin, P., Kolb, A. Mol. Microbiol. (2005) [Pubmed]
  4. Cyclopiazonic acid is a specific inhibitor of the Ca2+-ATPase of sarcoplasmic reticulum. Seidler, N.W., Jona, I., Vegh, M., Martonosi, A. J. Biol. Chem. (1989) [Pubmed]
  5. Escherichia coli acetate kinase mechanism studied by net initial rate, equilibrium, and independent isotopic exchange kinetics. Skarstedt, M.T., Silverstein, E. J. Biol. Chem. (1976) [Pubmed]
  6. The activation of PhoB by acetylphosphate. McCleary, W.R. Mol. Microbiol. (1996) [Pubmed]
  7. Fermentative metabolism of pyruvate by Rhodospirillum rubrum after anaerobic growth in darkness. Gorrell, T.E., Uffen, R.L. J. Bacteriol. (1977) [Pubmed]
  8. Role of Escherichia coli histone-like nucleoid-structuring protein in bacterial metabolism and stress response--identification of targets by two-dimensional electrophoresis. Laurent-Winter, C., Ngo, S., Danchin, A., Bertin, P. Eur. J. Biochem. (1997) [Pubmed]
  9. Observations on the elimination of water from 2-hydroxy acids in the metabolism of amino acids by Clostridium sporogenes. Machacek-Pitsch, C., Rauschenbach, P., Simon, H. Biol. Chem. Hoppe-Seyler (1985) [Pubmed]
  10. Accelerating effect of ATP on calcium binding to sarcoplasmic reticulum ATPase. Fernandez-Belda, F., Garcia-Carmona, F., Inesi, G. Arch. Biochem. Biophys. (1988) [Pubmed]
  11. Non-hydrated state of the acyl phosphate group in the phosphorylated intermediate of (Na+,K+)-ATPase. Ushimaru, M., Shinohara, Y., Fukushima, Y. J. Biochem. (1997) [Pubmed]
  12. Glutathione specifically labeled with isotopes. Murata, K., Abbott, W.A., Bridges, R.J., Meister, A. Anal. Biochem. (1985) [Pubmed]
  13. Lactate and acetate production in Listeria innocua. Kelly, A.F., Patchett, R.A. Lett. Appl. Microbiol. (1996) [Pubmed]
  14. Conditions of occurrence for primeval processes of transphosphorylations. Etzix, E., Buvet, R. Orig. Life (1975) [Pubmed]
WikiGenes - Universities