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Chemical Compound Review

AG-K-07542     2-oxoethylphosphonic acid

Synonyms: CHEBI:18124, KST-1A1869, CTK4D0468, AR-1A2560, DB03174, ...
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Disease relevance of acetylphosphonate


High impact information on acetylphosphonate

  • X-ray structure determination of the D12A mutant in the presence of the substrate phosphonoacetaldehyde showed that replacement of the loop 1 Asp, common to all HAD family members, with Ala shifts the position of Mg(II), thereby allowing innersphere coordination to Asp190 and causing a shift in the position of the substrate [3].
  • The active site contains a cofactor, pyridoxal 5'-phosphate (PLP), and the product phosphonoacetaldehyde [4].
  • The ability of the phosphonatase competitive inhibitor (Ki = 230 +/- 20 microM) acetonylphosphonate to protect the enzyme from phosphonoacetaldehyde/NaBH4-induced inactivation suggested that the reactive lysine residue is located in the enzyme active site [5].
  • The inhibition by phosphonates and phosphate analogues of the alkaline phosphatase activity of rat intestinal brush-border membrane vesicles was studied at pH 7.5 and 30 degrees C. Phenylene-1,3-diphosphonate, 2,6-dinitrophenylphosphonate and phosphonoacetaldehyde were found to be competitive inhibitors, with Ki values in the range 16-80 microM [6].
  • The phnX gene encoding the phosphonoacetaldehyde hydrolase (phosphonatase) from the Gram-negative bacterium Pseudomonas aeruginosa A237 has been cloned and its sequence determined [2].

Chemical compound and disease context of acetylphosphonate


Biological context of acetylphosphonate


Associations of acetylphosphonate with other chemical compounds

  • The reaction proceeds via a novel bicovalent catalytic mechanism in which an active-site nucleophile abstracts the phosphoryl group from the Schiff-base intermediate formed from Lys53 and phosphonoacetaldehyde [8].
  • Phosphonatase functions in the 2-aminoethylphosphonate (AEP) degradation pathway of bacteria, catalyzing the hydrolysis of the CP bond in phosphonoacetaldehyde (Pald) via formation of a bi-covalent Lys53ethylenamine/Asp12 aspartylphosphate intermediate [9].
  • The X-ray crystallographic structure of wild-type phosphonatase reduced with NaBH(4) in the presence of Pald was determined at 2.4A resolution to reveal Nepsilon-ethyl-Lys53 juxtaposed with a sulfate ligand bound in the phosphate site [9].

Gene context of acetylphosphonate

  • Kinetic studies with substrate analogs and group-directed chemical modification agents were carried out for the purpose of identifying the enzyme-substrate interactions required for phosphonoacetaldehyde (P-Ald) binding and catalyzed hydrolysis by P-Ald hydrolase (phosphonatase) [10].


  1. Kinetic evidence for a substrate-induced fit in phosphonoacetaldehyde hydrolase catalysis. Zhang, G., Mazurkie, A.S., Dunaway-Mariano, D., Allen, K.N. Biochemistry (2002) [Pubmed]
  2. First characterization of the phosphonoacetaldehyde hydrolase gene of Pseudomonas aeruginosa. Dumora, C., Marche, M., Doignon, F., Aigle, M., Cassaigne, A., Crouzet, M. Gene (1997) [Pubmed]
  3. Investigation of metal ion binding in phosphonoacetaldehyde hydrolase identifies sequence markers for metal-activated enzymes of the HAD enzyme superfamily. Zhang, G., Morais, M.C., Dai, J., Zhang, W., Dunaway-Mariano, D., Allen, K.N. Biochemistry (2004) [Pubmed]
  4. Degradation pathway of the phosphonate ciliatine: crystal structure of 2-aminoethylphosphonate transaminase. Chen, C.C., Zhang, H., Kim, A.D., Howard, A., Sheldrick, G.M., Mariano-Dunaway, D., Herzberg, O. Biochemistry (2002) [Pubmed]
  5. Investigation of the Bacillus cereus phosphonoacetaldehyde hydrolase. Evidence for a Schiff base mechanism and sequence analysis of an active-site peptide containing the catalytic lysine residue. Olsen, D.B., Hepburn, T.W., Moos, M., Mariano, P.S., Dunaway-Mariano, D. Biochemistry (1988) [Pubmed]
  6. Potent inhibition of membrane-bound rat intestinal alkaline phosphatase by a new series of phosphate analogues. Shirazi, S.P., Beechey, R.B., Butterworth, P.J. Biochem. J. (1981) [Pubmed]
  7. Phosphonate analogues of pyruvate. Probes of substrate binding to pyruvate oxidase and other thiamin pyrophosphate-dependent decarboxylases. O'Brien, T.A., Kluger, R., Pike, D.C., Gennis, R.B. Biochim. Biophys. Acta (1980) [Pubmed]
  8. The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. Morais, M.C., Zhang, W., Baker, A.S., Zhang, G., Dunaway-Mariano, D., Allen, K.N. Biochemistry (2000) [Pubmed]
  9. Diversification of function in the haloacid dehalogenase enzyme superfamily: The role of the cap domain in hydrolytic phosphoruscarbon bond cleavage. Lahiri, S.D., Zhang, G., Dunaway-Mariano, D., Allen, K.N. Bioorg. Chem. (2006) [Pubmed]
  10. Investigation of the substrate binding and catalytic groups of the P-C bond cleaving enzyme, phosphonoacetaldehyde hydrolase. Olsen, D.B., Hepburn, T.W., Lee, S.L., Martin, B.M., Mariano, P.S., Dunaway-Mariano, D. Arch. Biochem. Biophys. (1992) [Pubmed]
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