Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1974 Sep;141(3):715–719. doi: 10.1042/bj1410715

Phosphonomethyl analogues of phosphate ester glycolytic intermediates

Henry B F Dixon 1, Michael J Sparkes 1
PMCID: PMC1168176  PMID: 4377103

Abstract

Analogues of dihydroxyacetone phosphate and of 3-phosphoglycerate were made in which the phosphate group, –O–PO3H2, is replaced by the phosphonomethyl group, –CH2–PO3H2. The analogue of dihydroxyacetone phosphate is a substrate for aldolase and glycerol 1-phosphate dehydrogenase (Stribling, 1974), but not for triose phosphate isomerase. The analogue of 3-phosphoglycerate oxidizes NADH under the combined action of 3-phosphoglycerate kinase and glyceraldehyde 3-phosphate dehydrogenase if ATP is added. Thus four out of the five glycolytic enzymes tested handle the phosphonomethyl compounds like the natural phosphates.

Full text

PDF
715

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adams P. R., Harrison R. Dehydration of a phosphonate substrate analogue by glycerol 3-phosphate dehydrogenase. Biochem J. 1974 Sep;141(3):729–732. doi: 10.1042/bj1410729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cheng P. J., Hickey R., Engel R., Tropp B. E. Rabbit muscle L-glycerol-3-phosphate dehydrogenase. Substrate activity of 3,4-dihydroxybutyl 1-phosphonate and 4-hydroxy-3-oxobutyl 1-phosphonate. Biochim Biophys Acta. 1974 Mar 21;341(1):85–92. doi: 10.1016/0005-2744(74)90068-0. [DOI] [PubMed] [Google Scholar]
  3. De la Mare S., Coulson A. F., Knowles J. R., Priddle J. D., Offord R. E. Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine. Biochem J. 1972 Sep;129(2):321–331. doi: 10.1042/bj1290321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dixon H. B. A reaction of glucose with peptides. Biochem J. 1972 Aug;129(1):203–208. doi: 10.1042/bj1290203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dixon H. B., Gibbs K., Walshe J. M. Preparation of triethylenetetramine dihydrochloride for the treatment of Wilson's disease. Lancet. 1972 Apr 15;1(7755):853–853. doi: 10.1016/s0140-6736(72)90845-8. [DOI] [PubMed] [Google Scholar]
  6. Dixon H. B. Transamination of peptides. Biochem J. 1964 Sep;92(3):661–666. doi: 10.1042/bj0920661. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Goldstein S. L., Braksmayer D., Tropp B. E., Engel R. Isosteres of natural phosphates. 2. Synthesis of the monosodium salt of 4-hydroxy-3-oxobutyl-1-phosphonic acid, an isostere of dihydroxyacetone phosphate. J Med Chem. 1974 Mar;17(3):363–364. doi: 10.1021/jm00249a026. [DOI] [PubMed] [Google Scholar]
  8. HARTING J., VELICK S. F. Acetyl phosphate formation catalyzed by glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem. 1954 Apr;207(2):857–865. [PubMed] [Google Scholar]
  9. Kabak J., DeFilippe L., Engel R., Tropp B. Synthesis of the phosphonic acid isostere of glycerol 3-phosphate. J Med Chem. 1972 Oct;15(10):1074–1075. doi: 10.1021/jm00280a022. [DOI] [PubMed] [Google Scholar]
  10. Nowak T., Mildvan A. S., Kenyon G. L. Nuclear relaxation and kinetic studies of the role of Mn 2+ in the mechanism of enolase. Biochemistry. 1973 Apr 24;12(9):1690–1701. doi: 10.1021/bi00733a005. [DOI] [PubMed] [Google Scholar]
  11. Orr G. A., Knowles J. R. The interaction of the phosphonate analogue of 3-phospho-D-glycerate with phosphoglycerate kinase. Biochem J. 1974 Sep;141(3):721–723. doi: 10.1042/bj1410721. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pfeiffer F. R., Mier J. D., Weisbach J. A. Synthesis of phosphonic acid isosteres of 2-phospho-, 3-phospho-, and 2,3-diphosphoglyceric acid. J Med Chem. 1974 Jan;17(1):112–115. doi: 10.1021/jm00247a020. [DOI] [PubMed] [Google Scholar]
  13. Plaut B., Knowles J. R. pH-dependence of the triose phosphate isomerase reaction. Biochem J. 1972 Sep;129(2):311–320. doi: 10.1042/bj1290311. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Richards F. M., Wyckoff H. W., Carlson W. D., Allewell N. M., Lee B., Mitsui Y. Protein structure, ribonuclease-S and nucleotide interactions. Cold Spring Harb Symp Quant Biol. 1972;36:35–43. doi: 10.1101/sqb.1972.036.01.008. [DOI] [PubMed] [Google Scholar]
  15. Rose I. A., O'Connell E. L. Studies on the interaction of aldolase with substrate analogues. J Biol Chem. 1969 Jan 10;244(1):126–134. [PubMed] [Google Scholar]
  16. Shopsis C. S., Engel R., Tropp B. E. Effects of phosphonic acid analogues of glycerol-3-phosphate on the growth of Escherichia coli. J Bacteriol. 1972 Oct;112(1):408–412. doi: 10.1128/jb.112.1.408-412.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Stribling D. Properties of the phosphonomethyl isosteres of two phosphate ester glycolytic intermediates. Biochem J. 1974 Sep;141(3):725–728. doi: 10.1042/bj1410725. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Stubbe J. A., Kenyon G. L. Analogs of phosphoenolpyruvate. Substrate specificities of enolase and pyruvate kinase from rabbit muscle. Biochemistry. 1972 Feb 1;11(3):338–345. doi: 10.1021/bi00753a005. [DOI] [PubMed] [Google Scholar]
  19. WADE H. E., MORGAN D. M. Detection of phosphate esters on paper chromatograms. Nature. 1953 Mar 21;171(4351):529–530. doi: 10.1038/171529a0. [DOI] [PubMed] [Google Scholar]
  20. Waley S. G. Refolding of triose phosphate isomerase. Biochem J. 1973 Sep;135(1):165–172. doi: 10.1042/bj1350165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Wolfenden R. Binding of substrate and transition state analog to trisephosphate isomerase. Biochemistry. 1970 Aug 18;9(17):3404–3407. doi: 10.1021/bi00819a018. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES