Practical synthesis of 4-hydroxy-3-oxobutylphosphonic acid and its evaluation as a bio-isosteric substrate of DHAP aldolase

Carbohydrate Research

Volumn 305, Issue 3-4, 1997, Pages 313-321

  Arth, Hans Lothar ^a   Fessner, Wolf Dieter ^a  

^a RWTH AACHEN UNIVERSITY   (Germany)

Author keywords

Asymmetric synthesis; D Fructose 1,6 bisphosphate aldolase; Dihydroxyacetone phosphate mimic; Enzyme catalysis; Sugar phosphonates

Indexed keywords

2 BUTANONE; ALDEHYDE; DIHYDROXYACETONE PHOSPHATE; FRUCTOSE BISPHOSPHATE ALDOLASE; PHOSPHONIC ACID DERIVATIVE; SCHIFF BASE; SUGAR PHOSPHATE; ZINC ION;

ARTICLE; CARBOHYDRATE METABOLISM; CARBOHYDRATE SYNTHESIS; CATALYSIS; CHEMICAL REACTION; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; PRIORITY JOURNAL; STEREOSPECIFICITY; X RAY CRYSTALLOGRAPHY;

ALDEHYDES; DIHYDROXYACETONE PHOSPHATE; ENZYME INHIBITORS; FRUCTOSE-BISPHOSPHATE ALDOLASE; GLYCERALDEHYDE 3-PHOSPHATE; HYDROXAMIC ACIDS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; ORGANOPHOSPHORUS COMPOUNDS; PHOSPHONIC ACIDS; STEREOISOMERISM; SUBSTRATE SPECIFICITY; SUGAR PHOSPHATES;

EID: 0031398920     PISSN: 00086215     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6215(97)10026-X     Document Type: Article

References (48)

1. R. Engel, Chem. Rev., 77 (1977) 349-367.
2. R.L. Hilderbrand (Ed.), The Role of Phosphonates in Living Systems, CRC Press, Boca Raton, 1988.
3. R. Engel, The Use of Carbon-Phosphorus Analog Compounds in the Regulation of Biological Processes in R. Engel (Ed.), Handbook of Organophosphorus Chemistry, Dekker, New York, 1992, pp 559-600.
4. F.R. Opperdoes, Ann. Rev. Microbiol., 41 (1987) 127-151.
5. W.-D. Fessner, A Building Block Strategy for Asymmetric Synthesis: The DHAP Aldolases, in S. Servi (Ed.), Microbial Reagents in Organic Synthesis, Kluwer Academic Publishers, Dordrecht, 1992, pp 43-55
6. W.-D. Fessner and C. Walter, Top. Curr. Chem., 184 (1996) 97-194.
7. C.-H. Wong and G.M. Whitesides, Enzymes in Synthetic Organic Chemistry, Pergamon, Oxford, 1994, pp 195-251
8. T. Gefflaut, C. Blonski, J. Perie, and M. Willson, Prog. Biophys. Mol. Biol., 63 (1995) 301-340.
9. J.A. Littlechild and H.C. Watson, Trends Biochem. Sci., 18 (1993) 36-39.
10. W.-D. Fessner, A. Schneider, H. Held, G. Sinerius, C. Walter, M. Hixon, and J.V. Schloss, Angew. Chem. Int. Ed. Engl., 35 (1996) 2219-2221.
11. M.K. Dreyer and G.E. Schulz, J. Mol. Biol., 231 (1993) 549-553.
12. M.K. Dreyer and G.E. Schulz, J. Mol. Biol., 259 (1996) 458-466.
13. M.K. Dreyer and G.E. Schulz, Acta Cryst., D52 (1996) 1082-1091.
14. J. Sygusch, D. Beaudry, and M. Allaire, Proc. Natl. Acad. Sci. USA, 84 (1987) 7846-7850.
15. S.J. Gamblin, G.J. Davies, J.M. Grimes, R.M. Jackson, J.A. Littlechild, and H.C. Watson, J. Mol. Biol., 219 (1991) 573-576.
16. G. Hester, O. Brenner-Holzach, F.A. Rossi, M. Struck-Donatz, K.H. Winterhalter, J.D.G. Smit, and K. Piontek, FEBS Lett., 292 (1991) 237-242.
17. S.J. Cooper, G.A. Leonard, S.M. McSweeney, A.W. Thompson, J.H. Naismith, S. Qamar, A. Plater, A. Berry, and W.N. Hunter, Structure, 4 (1996) 1303.
18. W.-D. Fessner and G. Sinerius, Angew. Chem. Int. Ed. Engl., 33 (1994) 209-212.
19. H.-L. Arth, G. Sinerius, and W.-D. Fessner, Liebigs Ann., (1995) 2037-2042.
20. J. Kabak, L. DeFilippe, R. Engel, and B.E. Tropp, J. Med. Chem., 15 (1972) 1074-1075.
21. S.L. Goldstein, D. Braksmayer, B.E. Tropp, and R. Engel, J. Med. Chem., 17 (1974) 363-364.
22. H.B.F. Dixon and M.J. Sparkes, Biochem. J., 141 (1974) 715-719.
23. H. Paulsen and W. Bartsch, Chem. Ber., 108 (1975) 1745-1755.
24. P. Page, C. Blonski, and J. Périé, Tetrahedron Lett., 36 (1995) 8027-8030.
25. G.F. Hennion and F.P. Kupiecki, J. Org. Chem., 18 (1953) 1601-1609.
26. W. Reppe, Liebigs Ann. Chem., 596 (1955) 44-77.
27. M.E. Jung and M.A. Lyster, J. Org. Chem., 42 (1977) 3761-3764.
28. G.A. Olah, S.C. Narang, B.G.B. Gupta, and R. Malhotra, J. Org. Chem., 44 (1979) 1247-1251.
29. M.E. Jung and M.A. Lyster, J. Am. Chem. Soc., 99 (1977) 968-969.
30. D. Stribling, Biochem. J., 141 (1974) 725-728.
31. P.-J. Cheng, R. Hickey, R. Engel, and B.E. Tropp, Biochim. Biophys. Acta, 341 (1974) 85-92.
32. P.R. Adams, R. Harrison, and T.D. Inch, Biochem. J., 141 (1974) 729-732.
33. N. Bischofberger, H. Waldmann, T. Saito, E.S. Simon, W. Lees, M.D. Bednarski, and G.M. Whitesides, J. Org. Chem., 53 (1988) 3457-3465.
34. M.D. Bednarski, E.S. Simon, N. Bischofberger, W.-D. Fessner, M.-J. Kim, W. Lees, T. Saito, H. Waldmann, and G.M. Whitesides, J. Am. Chem. Soc., 111 (1989) 627-635.
35. H.P. Brockamp and M.R. Kula, Appl. Biochem. Biotechnol., 34 (1990) 287-291.
36. C. Witke and F. Götz, J. Bacteriol., 175 (1993) 7495-7499.
37. C.H. von der Osten, A.J. Sinskey, C.F. Barbas, R.L. Pederson, Y.F. Wang, and C.-H. Wong, J. Am. Chem. Soc., 111 (1989) 3924-3927.
38. W.-D. Fessner, G. Sinerius, A. Schneider, M. Dreyer, G.E. Schulz, J. Badía, and J. Aguilar, Angew. Chem. Int. Ed. Engl., 30 (1991) 555-558.
39. J.P. Richard, J. Am. Chem. Soc., 106 (1984) 4926-4936.
40. J.P. Richard, Biochem. Soc. Trans., 21 (1993) 549-553.
41. D. Schomburg and M. Salzmann (Eds.), Enzyme Handbook, Vol. 1, Springer, Berlin, 1990.
42. W.J. Rutter, Fed. Proc., 23 (1964) 1248-1257.
43. P.D. Spolter, R.C. Adelman, and S. Weinhouse, J. Biol. Chem., 240 (1965) 1327-1331.
44. Z.D. Zhang, S. Sugio, E.A. Komives, K.D. Liu, J.R. Knowles, G.A. Petsko, and D. Ringe, Biochemistry, 33 (1994) 2830-2837.
45. B. Plaut and J.R. Knowles, Biochem. J., 129 (1972) 311-320.
46. J.-M. Lehn, in G. Chiurdoglu (Ed.), Conformational Analysis, Academic Press, New York, 1971, pp 129-155
47. T.S. Papas and R.V. Case, Fed. Proc. Fed. Amer. Soc. Exp. Biol., 29 (1970) 915-918.
48. H.U. Bergmeyer, Methods of Enzymatic Analysis, 3rd edn., Vol. 2, Verlag Chemie, Deerfield, 1984, pp 146-147