Synthesis and evaluation of C-9 modified N-acetylneuraminic acid derivatives as substrates for N-acetylneuraminic acid aldolase

Bioorganic and Medicinal Chemistry

Volumn 8, Issue 3, 2000, Pages 657-664

  Kiefel, Milton J ^a,b   Wilson, Jennifer C ^c   Bennett, Simon ^c   Gredley, Matt ^c   Von Itzstein, Mark ^c  

^a MONASH UNIVERSITY   (Australia)

^b Grith University (Gold Coast Campus)   (Australia)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE; N ACETYLNEURAMINATE LYASE; N ACETYLNEURAMINIC ACID; N ACETYLNEURAMINIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME INHIBITION; ENZYME SUBSTRATE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PROTON NUCLEAR MAGNETIC RESONANCE; SYNTHESIS;

BACTERIAL PROTEINS; BINDING SITES; ESCHERICHIA COLI; KINETICS; MEMBRANES, ARTIFICIAL; MOLECULAR PROBES; N-ACETYLNEURAMINIC ACID; OXO-ACID-LYASES; SUBSTRATE SPECIFICITY;

EID: 0033996959     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0896(99)00325-9     Document Type: Article

References (37)

1. Corfield, A. P.; Schauer, R. In Sialic Acids: Chemistry, Metabolism and Function in Cell Biology Monographs; Schauer, R., Ed.; Springer-Verlag: Wien, 1982; Vol. 10, pp 195-261.
2. Schauer R. Adv. Carbohydr. Chem. Biochem. 40:1982;131.
3. Augé C., David S., Gautheron C. Tetrahedron Lett. 25:1984;4663.
4. Uchida Y., Tsukada Y., Sugimori T. J. Biochem. 96:1984;507.
5. Nees S., Schauer R., Mayer F., Ehrlich K. Hoppe-Seyler's Z. Physiol. Chem. 357:1976;839.
6. Sirbasku D.A., Binkley S.B. Biochim. Biophys. Acta. 198:1970;479.
7. Izard T., Lawrence M.C., Malby R.L., Lilley G.G., Colman P.M. Structure. 2:1994;361.
8. Kragl, U.; Gödde, A.; Wandrey, C.; Lubin, N.; Augé, C. J. Chem. Soc., Perkin Trans. 1 1994, 119.
9. Lawrence M.C., Barbosa J.A.R.G., Smith B.J., Hall N.E., Pilling P.A., Ooi H.C., Marcuccio S.M. J. Mol. Biol. 266:1997;381.
10. Smith B.J., Lawrence M.C., Barbosa J.A.R.G. J. Org. Chem. 64:1999;945.
11. Kong D.C.M., von Itzstein M. Carbohydr. Res. 305:1998;323.
12. Kong D.C.M., von Itzstein M. Tetrahedron Lett. 36:1995;957.
13. Wong, C.-H. In Enzymes in Synthetic Organic Chemistry; Wong, C.-H.; Whitesides, G. M., Eds.; Elsevier: Oxford, 1994; pp 215-228.
14. Fitz W., Schwark J.-R., Wong C.-H. J. Org. Chem. 60:1995;3663. and references therein.
15. David S., Malleron A., Cavayé B. New, J. Chem. 16:1992;751.
16. Lin C.-C., Lin C.-H., Wong C.-H. Tetrahedron Lett. 38:1997;2649.
17. Baumann W., Freidenreich J., Weisshaar G., Brossmer R., Freibolin H. Biol. Chem. Hoppe-Seyler. 370:1989;141.
18. Grob H.J., Brossmer R. FEBS Lett. 232:1988;145.
19. Suttajit M., Urban C., McLean R.L. J. Biol. Chem. 246:1971;810.
20. Schauer R., Stoll S., Zbiral E., Schreiner E., Brandstetter H.H., Vasella A., Baumberger F. Glycoconjugate J. 4:1987;361.
21. Zbiral E., Kleineidam R.G., Schreiner E., Hartmann M., Christian R., Schauer R. Biochem J. 282:1992;511.
22. Shukla A.K., Schauer R. Anal. Biochem. 158:1986;158.
23. Kim M.-J., Hennen W.J., Sweers H.M., Wong C.-H. J. Am. Chem. Soc. 110:1988;6481.
24. von Itzstein, M.; Kiefel, M. J. In Carbohydrates: Targets for Rational Drug Design; Witczak, Z. J.; Nieforth, K. A., Eds.; MDI: New York, 1997; pp 39-82.
25. Chong A.K.J., Pegg M.S., von Itzstein M. Biochem. Biophys. Acta. 1077:1991;65.
26. Ciccotosto S., Kiefel M.J., Abo S., Stewart W., Quelch K., von Itzstein M. Glycoconjugate J. 15:1998;663.
27. Ogura H., Furuhata K., Sato S., Anazawa K., Itoh M., Shitori Y. Carbohydr. Res. 167:1987;77.
28. Greene T.W., Wuts P.G.M. In Protective Groups in Organic Synthesis. 3rd ed. 1999;John Wiley & Sons, New York.
29. Brandstetter, H. H.; Zbiral, E.; Schulz, G. Liebigs Ann. Chem. 1982, 1.
30. Chandler, M.; Bamford, M. J.; Conroy, R.; Lamont, B.; Patel, B.; Patel, V. K.; Steeples, I. P.; Storer, R.; Weir, N. G.; Wright, M.; Williamson, C. J. Chem. Soc., Perkin Trans. 1 1995, 1173.
31. Kiefel, M. J.; Bennett, S.; von Itzstein, M. J. Chem. Soc., Perkin Trans. 1 1996, 439.
32. Deacetylation at -10 °C provided the highest yield of compound 15. Temperatures lower than this resulted in only partial deacetylation, whilst temperatures above -5 °C resulted in the rapid and extensive decomposition of 14.
33. Bednarski M.D., Chenault H.K., Simon E.S., Whitesides G.M. J. Am. Chem. Soc. 109:1987;1283.
34. Fitz W., Wong C.-H. J. Org. Chem. 59:1994;8279.
35. Augé C., David S., Gautheron C., Malleron A., Cavayé B. New J. Chem. 12:1988;733.
36. Deijl C.M., Vliegenthart J.F.G. Biochem. Biophys. Res. Comm. 111:1983;668.
37. 1H NMR spectroscopy to monitor the progress of Neu5Ac aldolase catalysed transformations is also described in ref 17.