Inhibition kinetics of carba- and C-fucosyl analogues of GDP-fucose against fucosyltransferase V: Implication for the reaction mechanism

Bioorganic and Medicinal Chemistry Letters

Volumn 14, Issue 3, 2004, Pages 571-573

  Norris, Andrew J ^a,b   Whitelegge, Julian P ^b   Strouse, M Jane ^b   Faull, Kym F ^b   Toyokuni, Tatsushi ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FUCOSE; FUCOSYLTRANSFERASE;

ARTICLE; CHEMICAL REACTION; ELECTROSPRAY; ENZYME INHIBITION; INHIBITION KINETICS; STEREOCHEMISTRY;

EID: 1642493653     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2003.12.003     Document Type: Article

References (31)

1. Becker D.J., Lowe J.B. Glycobiology. 13:2003;41. R.
2. deVries T., Knegtel R.M.A., Holmes E.H., Macher B.A. Glycobiology. 11:2001;119. R.
3. Weston B.W., Nair R.P., Larsen R.D., Lowe J.B. J. Biol. Chem. 267:1992;4152.
4. Murray B.W., Takayama S., Schultz J., Wong C.-H. Biochemistry. 35:1996;11183.
5. Compain P., Martin O.R. Bioorg. Med. Chem. 9:2001;3077.
6. Mitchell M.L., Tian F., Lee L.V., Wong C.-H. Angew. Chem., Int. Ed. 41:2002;3041.
7. Cai S., Stroud M.R., Hakomori S., Toyokuni T. J. Org. Chem. 57:1992;6693.
8. Luengo J.I., Gleason J.G. Tetrahedron Lett. 33:1992;6911.
9. Norris A.J., Toyokuni T. J. Carbohydrate Chem. 18:1999;1097.
10. Reviews on carba-sugars: (a) Suami T., Ogawa S. Adv. Carbohydr. Chem. 48:1990;21.
11. Ogawa, S., In Carbohydrate Mimics, Concepts and Methods; Chapleur, Y., Ed.: Wiley-VCH: Weinheim, 1998, p 87.
12. A review on C-glycosides: Postema M.H.D. C-Glycoside Synthesis. 1995;CRC, Boca Raton.
13. The carba-sugar and C-glycoside analogues of other sugar nucleotides have been synthesized as potential inhibitors of the corresponding glycosyltransferases. However, very few biological data have been reported, except for the carba-Gal analogue of UDP-Gal. See: Yuasa H., Palcic M.M., Hindsgaul O. Can. J. Chem. 73:1995;2190.
14. Norris A.J., Whitelegge J.P., Faull K.F., Toyokuni T. Biochemistry. 40:2001;3774.
15. Norris A.J., Whitelegge J.P., Faull K.F., Toyokuni T. Anal. Chem. 73:2001;6024.
16. 3 over 13 min at 3 mL/min. The effluent was monitored by absorbance at 254 nm. The GDP-Fuc analogues 1, 2 and 3 eluted at 12.5 min, 11.0 min and 13.0 min, respectively.
17. 31P decoupling. The vicinal coupling constants of ring protons are in concordance with those for a chair conformation (for GDP-Fuc, 1 and 2) and for a distorted half-chair-like conformation (for 3).
18. See refs 11 and 12 for the experimental detail.
19. i)+[GDP-Fuc]
20. Schuster M., Blechert S. Bioorg. Med. Chem. Lett. 11:2001;1809.
21. Horton N.C., Perona J.J. Nat. Struct. Biol. 8:2001;290.
22. Tsopanakis A.D., Herries D.G. Eur. J. Biochem. 83:1978;179.
23. Bovine β-1,4-galactosyltransferase (Gal-T1) is believed to possess two closely spaced (18 Å) metal binding sites. See: O'Keeffe E.T., Hill R.L., Bell J.E. Biochemistry. 19:1980;4954.
24. 2 supports these metal binding sites. One metal seems to be required for UDP-Gal binding and catalysis and the other for catalysis in addition to aiding acceptor binding. See: Ramakrishnan B., Balaji P.V., Qasba P.K. J. Mol. Biol. 318:2002;491.
25. Lariviére L., Gueguen-Chaignon V., Moréra S. J. Mol. Biol. 330:2003;1077.
26. Pedersen L.C., Darden T.A., Negishi M. J. Biol. Chem. 277:2002;21869.
27. Ünligil U.M., Zhou S., Yuwaraj S., Sarkar M., Schachter H., Rini J.M. EMBO J. 19:2000;5269.
28. Deslongchamps P. Stereoelectronic Effects in Organic Chemistry. 1983;Pergamon Press, New York.
29. Kirby A.J. Acc. Chem. Res. 17:1984;305.
30. X-ray crystallographic studies of enzyme-bound substrates of several cellulases have shown that the glycoside ring is distorted into a boat/skew conformation prior to cleavage. See: (a) Davies G.J., Mackenzie L., Varrot A., Dauter M., Brzozowski A.M., Schülein M., Withers S.G. Biochemistry. 37:1998;11707.
31. Sulzenbacher G., Driguez H., Henrissat B., Schülein M., Davies G.J. Biochemistry. 35:1996;15280.