Discovery of selective small-molecule activators of a bacterial glycoside hydrolase

Angewandte Chemie - International Edition

Volumn 53, Issue 49, 2014, Pages 13419-13423

  Darby, John F ^a   Landström, Jens ^a   Roth, Christian ^a   He, Yuan ^a   Davies, Gideon J ^a   Hubbard, Roderick E ^a  

^a UNIVERSITY OF YORK   (United Kingdom)

Author keywords

Enzyme catalysis; Glycoside hydrolase; Glycosylation; Inhibitors; Protein structures

Indexed keywords

CORROSION INHIBITORS; ENZYME INHIBITION; GLYCOSYLATION; HYDROLASES; MOLECULES; RATE CONSTANTS; SUGARS;

CATALYTIC CENTER; ENZYME CATALYSIS; ENZYME INHIBITORS; GLYCOSIDE HYDROLASES; INDUSTRIAL PROCESSS; MICHAELIS CONSTANTS; PROTEIN STRUCTURES; THERAPEUTIC AGENTS;

ENZYME ACTIVITY;

GLYCOSIDASE; MOLECULAR LIBRARY;

BACTEROIDES; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECTS; ENZYME ACTIVATION; ENZYMOLOGY; METABOLISM; MOLECULAR LIBRARY; PHARMACOLOGY; X RAY CRYSTALLOGRAPHY;

BACTEROIDES; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; GLYCOSIDE HYDROLASES; MODELS, MOLECULAR; SMALL MOLECULE LIBRARIES;

EID: 84915820942     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201407081     Document Type: Article

References (24)

1. T. M. Bakheet, A. J. Doig, Bioinformatics 2009, 25, 451-457.
2. B. Xiao, M. J. Sanders, D. Carmena, N. J. Bright, L. F. Haire, E. Underwood, B. R. Patel, R. B. Heath, P. A.Walker, S. Hallen, F. Giordanetto, S. R. Martin, D. Carling, S. J. Gamblin, Nat. Commun. 2013, 4:3017 doi: 10.1038/ncomms4017.
3. K. Kamata, M. Mitsuya, T. Nishimura, J.-i. Eiki, Y. Nagata, Structure 2004, 12, 429-438.
4. S. Perez-Miller, H. Younus, R. Vanam, C. H. Chen, D. Mochly- Rosen, T. D. Hurley, Nat. Struct. Mol. Biol. 2010, 17, 159-164.
5. B. P. Hubbard, D. A. Sinclair, Trends Pharmacol. Sci. 2014, 35, 146-154.
6. M. N. Schulz, R. E. Hubbard, Curr. Opin. Pharmacol. 2009, 9, 615-621.
7. R. E. Hubbard, J. B. Murray, Methods Enzymol. 2011, 493, 509-531.
8. G.W. Hart, Y. Akimoto in Essentials of Glycobiology, 2ednd ed(Eds.: A. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi, G. W. Hart, M. E. Etzler), Cold Spring Harbor, New York, 2009.
9. S. A. Yuzwa, X. Shan, M. S. Macauley, T. Clark, Y. Skorobogatko, K. Vosseller, D. J. Vocadlo, Nat. Chem. Biol. 2012, 8, 393-399.
10. T. M. Gloster, D. J. Vocadlo, Nat. Chem. Biol. 2012, 8, 683-694.
11. Y. He, C. Martinez-Fleites, A. Bubb, T. M. Gloster, G. J. Davies, Carbohydr. Res. 2009, 344, 627-631.
12. H. C. Dorfmueller, V. S. Borodkin, M. Schimpl, D. M. van Aalten, Biochem. J. 2009, 420, 221-227.
13. H. C. Dorfmueller, D. M. van Aalten, FEBS Lett. 2010, 584, 694-700.
14. M. N. Schulz, J. Landstrom, K. Bright, R. E. Hubbard, J. Comput.-Aided Mol. Des. 2011, 25, 611-620.
15. M. Mayer, B. Meyer, Angew. Chem. Int. Ed. 1999, 38, 1784-1788;
16. Angew. Chem. 1999, 111, 1902-1906.
17. A. D. Gossert, C. Henry, M. J. Blommers, W. Jahnke, C. Fernandez, J. Biomol. NMR 2009, 43, 211-217.
18. P. J. Hajduk, E. T. Olejniczak, S.W. Fesik, J. Am. Chem. Soc. 1997, 119, 12257-12261.
19. L. Fielding, Prog. Nucl. Magn. Reson. Spectrosc. 2007, 51, 219-242.
20. J. A. Zorn, J. A. Wells, Nat. Chem. Biol. 2010, 6, 179-188.
21. J. F. Sebastian, J. Chem. Educ. 1987, 64, 1031-1032.
22. B. F. Cravatt, E. J. Sorensen, Curr. Opin. Chem. Biol. 2000, 4, 663-668.
23. M. L. Cardenas, A. Cornish-Bowden, Biochem. J. 1989, 257, 339-345.
24. R. J. Dennis, E. J. Taylor, M. S. Macauley, K. A. Stubbs, J. P. Turkenburg, S. J. Hart, G. N. Black, D. J. Vocadlo, G. J. Davies, Nat. Struct. Mol. Biol. 2006, 13, 365-371.