Structural and kinetic differences between human and Aspergillus fumigatus D-glucosamine-6-phosphate N-acetyltransferase

Biochemical Journal

Volumn 415, Issue 2, 2008, Pages 217-223

  Hurtado Guerrero, Ramon ^a   Raimi, Olawale G ^a   Min, Jinrong ^b   Zeng, Hong ^b   Vallius, Laura ^a   Shepherd, Sharon ^a   Ibrahim, Adel F M ^a   Wu, Hong ^b   Plotnikov, Alexaner N ^b,c   van Aalten, Daan M F ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b UNIVERSITY OF TORONTO   (Canada)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

Aspergillus fumigatus; Inhibitor design; Kinetics; Mutagenesis; Protein structure; UDP GlcNAc biosynthesis; X ray crystallography

Indexed keywords

BINDING ENERGY; BINDING SITES; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; CRYSTALLOGRAPHY; ENZYMES; INTERNET PROTOCOLS; MINERALOGY; MUTAGENESIS; SUGAR (SUCROSE); SUGARS;

ACETYLGLUCOSAMINE; ACTIVE SITES; ASPERGILLUS FUMIGATUS; BINDING POCKETS; BIOSYNTHETIC PATHWAYS; CANDIDA ALBICANS; CAUSATIVE AGENTS; DRASTIC EFFECTS; FUNGAL ENZYMES; GENE DISRUPTIONS; GLUCOSAMINE; INHIBITOR DESIGN; KEY INTERMEDIATES; KINETIC; KINETIC CHARACTERIZATIONS; MOLECULE INHIBITORS; PROTEIN STRUCTURE; SELECTIVE INHIBITORS; UDP-GLCNAC BIOSYNTHESIS;

X RAY CRYSTALLOGRAPHY;

GLUCOSAMINE PHOSPHATE ACETYLTRANSFERASE;

AMINO ACID SUBSTITUTION; ARTICLE; ASPERGILLUS FUMIGATUS; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME STRUCTURE; MUTAGENESIS; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SPECIES DIFFERENCE; STEADY STATE;

AMINO ACID SEQUENCE; ASPERGILLUS FUMIGATUS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; FUNGAL PROTEINS; GLUCOSAMINE 6-PHOSPHATE N-ACETYLTRANSFERASE; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

ASPERGILLUS FUMIGATUS; CANDIDA ALBICANS;

EID: 54049143647     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20081000     Document Type: Article

References (36)

1. Latge, J. P. (1999) Aspergillus fumigatus and aspergillosis. Clin. Microbiol. Rev. 12, 310-350
2. Denning, D. W. (1998) Invasive aspergillosis. Clin. Infect. Dis. 26, 781-803
3. Golan, Y. (2005) Overview of transplant mycology. Am. J. Health Syst. Pharm. 62, S17-S21
4. Herbrecht, R., Denning, D. W., Patterson, T. F., Bennett, J. E., Greene, R. E., Oestmann, J.-W., Kern, W. V., Marr, K. A., Ribaud, P., Lortholary. O. et al. (2002) Voriconazole versus amphotericin b for primary therapy of invasive aspergillosis. N. Engl. J. Med. 347, 408-415
5. Dupont, B. (1990) Itraconazole therapy in aspergillosis: study In 49 patients. J. Am. Acad. Dermatol. 23, 607-614
6. Spanakis, E. K., Aperis, G. and Mylonakis, E. (2006) New agents for the treatment of fungal infections: clinical efficacy and gaps in coverage. Clin. Infect. Dis. 43, 1060-1068
7. Fontaine, T., Mouyna, I., Hartland, R. P., Paris, S., and Latgé, J. P. (1997) From the surface to the inner layer of the fungal cell wall. Biochem. Soc. Trans. 25, 194-199
8. Latgé. J. P., Mouyna, I., Tekaia, F., Beauvais, A., Debeaupuis, J. P. and Nierman, W. (2005) Specific molecular features in the organization and biosynthesis of the cell wall of Aspergillus fumigatus. Med. Mycol. 43, S15-S22
9. Katz, D. and Rosenberger, R. F. (1970) A mutation in Aspergillus nidulans producing hyphal walls which lack chitin. Biochim. Biophys. Acta 208, 452-460
10. Takeda, J. and Kinoshita, T. (1995) GPI-anchor biosynthesis. Trends Biochem. Sci. 20, 367-371
11. Selitrennikoff, C. P. and Sonneborn, D. R. (1976) The last two pathway-specific enzyme activities of hexosamine biosynthesis are present in Blastocladiella emersonii zoospores prior to germination. Biochim. Biophys. Acta 451, 408-416
12. Hofmann, M., Boles, E. and Zimmermann, F. K. (1994) Characterization of the essential yeast gene encoding N-acetylglucosamine-phosphate mutase. Eur. J. Biochem. 221, 741-747
13. Etchebehere, L. C., Simon, M. N., Campanhã, R. B., Zapella, P. D., Véron, M. and Maia, J. C. (1993) Developmental regulation of hexosamine biosynthesis by protein phosphatases 2a and 2c in Blastocladiella emersonfii. J. Bacteriol. 175, 5022-5027
14. Vetting, M. W., S deCarvalho, L. P., Yu, M., Hegde, S. S., Magnet. S., Roderick, S. L. and Blanchard, J. S. (2005) Structure and functions of the GNAT superfamily of acetyltransferases. Arch. Biochem. Biophys. 433, 212-226
15. Mio. T., Yamada-Okabe, T., Arisawa, M. and Yamada-Okabe, H. (1999) Saccharomyces cerevisiae gna1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis. J. Biol. Chem. 274, 424-429
16. Mio, T., Kokado, M., Arisawa, M. and Yamada-Okabe, H. (2000) Reduced virulence of Candida albicans mutants lacking the gna1 gene encoding glucosamine-6-phosphate acetyltransferase. Microbiology 146, 1753-1758
17. Boehmelt, G., Wakeham, A., Elia, A., Sasaki, T., Plyte, S., Potter, J.. Yang, Y., Tsang, E., Ruland, J., Iscove, N. N. et al. (2000) Decreased UDP-GlcNAc levels abrogate proliferation control in emeg32-deficient cells. EMBO J. 19, 5092-5104
18. Riddles, P., Blakeley, R. and Zerner, B. (1979) Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid)-a reexamination. Anal. Biochem. 97, 75-81
19. Gehring, A. M,, Lees, W. J., Mindiola, D. J., Walsh, C. T. and Brown, E. D. (1996) Acetyltranster precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional glmu protein of Escherichia coli. Biochemistry 35, 579-585
20. Leatherbarrow, R. J. (2001) GraFit Version 5, Erithacus Software Ltd., Horley, U.K.
21. Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
22. Sheldrick, G. M. and Schneider, T. R. (1997) SHELXL: high-resolution refinement. Methods Enzymol. 277, 319-343
23. Perrakis, A., Morris, R. and Lamzin, V. S. (1999) Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6, 458-463
24. Murshudov, G. N., Vagin, A. A. and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D Biol. Crystallogr. D53, 240-255
25. Emsley. P. and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D Biol. Crystallogr. D60. 2126-2132
26. Vagin, A. and Teplyakov, A. (1997) Molrep: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025
27. Schuettelkopf, A. W. and van Aalten, D. M. F. (2004) Prodrg: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. Sect. D Biol. Crystallogr. D60, 1355-1363
28. Vriend, G. (1990) WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8, 52-56
29. DeLano, W. L. (2004) Use of pymol as a communications tool for molecular science. Abstr. Pap. Am. Chem. Soc. 228, 030-CHED
30. Peneff, C., Mengin-Lecreulx, D. and Bourne, Y. (2001) The crystal structures of apo and complexed Saccharomyces cerevisiae gna1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase. J. Biol. Chem. 276, 1632&-16334
31. Pattabiraman, T. N. and Bachhawat, B. K. (1962) Purification of glucosamine-6-phosphate N-acetylase from sheep brain. Biochim. Biophys. Acta 59, 681-689
32. Boehmelt, G., Fialka. I.. Brothers, G., McGinley, M. D., Patterson, S. D., Mo, R., Hui, C. C., Chung, S., Huber, L. A., Mak, T. W. and Iscove, N. N. (2000) Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase emeg32. Differential expression and intracellular membrane association. J. Biol. Chem. 275, 12821-12832
33. Gao, F., Yan, X., Shakya, T., Baettig, O. M., Ait-Mohand-Brunet, S., Berghuis, A. M., Wright, G. D. and Auclair, K. (2006) Synthesis and structure-activity relationships of truncated bisubstrate inhibitors of aminoglycoside 6′-N-acelyltransferases. J. Med. Chem. 49, 5273-5281
34. Wolf, E., De Angelis, J., Khalil, E. M., Cole, P. A. and Burley, S. K. (2002) X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition. J. Mol. Biol. 317, 215-224
35. Poux, A. N., Cebrat. M., Kim, C. M., Cole, P. A. and Marmorstein, R. (2002) Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor. Proc. Natl. Acad. Sci. U.S.A. 99, 14065-14070
36. Lipinski, C. A. (2000) Drug-like properties and the causes of poor solubility and poor permeability. J. Pharmacol. Toxicol. Methods 44, 235-249