UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism

Journal of Biological Chemistry

Volumn 280, Issue 17, 2005, Pages 16969-16978

  Hernick, Marcy ^a   Gennadios, Heather A ^b   Whittington, Douglas A ^b   Rusche, Kristin M ^a   Christianson, David W ^b   Fierke, Carol A ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; CRYSTAL STRUCTURE; HYDROGEN BONDS; MUTAGENS; PH EFFECTS;

ACTIVE SITES; CATALYST PAIR; DEACETYLATION; HYDROXYMYRISTOYL;

ENZYMES;

ACETIC ACID; GLUTAMIC ACID; HISTIDINE; HYDROLASE; N ACETYLGLUCOSAMINE; OXYGEN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE 3 O (3 HYDROXYMYRISTOYL) N ACETYLGLUCOSAMINE; URIDINE DIPHOSPHATE 3 O (3 HYDROXYMYRISTOYL) N ACETYLGLUCOSAMINE DEACETYLASE; URIDINE DIPHOSPHATE 3 O (3 HYDROXYMYRISTOYL)GLUCOSAMINE; ZINC; AMIDASE; CACODYLIC ACID; DRUG DERIVATIVE; ION; MYRISTIC ACID DERIVATIVE; PALMITIC ACID; UDP 3 O (3 HYDROXYMYRISTOYL) N ACETYLGLUCOSAMINE; UDP 3 O ACYL N ACETYLGLUCOSAMINE DEACETYLASE; UDP-3-O-(3-HYDROXYMYRISTOYL)-N-ACETYLGLUCOSAMINE; UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

AQUIFEX AEOLICUS; ARTICLE; CATALYSIS; CONTROLLED STUDY; DEACETYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; HYDROGEN BOND; IONIZATION; MUTAGENESIS; PH; PKA; PRIORITY JOURNAL; PROTON TRANSPORT; BACTERIUM; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON; ENZYME SPECIFICITY; KINETICS; METABOLISM; MUTATION; PHYSIOLOGY; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

AQUIFEX AEOLICUS; ESCHERICHIA COLI;

AMIDOHYDROLASES; BACTERIA; BINDING SITES; CACODYLIC ACID; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ELECTRONS; ESCHERICHIA COLI; HISTIDINE; HYDROGEN-ION CONCENTRATION; IONS; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; MUTATION; MYRISTIC ACIDS; OXYGEN; PALMITIC ACID; SUBSTRATE SPECIFICITY; URIDINE DIPHOSPHATE N-ACETYLGLUCOSAMINE; ZINC;

EID: 20444469255     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M413560200     Document Type: Article

References (43)

1. Raetz, C. R. H., and Whitfield, C. (2002) Annu. Rev. Biochem. 71, 635-700
2. White, R. J., Margolis, P. S., Trias, J., and Yuan, Z. Y. (2003) Curr. Opin. Pharmacol. 3, 502-507
3. Onishi, H. R., Pelak, B. A., Gerckens, L. S., Silver, L. L., Kahan, F. M., Chen, M. H., Patchett, A. A., Galloway, S. M., Hyland, S. A., Anderson, M. S., and Raetz, C. R. H. (1996) Science 274, 980-982
4. Wyckoff, T. J. O., Raetz, C. R. H., and Jackman, J. E. (1998) Trends Microbiol. 6, 154-159
5. Manocha, S., Feinstein, D., and Kumar, A. (2002) Exp. Opin. Investig. Drugs 11, 1795-1812
6. Jackman, J. E., Raetz, C. R. H., and Fierke, C. A. (1999) Biochemistry 38, 1902-1911
7. Anderson, M., Bull, H., Galloway, S., Kelly, T., Mohan, S., Radika, K., and Raetz, C. (1993) J. Biol. Chem. 268, 19858-19865
8. Jackman, J. E., Fierke, C. A., Tumey, L. N., Pirrung, M., Uchiyama, T., Tahir, S. H., Hindsgaul, O., and Raetz, C. R. H. (2000) J. Biol. Chem. 275, 11002-11009
9. Pirrung, M. C., Tumey, L. N., Raetz, C. R. H., Jackman, J. E., Snehalatha, K., McClerren, A. L., Fierke, C. A., Gantt, S. L., and Rusche, K. M. (2002) J. Med. Chem. 45, 4359-4370
10. Clements, J. M., Coignard, F., Johnson, I., Chandler, S., Palan, S., Waller, A., Wijkmans, J., and Hunter, M. G. (2002) Antimicrob. Agents Chemother. 46, 1793-1799
11. Christianson, D. W., and Lipscomb, W. N. (1989) Acc. Chem. Res. 22, 62-69
12. Aoki, S., and Kimura, E. (2004) Comp. Coord. Chem. II 8, 601-640
13. Lipscomb, W. N., and Strater, N. (1996) Chem. Rev. 96, 2375-2433
14. Hernick, M., and Fierke, C. A. (2005) Arch. Biochem. Biophys. 433, 71-84
15. Whittington, D. A., Rusche, K. M., Shin, H., Fierke, C. A., and Christianson, D. W. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 8146-8150
16. Coggins, B. E., Li, X. C., McClerren, A. L., Hindsgaul, O., Raetz, C. R. H., and Zhou, P. (2003) Nat. Struct. Biol. 10, 645-651
17. Jackman, J. E., Raetz, C. R. H., and Fierke, C. A. (2001) Biochemistry 40, 514-523
18. Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., and Pavletich, N. P. (1999) Nature 401, 188-193
19. McClerren, A. L., Zhou, P., Guan, Z., Raetz, C. R. H., and Rudolph, J. (2005) Biochemistry 44, 1106-1113
20. Young, K., Silver, L. L., Bramhill, D., Cameron, P., Evelaud, S. S., Raetz, C. R. H., Hyland, S. A., and Anderson, M. S. (1995) J. Biol. Chem. 270, 30384-30391
21. McClure, C. P., Rusche, K. M., Peariso, K., Jackman, J. E., Fierke, C. A., and Penner-Hahn, J. E. (2003) J. Inorg. Biochem. 94, 78-85
22. Kelly, T. M., Stachula, S. A., Raetz, C. R. H., and Anderson, M. S. (1993) J. Biol. Chem. 268, 19866-19874
23. Sorensen, P. G., Lutkenhaus, J., Young, K., Eveland, S. S., Anderson, M. S., and Raetz, C. R. H. (1996) J. Biol. Chem. 271, 25898-25905
24. Srere, P. A., Kosicki, G. W., and Lumry, R. (1961) Biochim. Biophys. Acta 50, 184-&
25. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 306-326
26. Navaza, J. (1994) Acta Crystallogr. Sect. A 50, 157-163
27. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 905-921
28. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Acta Crystallogr. Sect. A 47, 110-119
29. Pflugrath, J. W. (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 1718-1725
30. Kissinger, C. R., Gehlhaar, D. K., and Smith, B. A. (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 484-491
31. Esnouf, R. M. (1997) J. Mol. Graph. Model. 15, 132-134
32. Cleland, W. W. (1982) Methods Enzymol. 87, 390-405
33. Huheey, J. E., Keiter, E. A., and Kelter, R. L. (1993) Inorganic Chemistry: Principles of Structure and Reactivity, pp. 318-355, Harper Collins College Publishers, New York
34. Schowen, K. B., and Schowen, R. L. (1982) Methods Enzymol. 87, 551-606
35. Fersht, A. R. (1999) Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding, pp. 169-190, W. H. Freeman & Co., New York
36. Coggins, B. E., McClerren, A. L., Jiang, L., Li, X., Rudolph, J., Hindsgaul, O., Raetz, C. R. H., and Zhou, P. (2005) Biochemistry 44, 1114-1126
37. Cha, J., and Auld, D. S. (1997) Biochemistry 36, 16019-16024
38. Wetterholm, A., Medina, J. F., Radmark, O., Shapiro, R., Haeggstrom, J. Z., Vallee, B. L., and Samuelsson, B. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 9141-9145
39. Mildvan, A. S., Weber, D. J., and Kuliopulos, A. (1992)Arch. Biochem. Biophys. 294, 327-340
40. Mildvan, A. S. (2004) Biochemistry 43, 14517-14520
41. Merkler, D. J., and Schramm, V. L. (1993) Biochemistry 32, 5792-5799
42. Bachovchin, W. W. (2001) Magn. Reson. Chem. 39, S199-S213
43. Hedstrom, L. (2002) Chem. Rev. 102, 4501-4523