Metal mediated inhibition of methionine aminopeptidase by quinolinyl sulfonamides

Biochemical and Biophysical Research Communications

Volumn 339, Issue 2, 2006, Pages 506-513

  Huang, Min ^a   Xie, Sheng Xue ^a   Ma, Ze Qiang ^a   Hanzlik, Robert P ^a   Ye, Qi Zhuang ^a  

^a UNIVERSITY OF KANSAS   (United States)

Author keywords

Enzyme inhibition; Metalloenzyme; Protein structure

Indexed keywords

COBALT; FERROUS ION; HYDROGEN; MANGANESE; METAL; METHIONYL AMINOPEPTIDASE; N (5 CHLOROQUINOLIN 8 YL)METHANESULFONAMIDE; N (QUINOLIN 8 YL)METHANESULFONAMIDE; NICKEL; ORGANIC COMPOUND; PEPTIDE; SULFONAMIDE; UNCLASSIFIED DRUG; ZINC;

ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG IDENTIFICATION; DRUG MECHANISM; DRUG POTENCY; DRUG SCREENING; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME STABILITY; ESCHERICHIA COLI; GENE LIBRARY; GENETIC VARIABILITY; HIGH THROUGHPUT SCREENING; HYDROGEN BOND; MEDICAL INFORMATION; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; WASTE; X RAY ANALYSIS;

AMINOPEPTIDASES; BENZOQUINONES; BINDING SITES; CATIONS, DIVALENT; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDROGEN BONDING; INHIBITORY CONCENTRATION 50; METALS, HEAVY; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEASE INHIBITORS; PROTEIN STRUCTURE, TERTIARY; SPECTRUM ANALYSIS; SULFONAMIDES;

ESCHERICHIA COLI;

EID: 28444467469     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.11.042     Document Type: Article

References (39)

1. R.A. Bradshaw, W.W. Brickey, and K.W. Walker N-terminal processing: the methionine aminopeptidase and N alpha-acetyl transferase families Trends Biochem. Sci. 23 1998 263 267
2. S.Y. Chang, E.C. McGary, and S. Chang Methionine aminopeptidase gene of Escherichia coli is essential for cell growth J. Bacteriol. 171 1989 4071 4072
3. C.G. Miller, A.M. Kukral, J.L. Miller, and N.R. Movva pepM is an essential gene in Salmonella typhimurium J. Bacteriol. 171 1989 5215 5217
4. M.D. Vaughan, P.B. Sampson, and J.F. Honek Methionine in and out of proteins: targets for drug design Curr. Med. Chem. 9 2002 385 409
5. E.C. Griffith, Z. Su, S. Niwayama, C.A. Ramsay, Y.H. Chang, and J.O. Liu Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2 Proc. Natl. Acad. Sci. USA 95 1998 15183 15188
6. E.C. Griffith, Z. Su, B.E. Turk, S. Chen, Y.H. Chang, Z. Wu, K. Biemann, and J.O. Liu Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin Chem. Biol. 4 1997 461 471
7. N. Sin, L. Meng, M.Q. Wang, J.J. Wen, W.G. Bornmann, and C.M. Crews The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2 Proc. Natl. Acad. Sci. USA 94 1997 6099 6103
8. H. Towbin, K.W. Bair, J.A. DeCaprio, M.J. Eck, S. Kim, F.R. Kinder, A. Morollo, D.R. Mueller, P. Schindler, H.K. Song, J. van Oostrum, R.W. Versace, H. Voshol, J. Wood, S. Zabludoff, and P.E. Phillips Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors J. Biol. Chem. 278 2003 52964 52971
9. I.S. Sheen, K.S. Jeng, W.J. Jeng, C.J. Jeng, Y.C. Wang, S.L. Gu, S.Y. Tseng, C.M. Chu, C.H. Lin, and K.M. Chang Fumagillin treatment of hepatocellular carcinoma in rats: an in vivo study of antiangiogenesis World J. Gastroenterol. 11 2005 771 777
10. M.J. Morowitz, R. Barr, Q. Wang, R. King, N. Rhodin, B. Pawel, H. Zhao, S.A. Erickson, G.S. Sheppard, J. Wang, J.M. Maris, and S. Shusterman Methionine aminopeptidase 2 inhibition is an effective treatment strategy for neuroblastoma in preclinical models Clin. Cancer Res. 11 2005 2680 2685
11. S.G. Bernier, D.D. Lazarus, E. Clark, B. Doyle, M.T. Labenski, C.D. Thompson, W.F. Westlin, and G. Hannig A methionine aminopeptidase-2 inhibitor, PPI-2458, for the treatment of rheumatoid arthritis Proc. Natl. Acad. Sci. USA 101 2004 10768 10773
12. S. Liu, J. Widom, C.W. Kemp, C.M. Crews, and J. Clardy Structure of human methionine aminopeptidase-2 complexed with fumagillin Science 282 1998 1324 1327
13. E.A. Kruger, and W.D. Figg TNP-470: an angiogenesis inhibitor in clinical development for cancer Expert Opin. Investig. Drugs 9 2000 1383 1396
14. S. Chen, J.A. Vetro, and Y.H. Chang The specificity in vivo of two distinct methionine aminopeptidases in Saccharomyces cerevisiae Arch. Biochem. Biophys. 398 2002 87 93
15. W.T. Lowther, D.A. McMillen, A.M. Orville, and B.W. Matthews The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase Proc. Natl. Acad. Sci. USA 95 1998 12153 12157
16. S.J. Keding, N.A. Dales, S. Lim, D. Beauliu, and D.H. Rich Synthesis of (3R)-amino-(2S)-hydroxy amino acids for inhibition of methionine aminopeptidase-1 Synth. Commun. 28 1998 4463 4470
17. C. Oefner, A. Douangamath, A. D'Arcy, S. Hafeli, D. Mareque, A. Mac Sweeney, J. Padilla, S. Pierau, H. Schulz, M. Thormann, S. Wadman, and G.E. Dale The 1.15A crystal structure of the Staphylococcus aureus methionyl- aminopeptidase and complexes with triazole based inhibitors J. Mol. Biol. 332 2003 13 21
18. J. Wang, G.S. Sheppard, P. Lou, M. Kawai, C. Park, D.A. Egan, A. Schneider, J. Bouska, R. Lesniewski, and J. Henkin Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese Biochemistry 42 2003 5035 5042
19. T. Garrabrant, R.W. Tuman, D. Ludovici, R. Tominovich, R.L. Simoneaux, R.A. Galemmo Jr., and D.L. Johnson Small molecule inhibitors of methionine aminopeptidase type 2 (MetAP-2) fail to inhibit endothelial cell proliferation or formation of microvessels from rat aortic rings in vitro Angiogenesis 7 2004 91 96
20. R. Schiffmann, A. Heine, G. Klebe, and C.D. Klein Metal ions as cofactors for the binding of inhibitors to methionine aminopeptidase: a critical view of the relevance of in vitro metalloenzyme assays Angew. Chem. Int. Ed. Engl. 44 2005 3620 3623
21. Q.L. Luo, J.Y. Li, Z.Y. Liu, L.L. Chen, J. Li, Z. Qian, Q. Shen, Y. Li, G.H. Lushington, Q.Z. Ye, and F.J. Nan Discovery and structural modification of inhibitors of methionine aminopeptidases from Escherichia coli and Saccharomyces cerevisiae J. Med. Chem. 46 2003 2631 2640
22. Q.Z. Ye, S.X. Xie, M. Huang, W.J. Huang, J.P. Lu, and Z.Q. Ma Metalloform-selective inhibitors of Escherichia coli methionine aminopeptidase and X-ray structure of a Mn(II)-form enzyme complexed with an inhibitor J. Am. Chem. Soc. 126 2004 13940 13941
23. A. Douangamath, G.E. Dale, A. D'Arcy, M. Almstetter, R. Eckl, A. Frutos-Hoener, B. Henkel, K. Illgen, S. Nerdinger, H. Schulz, A. Mac Sweeney, M. Thormann, A. Treml, S. Pierau, S. Wadman, and C. Oefner Crystal structures of Staphylococcus aureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate J. Med. Chem. 47 2004 1325 1328
24. J.Y. Li, L.L. Chen, Y.M. Cui, Q.L. Luo, J. Li, F.J. Nan, and Q.Z. Ye Specificity for inhibitors of metal-substituted methionine aminopeptidase Biochem. Biophys. Res. Commun. 307 2003 172 179
25. G. Yang, R.B. Kirkpatrick, T. Ho, G.F. Zhang, P.H. Liang, K.O. Johanson, D.J. Casper, M.L. Doyle, J.P. Marino Jr., S.K. Thompson, W. Chen, D.G. Tew, and T.D. Meek Steady-state kinetic characterization of substrates and metal-ion specificities of the full-length and N-terminally truncated recombinant human methionine aminopeptidases (type 2) Biochemistry 40 2001 10645 10654
26. Y. Zhou, X.C. Guo, T. Yi, T. Yoshimoto, and D. Pei Two continuous spectrophotometric assays for methionine aminopeptidase Anal. Biochem. 280 2000 159 165
27. Collaborative Computational Project Number 4, The CCP4 Suite: Programs for Protein Crystallography, Acta Cryst. D 50 (1994) 760-763.
28. P. Emsley, and K. Cowtan Coot: model-building tools for molecular graphics Acta Crystallogr. D Biol. Crystallogr. 60 2004 2126 2132
29. W.L. DeLano, The PyMOL Molecular Graphics System, on World Wide Web http://www.pymol.org (2002).
30. A. Almela, M. Huebra, M.P. Elizalde, and B. Menoyo Copper(II) extraction by 4-chloro-N-8-quinolinylbenzenesulfonamide dissolved in toluene J. Chem. Technol. Biotechnol. 79 2004 299 305
31. W.T. Lowther, and B.W. Matthews Structure and function of the methionine aminopeptidases Biochim. Biophys. Acta 1477 2000 157 167
32. N.J. Cosper, V.M. D'Souza, R.A. Scott, and R.C. Holz Structural evidence that the methionyl aminopeptidase from Escherichia coli is a mononuclear metalloprotease Biochemistry 40 2001 13302 13309
33. W.T. Lowther, A.M. Orville, D.T. Madden, S. Lim, D.H. Rich, and B.W. Matthews Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis Biochemistry 38 1999 7678 7688
34. R.P. Hanzlik Inorganic Aspects of Biological and Organic Chemistry 1976 Academic Press New York
35. H. Sigel, and D.B. McCormick Discriminating behavior of metal ions and ligands with regard to their biological significance Acc. Chem. Res. 1970 201 208
36. D. Dhanak, G. Burton, L.T. Christmann, M.G. Darcy, K.C. Elrod, A. Kaura, R.M. Keenan, J.O. Link, C.E. Peishoff, and D.H. Shah Metal mediated protease inhibition: design and synthesis of inhibitors of the human cytomegalovirus (hCMV) protease Bioorg. Med. Chem. Lett. 10 2000 2279 2282
37. B.A. Katz, J.M. Clark, J.S. Finer-Moore, T.E. Jenkins, C.R. Johnson, M.J. Ross, C. Luong, W.R. Moore, and R.M. Stroud Design of potent selective zinc-mediated serine protease inhibitors Nature 391 1998 608 612
38. K.W. Walker, E. Yi, and R.A. Bradshaw Yeast (Saccharomyces cerevisiae) methionine aminopeptidase I: rapid purification and improved activity assay Biotechnol. Appl. Biochem. 29 Pt 2 1999 157 163
39. C.E. Outten, and T.V. O'Halloran Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis Science 292 2001 2488 2492