메뉴 건너뛰기




Volumn 168, Issue 2, 2009, Pages 158-167

Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470

Author keywords

Encephalitozoon cuniculi; Enterocytozoon bieneusi; Methionine Aminopeptidase; Microsporidia; Therapeutics; X ray crystal structure

Indexed keywords

FUMAGILLIN; FUMAGILLOL CHLOROACETYLCARBAMATE; METHIONYL AMINOPEPTIDASE 2;

EID: 70349270555     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2009.07.008     Document Type: Article
Times cited : (31)

References (68)
  • 3
    • 0028512960 scopus 로고
    • Enzyme histochemical identification of the Golgi apparatus in the microsporidian, Glugea stephani
    • Takvorian P.M., and Cali A. Enzyme histochemical identification of the Golgi apparatus in the microsporidian, Glugea stephani. J Eukaryot Microbiol 41 (1994) 63S-64S
    • (1994) J Eukaryot Microbiol , vol.41
    • Takvorian, P.M.1    Cali, A.2
  • 4
    • 0037158721 scopus 로고    scopus 로고
    • A mitochondrial remnant in the microsporidian Trachipleistophora hominis
    • Williams B.A., Hirt R.P., Lucocq J.M., and Embley T.M. A mitochondrial remnant in the microsporidian Trachipleistophora hominis. Nature 418 (2002) 865-869
    • (2002) Nature , vol.418 , pp. 865-869
    • Williams, B.A.1    Hirt, R.P.2    Lucocq, J.M.3    Embley, T.M.4
  • 5
    • 0037384263 scopus 로고    scopus 로고
    • Congruent evidence from alpha-tubulin and beta-tubulin gene phylogenies for a zygomycete origin of microsporidia
    • Keeling P.J. Congruent evidence from alpha-tubulin and beta-tubulin gene phylogenies for a zygomycete origin of microsporidia. Fungal Genet Biol 38 (2003) 298-309
    • (2003) Fungal Genet Biol , vol.38 , pp. 298-309
    • Keeling, P.J.1
  • 7
    • 0026073166 scopus 로고
    • Evidence for widespread occurrence of antibodies to Encephalitozoon cuniculi (Microspora) in man provided by ELISA and other serological tests
    • Hollister W.S., Canning E.U., and Willcox A. Evidence for widespread occurrence of antibodies to Encephalitozoon cuniculi (Microspora) in man provided by ELISA and other serological tests. Parasitology 102 Pt 1 (1991) 33-43
    • (1991) Parasitology , vol.102 , Issue.PART 1 , pp. 33-43
    • Hollister, W.S.1    Canning, E.U.2    Willcox, A.3
  • 8
    • 0029263282 scopus 로고
    • Vittaforma corneae n. comb. for the human microsporidium Nosema corneum Shadduck, Meccoli, Davis & Font, 1990, based on its ultrastructure in the liver of experimentally infected athymic mice
    • Silveira H., and Canning E.U. Vittaforma corneae n. comb. for the human microsporidium Nosema corneum Shadduck, Meccoli, Davis & Font, 1990, based on its ultrastructure in the liver of experimentally infected athymic mice. J Eukaryot Microbiol 42 (1995) 158-165
    • (1995) J Eukaryot Microbiol , vol.42 , pp. 158-165
    • Silveira, H.1    Canning, E.U.2
  • 9
    • 0038814788 scopus 로고    scopus 로고
    • Ultrastructure and development of Pleistophora ronneafiei n. sp., a microsporidium (Protista) in the skeletal muscle of an immune-compromised individual
    • Cali A., and Takvorian P.M. Ultrastructure and development of Pleistophora ronneafiei n. sp., a microsporidium (Protista) in the skeletal muscle of an immune-compromised individual. J Eukaryot Microbiol 50 (2003) 77-85
    • (2003) J Eukaryot Microbiol , vol.50 , pp. 77-85
    • Cali, A.1    Takvorian, P.M.2
  • 10
    • 0026102044 scopus 로고
    • Isolation and characterization of a new human microsporidian, Encephalitozoon hellem (n. sp.), from three AIDS patients with keratoconjunctivitis
    • Didier E.S., Didier P.J., Friedberg D.N., et al. Isolation and characterization of a new human microsporidian, Encephalitozoon hellem (n. sp.), from three AIDS patients with keratoconjunctivitis. J Infect Dis 163 (1991) 617-621
    • (1991) J Infect Dis , vol.163 , pp. 617-621
    • Didier, E.S.1    Didier, P.J.2    Friedberg, D.N.3
  • 11
    • 0022068291 scopus 로고
    • Occurrence of a new microsporidan: Enterocytozoon bieneusi n.g., n. sp., in the enterocytes of a human patient with AIDS
    • Desportes I., Le Charpentier Y., Galian A., et al. Occurrence of a new microsporidan: Enterocytozoon bieneusi n.g., n. sp., in the enterocytes of a human patient with AIDS. J Protozool 32 (1985) 250-254
    • (1985) J Protozool , vol.32 , pp. 250-254
    • Desportes, I.1    Le Charpentier, Y.2    Galian, A.3
  • 12
    • 0027346642 scopus 로고
    • Septata intestinalis N. G., N. sp., an intestinal microsporidian associated with chronic diarrhea and dissemination in AIDS patients
    • Cali A., Kotler D.P., and Orenstein J.M. Septata intestinalis N. G., N. sp., an intestinal microsporidian associated with chronic diarrhea and dissemination in AIDS patients. J Eukaryot Microbiol 40 (1993) 101-112
    • (1993) J Eukaryot Microbiol , vol.40 , pp. 101-112
    • Cali, A.1    Kotler, D.P.2    Orenstein, J.M.3
  • 13
    • 0029907578 scopus 로고    scopus 로고
    • Myositis associated with a newly described microsporidian, Trachipleistophora hominis, in a patient with AIDS
    • Field A.S., Marriott D.J., Milliken S.T., et al. Myositis associated with a newly described microsporidian, Trachipleistophora hominis, in a patient with AIDS. J Clin Microbiol 34 (1996) 2803-2811
    • (1996) J Clin Microbiol , vol.34 , pp. 2803-2811
    • Field, A.S.1    Marriott, D.J.2    Milliken, S.T.3
  • 14
    • 0032078454 scopus 로고    scopus 로고
    • Brachiola vesicularum, n. g., n. sp., a new microsporidium associated with AIDS and myositis
    • Cali A., Takvorian P.M., Lewin S., et al. Brachiola vesicularum, n. g., n. sp., a new microsporidium associated with AIDS and myositis. J Eukaryot Microbiol 45 (1998) 240-251
    • (1998) J Eukaryot Microbiol , vol.45 , pp. 240-251
    • Cali, A.1    Takvorian, P.M.2    Lewin, S.3
  • 15
    • 3042551358 scopus 로고    scopus 로고
    • Fatal myositis due to the microsporidian Brachiola algerae, a mosquito pathogen
    • Coyle C.M., Weiss L.M., Rhodes III L.V., et al. Fatal myositis due to the microsporidian Brachiola algerae, a mosquito pathogen. N Engl J Med 351 (2004) 42-47
    • (2004) N Engl J Med , vol.351 , pp. 42-47
    • Coyle, C.M.1    Weiss, L.M.2    Rhodes III, L.V.3
  • 16
    • 33644819505 scopus 로고    scopus 로고
    • Transfer of the members of the genus Brachiola (microsporidia) to the genus Anncaliia based on ultrastructural and molecular data
    • Franzen C., Nassonova E.S., Scholmerich J., and Issi I.V. Transfer of the members of the genus Brachiola (microsporidia) to the genus Anncaliia based on ultrastructural and molecular data. J Eukaryot Microbiol 53 (2006) 26-35
    • (2006) J Eukaryot Microbiol , vol.53 , pp. 26-35
    • Franzen, C.1    Nassonova, E.S.2    Scholmerich, J.3    Issi, I.V.4
  • 18
    • 0346966118 scopus 로고    scopus 로고
    • Microsporidiosis and transplantation: a retrospective study of 23 cases
    • Rabodonirina M., Cotte L., Radenne S., Besada E., and Trepo C. Microsporidiosis and transplantation: a retrospective study of 23 cases. J Eukaryot Microbiol 50 Suppl. (2003) 583
    • (2003) J Eukaryot Microbiol , vol.50 , Issue.SUPPL , pp. 583
    • Rabodonirina, M.1    Cotte, L.2    Radenne, S.3    Besada, E.4    Trepo, C.5
  • 19
    • 0036532106 scopus 로고    scopus 로고
    • Intestinal microsporidiosis due to Enterocytozoon bieneusi in elderly human immunodeficiency virus-negative patients from Vigo, Spain
    • Lores B., Lopez-Miragaya I., Arias C., Fenoy S., Torres J., and del Aguila C. Intestinal microsporidiosis due to Enterocytozoon bieneusi in elderly human immunodeficiency virus-negative patients from Vigo, Spain. Clin Infect Dis 34 (2002) 918-921
    • (2002) Clin Infect Dis , vol.34 , pp. 918-921
    • Lores, B.1    Lopez-Miragaya, I.2    Arias, C.3    Fenoy, S.4    Torres, J.5    del Aguila, C.6
  • 20
    • 0028070972 scopus 로고
    • Microsporidial infections in immunodeficient and immunocompetent patients
    • Weber R., and Bryan R.T. Microsporidial infections in immunodeficient and immunocompetent patients. Clin Infect Dis 19 (1994) 517-521
    • (1994) Clin Infect Dis , vol.19 , pp. 517-521
    • Weber, R.1    Bryan, R.T.2
  • 21
    • 0034511746 scopus 로고    scopus 로고
    • Drug treatment of microsporidiosis
    • Costa S.F., and Weiss L.M. Drug treatment of microsporidiosis. Drug Resist Updat 3 (2000) 384-399
    • (2000) Drug Resist Updat , vol.3 , pp. 384-399
    • Costa, S.F.1    Weiss, L.M.2
  • 23
    • 33744486327 scopus 로고    scopus 로고
    • Antimicrosporidial activities of fumagillin, TNP-470, ovalicin, and ovalicin derivatives in vitro and in vivo
    • Didier P.J., Phillips J.N., Kuebler D.J., et al. Antimicrosporidial activities of fumagillin, TNP-470, ovalicin, and ovalicin derivatives in vitro and in vivo. Antimicrob Agents Chemother 50 (2006) 2146-2155
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 2146-2155
    • Didier, P.J.1    Phillips, J.N.2    Kuebler, D.J.3
  • 24
    • 0002782054 scopus 로고
    • Control of nosema disease of honeybees with fumagillin
    • Katznelson H., and Jamieson C.A. Control of nosema disease of honeybees with fumagillin. Science 115 (1952) 70-71
    • (1952) Science , vol.115 , pp. 70-71
    • Katznelson, H.1    Jamieson, C.A.2
  • 25
    • 0037142093 scopus 로고    scopus 로고
    • Fumagillin treatment of intestinal microsporidiosis
    • Molina J.M., Tourneur M., Sarfati C., et al. Fumagillin treatment of intestinal microsporidiosis. N Engl J Med 346 (2002) 1963-1969
    • (2002) N Engl J Med , vol.346 , pp. 1963-1969
    • Molina, J.M.1    Tourneur, M.2    Sarfati, C.3
  • 26
    • 0031171961 scopus 로고    scopus 로고
    • Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin
    • Griffith E.C., Su Z., Turk B.E., et al. Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin. Chem Biol 4 (1997) 461-471
    • (1997) Chem Biol , vol.4 , pp. 461-471
    • Griffith, E.C.1    Su, Z.2    Turk, B.E.3
  • 27
    • 0030924753 scopus 로고    scopus 로고
    • The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2
    • Sin N., Meng L., Wang M.Q., Wen J.J., Bornmann W.G., and Crews C.M. The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2. Proc Natl Acad Sci USA 94 (1997) 6099-6103
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6099-6103
    • Sin, N.1    Meng, L.2    Wang, M.Q.3    Wen, J.J.4    Bornmann, W.G.5    Crews, C.M.6
  • 28
    • 0032515029 scopus 로고    scopus 로고
    • Structure of human methionine aminopeptidase-2 complexed with fumagillin
    • Liu S., Widom J., Kemp C.W., Crews C.M., and Clardy J. Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science 282 (1998) 1324-1327
    • (1998) Science , vol.282 , pp. 1324-1327
    • Liu, S.1    Widom, J.2    Kemp, C.W.3    Crews, C.M.4    Clardy, J.5
  • 29
    • 0035936144 scopus 로고    scopus 로고
    • Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi
    • Katinka M.D., Duprat S., Cornillot E., et al. Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi. Nature 414 (2001) 450-453
    • (2001) Nature , vol.414 , pp. 450-453
    • Katinka, M.D.1    Duprat, S.2    Cornillot, E.3
  • 30
    • 20444444391 scopus 로고    scopus 로고
    • Investigations into microsporidian methionine aminopeptidase type 2: a therapeutic target for microsporidiosis
    • Zhang H., Huang H., Cali A., et al. Investigations into microsporidian methionine aminopeptidase type 2: a therapeutic target for microsporidiosis. Folia Parasitol (Praha) 52 (2005) 182-192
    • (2005) Folia Parasitol (Praha) , vol.52 , pp. 182-192
    • Zhang, H.1    Huang, H.2    Cali, A.3
  • 31
    • 9144236238 scopus 로고    scopus 로고
    • Methionine aminopeptidase 2 expression in microsporidia
    • Didier E.S., Martin A.D., Stovall M.E., et al. Methionine aminopeptidase 2 expression in microsporidia. J Eukaryot Microbiol 50 Suppl. (2003) 569-571
    • (2003) J Eukaryot Microbiol , vol.50 , Issue.SUPPL , pp. 569-571
    • Didier, E.S.1    Martin, A.D.2    Stovall, M.E.3
  • 32
    • 0031661585 scopus 로고    scopus 로고
    • Synthetic analogues of TNP-470 and ovalicin reveal a common molecular basis for inhibition of angiogenesis and immunosuppression
    • Turk B.E., Su Z., and Liu J.O. Synthetic analogues of TNP-470 and ovalicin reveal a common molecular basis for inhibition of angiogenesis and immunosuppression. Bioorg Med Chem 6 (1998) 1163-1169
    • (1998) Bioorg Med Chem , vol.6 , pp. 1163-1169
    • Turk, B.E.1    Su, Z.2    Liu, J.O.3
  • 33
    • 0035807015 scopus 로고    scopus 로고
    • Steady-state kinetic characterization of substrates and metal-ion specificities of the full-length and N-terminally truncated recombinant human methionine aminopeptidases (type 2)
    • Yang G., Kirkpatrick R.B., Ho T., et al. 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
    • (2001) Biochemistry , vol.40 , pp. 10645-10654
    • Yang, G.1    Kirkpatrick, R.B.2    Ho, T.3
  • 34
    • 26444500150 scopus 로고    scopus 로고
    • Metalloproteomics: high-throughput structural and functional annotation of proteins in structural genomics
    • Shi W., Zhan C., Ignatov A., et al. Metalloproteomics: high-throughput structural and functional annotation of proteins in structural genomics. Structure 13 (2005) 1473-1486
    • (2005) Structure , vol.13 , pp. 1473-1486
    • Shi, W.1    Zhan, C.2    Ignatov, A.3
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode, Methods in Enzymology
    • Otwinowski Z., and Minor W. Processing of X-ray Diffraction Data Collected in Oscillation Mode, Methods in Enzymology. Macromol Crystallogr, part A 276 (1997) 307-326
    • (1997) Macromol Crystallogr, part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin A., and Teplyakov A. An approach to multi-copy search in molecular replacement. Acta Crystallogr D: Biol Crystallogr 56 (2000) 1622-1624
    • (2000) Acta Crystallogr D: Biol Crystallogr , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 39
    • 0030809260 scopus 로고    scopus 로고
    • wARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models
    • Perrakis A., Sixma T.K., Wilson K.S., and Lamzin V.S. wARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models. Acta Crystallogr D: Biol Crystallogr 53 (1997) 448-455
    • (1997) Acta Crystallogr D: Biol Crystallogr , vol.53 , pp. 448-455
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 40
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D: Biol Crystallogr 60 (2004) 2126-2132
    • (2004) Acta Crystallogr D: Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 41
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26 (1993) 283-291
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 42
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by Calpha geometry: phi, psi and Cbeta deviation
    • Lovell S.C., Davis I.W., Arendall III W.B., et al. Structure validation by Calpha geometry: phi, psi and Cbeta deviation. Proteins 50 (2003) 437-450
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1    Davis, I.W.2    Arendall III, W.B.3
  • 44
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet P., Robert X., and Courcelle E. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res 31 (2003) 3320-3323
    • (2003) Nucleic Acids Res , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 45
    • 27744565323 scopus 로고    scopus 로고
    • Structural basis for the functional differences between type I and type II human methionine aminopeptidases
    • Addlagatta A., Hu X., Liu J.O., and Matthews B.W. Structural basis for the functional differences between type I and type II human methionine aminopeptidases. Biochemistry 44 (2005) 14741-14749
    • (2005) Biochemistry , vol.44 , pp. 14741-14749
    • Addlagatta, A.1    Hu, X.2    Liu, J.O.3    Matthews, B.W.4
  • 46
    • 33746496094 scopus 로고    scopus 로고
    • Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase
    • Addlagatta A., and Matthews B.W. Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase. Protein Sci 15 (2006) 1842-1848
    • (2006) Protein Sci , vol.15 , pp. 1842-1848
    • Addlagatta, A.1    Matthews, B.W.2
  • 47
    • 18544383303 scopus 로고    scopus 로고
    • Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome
    • Addlagatta A., Quillin M.L., Omotoso O., Liu J.O., and Matthews B.W. Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome. Biochemistry 44 (2005) 7166-7174
    • (2005) Biochemistry , vol.44 , pp. 7166-7174
    • Addlagatta, A.1    Quillin, M.L.2    Omotoso, O.3    Liu, J.O.4    Matthews, B.W.5
  • 48
    • 0041735178 scopus 로고    scopus 로고
    • The 1.15A crystal structure of the Staphylococcus aureus methionyl-aminopeptidase and complexes with triazole based inhibitors
    • Oefner C., Douangamath A., D'Arcy A., et al. The 1.15A crystal structure of the Staphylococcus aureus methionyl-aminopeptidase and complexes with triazole based inhibitors. J Mol Biol 332 (2003) 13-21
    • (2003) J Mol Biol , vol.332 , pp. 13-21
    • Oefner, C.1    Douangamath, A.2    D'Arcy, A.3
  • 49
    • 0027273988 scopus 로고
    • Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme
    • Roderick S.L., and Matthews B.W. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Biochemistry 32 (1993) 3907-3912
    • (1993) Biochemistry , vol.32 , pp. 3907-3912
    • Roderick, S.L.1    Matthews, B.W.2
  • 50
    • 3042724734 scopus 로고    scopus 로고
    • Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 A resolution
    • Spraggon G., Schwarzenbacher R., Kreusch A., et al. Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 A resolution. Proteins 56 (2004) 396-400
    • (2004) Proteins , vol.56 , pp. 396-400
    • Spraggon, G.1    Schwarzenbacher, R.2    Kreusch, A.3
  • 51
    • 0032553557 scopus 로고    scopus 로고
    • Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus
    • Tahirov T.H., Oki H., Tsukihara T., et al. Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus. J Mol Biol 284 (1998) 101-124
    • (1998) J Mol Biol , vol.284 , pp. 101-124
    • Tahirov, T.H.1    Oki, H.2    Tsukihara, T.3
  • 52
    • 0032127904 scopus 로고    scopus 로고
    • N-terminal processing: the methionine aminopeptidase and N alpha-acetyl transferase families
    • Bradshaw R.A., Brickey W.W., and Walker K.W. N-terminal processing: the methionine aminopeptidase and N alpha-acetyl transferase families. Trends Biochem Sci 23 (1998) 263-267
    • (1998) Trends Biochem Sci , vol.23 , pp. 263-267
    • Bradshaw, R.A.1    Brickey, W.W.2    Walker, K.W.3
  • 53
    • 0034615568 scopus 로고    scopus 로고
    • Structure and function of the methionine aminopeptidases
    • Lowther W.T., and Matthews B.W. Structure and function of the methionine aminopeptidases. Biochim Biophys Acta 1477 (2000) 157-167
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 157-167
    • Lowther, W.T.1    Matthews, B.W.2
  • 54
    • 0036235240 scopus 로고    scopus 로고
    • Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo
    • Vetro J.A., and Chang Y.H. Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo. J Cell Biochem 85 (2002) 678-688
    • (2002) J Cell Biochem , vol.85 , pp. 678-688
    • Vetro, J.A.1    Chang, Y.H.2
  • 55
    • 0028819132 scopus 로고
    • Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth
    • Zuo S., Guo Q., Ling C., and Chang Y.H. Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth. Mol Gen Genet 246 (1995) 247-253
    • (1995) Mol Gen Genet , vol.246 , pp. 247-253
    • Zuo, S.1    Guo, Q.2    Ling, C.3    Chang, Y.H.4
  • 56
    • 0038333336 scopus 로고    scopus 로고
    • Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese
    • Wang J., Sheppard G.S., Lou P., et al. Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese. Biochemistry 42 (2003) 5035-5042
    • (2003) Biochemistry , vol.42 , pp. 5035-5042
    • Wang, J.1    Sheppard, G.S.2    Lou, P.3
  • 57
    • 0034603712 scopus 로고    scopus 로고
    • Divalent metal binding properties of the methionyl aminopeptidase from Escherichia coli
    • D'Souza V.M., Bennett B., Copik A.J., and Holz R.C. Divalent metal binding properties of the methionyl aminopeptidase from Escherichia coli. Biochemistry 39 (2000) 3817-3826
    • (2000) Biochemistry , vol.39 , pp. 3817-3826
    • D'Souza, V.M.1    Bennett, B.2    Copik, A.J.3    Holz, R.C.4
  • 58
    • 0033600583 scopus 로고    scopus 로고
    • The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme
    • D'Souza V.M., and Holz R.C. The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme. Biochemistry 38 (1999) 11079-11085
    • (1999) Biochemistry , vol.38 , pp. 11079-11085
    • D'Souza, V.M.1    Holz, R.C.2
  • 59
    • 0037062555 scopus 로고    scopus 로고
    • Overexpression and divalent metal binding properties of the methionyl aminopeptidase from Pyrococcus furiosus
    • Meng L., Ruebush S., D'Souza V.M., Copik A.J., Tsunasawa S., and Holz R.C. Overexpression and divalent metal binding properties of the methionyl aminopeptidase from Pyrococcus furiosus. Biochemistry 41 (2002) 7199-7208
    • (2002) Biochemistry , vol.41 , pp. 7199-7208
    • Meng, L.1    Ruebush, S.2    D'Souza, V.M.3    Copik, A.J.4    Tsunasawa, S.5    Holz, R.C.6
  • 60
    • 0031703555 scopus 로고    scopus 로고
    • 2+ as a cofactor: a case of mistaken identity?
    • 2+ as a cofactor: a case of mistaken identity?. Protein Sci 7 (1998) 2684-2687
    • (1998) Protein Sci , vol.7 , pp. 2684-2687
    • Walker, K.W.1    Bradshaw, R.A.2
  • 61
    • 13044300888 scopus 로고    scopus 로고
    • Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2
    • Griffith E.C., Su Z., Niwayama S., Ramsay C.A., Chang Y.H., and Liu J.O. Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2. Proc Natl Acad Sci USA 95 (1998) 15183-15188
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15183-15188
    • Griffith, E.C.1    Su, Z.2    Niwayama, S.3    Ramsay, C.A.4    Chang, Y.H.5    Liu, J.O.6
  • 62
    • 2442686862 scopus 로고    scopus 로고
    • Mutations at the S1 sites of methionine aminopeptidases from Escherichia coli and Homo sapiens reveal the residues critical for substrate specificity
    • Li J.Y., Cui Y.M., Chen L.L., et al. Mutations at the S1 sites of methionine aminopeptidases from Escherichia coli and Homo sapiens reveal the residues critical for substrate specificity. J Biol Chem 279 (2004) 21128-21134
    • (2004) J Biol Chem , vol.279 , pp. 21128-21134
    • Li, J.Y.1    Cui, Y.M.2    Chen, L.L.3
  • 63
    • 0033564306 scopus 로고    scopus 로고
    • Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis
    • Lowther W.T., Orville A.M., Madden D.T., Lim S., Rich D.H., and Matthews B.W. 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
    • (1999) Biochemistry , vol.38 , pp. 7678-7688
    • Lowther, W.T.1    Orville, A.M.2    Madden, D.T.3    Lim, S.4    Rich, D.H.5    Matthews, B.W.6
  • 64
    • 0033539594 scopus 로고    scopus 로고
    • Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues
    • Lowther W.T., Zhang Y., Sampson P.B., Honek J.F., and Matthews B.W. Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues. Biochemistry 38 (1999) 14810-14819
    • (1999) Biochemistry , vol.38 , pp. 14810-14819
    • Lowther, W.T.1    Zhang, Y.2    Sampson, P.B.3    Honek, J.F.4    Matthews, B.W.5
  • 65
    • 0032514659 scopus 로고    scopus 로고
    • The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase
    • Lowther W.T., McMillen D.A., Orville A.M., and Matthews B.W. 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
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12153-12157
    • Lowther, W.T.1    McMillen, D.A.2    Orville, A.M.3    Matthews, B.W.4
  • 66
    • 22244484427 scopus 로고    scopus 로고
    • Fumagillin class inhibitors of methionine aminopeptidase-2
    • Bernier S.G., Westlin W.F., and Hannig G. Fumagillin class inhibitors of methionine aminopeptidase-2. Drugs Future 30 (2005) 497-508
    • (2005) Drugs Future , vol.30 , pp. 497-508
    • Bernier, S.G.1    Westlin, W.F.2    Hannig, G.3
  • 67
    • 1542274566 scopus 로고    scopus 로고
    • A single amino acid residue defines the difference in ovalicin sensitivity between type I and II methionine aminopeptidases
    • Brdlik C.M., and Crews C.M. A single amino acid residue defines the difference in ovalicin sensitivity between type I and II methionine aminopeptidases. J Biol Chem 279 (2004) 9475-9480
    • (2004) J Biol Chem , vol.279 , pp. 9475-9480
    • Brdlik, C.M.1    Crews, C.M.2
  • 68
    • 59249083056 scopus 로고    scopus 로고
    • Genomic survey of the non-cultivatable opportunistic human pathogen, Enterocytozoon bieneusi
    • Akiyoshi D.E., Morrison H.G., Lei S., et al. Genomic survey of the non-cultivatable opportunistic human pathogen, Enterocytozoon bieneusi. PLoS Pathog 5 1 (2009) e1000261
    • (2009) PLoS Pathog , vol.5 , Issue.1
    • Akiyoshi, D.E.1    Morrison, H.G.2    Lei, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.