메뉴 건너뛰기




Volumn 48, Issue 11, 2009, Pages 2459-2467

Crystal structure of acivicin-inhibited γ-glutamyltranspeptidase reveals critical roles for Its C-Terminus in autoprocessing and catalysis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES; AUTOPROCESSING; BINDING POCKETS; C TERMINUS; C-TERMINAL REGIONS; CATALYTIC NUCLEOPHILES; ELECTROSTATIC INTERACTIONS; ENZYMATIC ACTIVITIES; ENZYMATIC REACTIONS; ESSENTIAL AMINO ACIDS; EXTRACELLULAR; GLUTATHIONE; HELICOBACTER PYLORUS; HYDROLASE; HYDROXYL GROUPS; MECHANISM OF ACTIONS; MUTATIONAL ANALYSIS; N TERMINALS; OXYANION HOLES; R FACTORS; SALT BRIDGES; STRUCTURE DETERMINATIONS; TIME DEPENDENTS; VIRULENCE FACTORS;

EID: 64849086541     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8014955     Document Type: Article
Times cited : (35)

References (34)
  • 1
    • 33745818526 scopus 로고    scopus 로고
    • Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori gamma- glutamyltranspeptidase
    • Boanca, G., Sand, A., and Barycki, J. J. (2006) Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori gamma- glutamyltranspeptidase. J. Biol. Chem. 281, 19029-19037.
    • (2006) J. Biol. Chem , vol.281 , pp. 19029-19037
    • Boanca, G.1    Sand, A.2    Barycki, J.J.3
  • 2
    • 0032982703 scopus 로고    scopus 로고
    • Essential role of Helicobacter pylori gamma-glutamyltranspeptidase for the colonization of the gastric mucosa of mice
    • Chevalier, C., Thiberge, J. M., Ferrero, R. L., and Labigne, A. (1999) Essential role of Helicobacter pylori gamma-glutamyltranspeptidase for the colonization of the gastric mucosa of mice. Mol. Microbiol. 31, 1359-1372.
    • (1999) Mol. Microbiol , vol.31 , pp. 1359-1372
    • Chevalier, C.1    Thiberge, J.M.2    Ferrero, R.L.3    Labigne, A.4
  • 4
    • 0037044805 scopus 로고    scopus 로고
    • Autocatalytic processing of gamma-glutamyltranspeptidase
    • Suzuki, H., and Kumagai, H. (2002) Autocatalytic processing of gamma-glutamyltranspeptidase. J. Biol. Chem. 277, 43536-43543.
    • (2002) J. Biol. Chem , vol.277 , pp. 43536-43543
    • Suzuki, H.1    Kumagai, H.2
  • 5
    • 0035017794 scopus 로고    scopus 로고
    • gamma-Glutamyltransferase is a Helicobacter pylori virulence factor but is not essential for colonization
    • McGovern, K. J., Blanchard, T. G., Gutierrez, J. A., Czinn, S. J., Krakowka, S., and Youngman, P. (2001) gamma-Glutamyltransferase is a Helicobacter pylori virulence factor but is not essential for colonization. Infect. Immun. 69, 4168-4173.
    • (2001) Infect. Immun , vol.69 , pp. 4168-4173
    • McGovern, K.J.1    Blanchard, T.G.2    Gutierrez, J.A.3    Czinn, S.J.4    Krakowka, S.5    Youngman, P.6
  • 6
    • 34247376049 scopus 로고    scopus 로고
    • Metabolism of glutamine and glutathione via gamma-glutamyltranspeptidase and glutamate transport in Helicobacter pylori: Possible significance in the pathophysiology of the organism
    • Shibayama, K., Wachino, J., Arakawa, Y., Saidijam, M., Rutherford, N. G., and Henderson, P. J. (2007) Metabolism of glutamine and glutathione via gamma-glutamyltranspeptidase and glutamate transport in Helicobacter pylori: possible significance in the pathophysiology of the organism. Mol. Microbiol. 64, 396-406.
    • (2007) Mol. Microbiol , vol.64 , pp. 396-406
    • Shibayama, K.1    Wachino, J.2    Arakawa, Y.3    Saidijam, M.4    Rutherford, N.G.5    Henderson, P.J.6
  • 7
    • 0026594392 scopus 로고
    • High resistance to cisplatin in human ovarian cancer cell lines is associated with marked increase of glutathione synthesis
    • Godwin, A. K., Meister, A., O'Dwyer, P. J., Huang, C. S., Hamilton, T. C., and Anderson, M. E. (1992) High resistance to cisplatin in human ovarian cancer cell lines is associated with marked increase of glutathione synthesis. Proc. Natl. Acad. Sci. U.S.A. 89, 3070-3074.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 3070-3074
    • Godwin, A.K.1    Meister, A.2    O'Dwyer, P.J.3    Huang, C.S.4    Hamilton, T.C.5    Anderson, M.E.6
  • 8
    • 0033065270 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase accelerates tumor growth and increases the resistance of tumors to cisplatin in vivo
    • Hanigan, M. H., Gallagher, B. C., Townsend, D. M., and Gabarra, V. (1999) Gamma-glutamyl transpeptidase accelerates tumor growth and increases the resistance of tumors to cisplatin in vivo. Carcinogenesis 20, 553-559.
    • (1999) Carcinogenesis , vol.20 , pp. 553-559
    • Hanigan, M.H.1    Gallagher, B.C.2    Townsend, D.M.3    Gabarra, V.4
  • 9
    • 0033806989 scopus 로고    scopus 로고
    • gamma- Glutamyltranspeptidase-deficient knockout mice as a model to study the relationship between glutathione status, mitochondrial function, and cellular function
    • Will, Y., Fischer, K. A., Horton, R. A., Kaetzel, R. S., Brown, M. K., Hedstrom, O., Lieberman, M. W., and Reed, D. J. (2000) gamma- Glutamyltranspeptidase-deficient knockout mice as a model to study the relationship between glutathione status, mitochondrial function, and cellular function. Hepatology 32, 740-749.
    • (2000) Hepatology , vol.32 , pp. 740-749
    • Will, Y.1    Fischer, K.A.2    Horton, R.A.3    Kaetzel, R.S.4    Brown, M.K.5    Hedstrom, O.6    Lieberman, M.W.7    Reed, D.J.8
  • 11
    • 0014876254 scopus 로고
    • The gamma-glutamyl cycle: A possible transport system for amino acids
    • Orlowski, M., and Meister, A. (1970) The gamma-glutamyl cycle: a possible transport system for amino acids. Proc. Natl. Acad. Sci. U.S.A. 67, 1248-1255.
    • (1970) Proc. Natl. Acad. Sci. U.S.A , vol.67 , pp. 1248-1255
    • Orlowski, M.1    Meister, A.2
  • 12
    • 0018168953 scopus 로고
    • Evidence that the gamma-glutamyl cycle functions in vivo using intracellular glutathione: Effects of amino acids and selective inhibition of enzymes
    • Griffith, O. W., Bridges, R. J., and Meister, A. (1978) Evidence that the gamma-glutamyl cycle functions in vivo using intracellular glutathione: effects of amino acids and selective inhibition of enzymes. Proc. Natl. Acad. Sci. U.S.A. 75, 5405-5408.
    • (1978) Proc. Natl. Acad. Sci. U.S.A , vol.75 , pp. 5405-5408
    • Griffith, O.W.1    Bridges, R.J.2    Meister, A.3
  • 13
    • 0021923753 scopus 로고
    • Use of acivicin in the determination of rate constants for turnover of rat renal gammaglutamyltranspeptidase
    • Capraro, M. A., and Hughey, R. P. (1985) Use of acivicin in the determination of rate constants for turnover of rat renal gammaglutamyltranspeptidase. J. Biol. Chem. 260, 3408-3412.
    • (1985) J. Biol. Chem , vol.260 , pp. 3408-3412
    • Capraro, M.A.1    Hughey, R.P.2
  • 14
    • 0021907385 scopus 로고
    • Effect of inhibition of gamma-glutamyltranspeptidase by AT-125 (acivicin) on glutathione and cysteine levels in rat brain and plasma
    • Hill, K. E., Von Hoff, D. D., and Burk, R. F. (1985) Effect of inhibition of gamma-glutamyltranspeptidase by AT-125 (acivicin) on glutathione and cysteine levels in rat brain and plasma. Invest. New Drugs 3, 31-34.
    • (1985) Invest. New Drugs , vol.3 , pp. 31-34
    • Hill, K.E.1    Von Hoff, D.D.2    Burk, R.F.3
  • 15
    • 0028951183 scopus 로고
    • Different sites of acivicin binding and inactivation of gamma-glutamyl transpeptidases
    • Smith, T. K., Ikeda, Y., Fujii, J., Taniguchi, N., and Meister, A. (1995) Different sites of acivicin binding and inactivation of gamma-glutamyl transpeptidases. Proc. Natl. Acad. Sci. U.S.A. 92, 2360-2364.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 2360-2364
    • Smith, T.K.1    Ikeda, Y.2    Fujii, J.3    Taniguchi, N.4    Meister, A.5
  • 16
    • 0028168829 scopus 로고
    • Interaction of gamma-glutamyl transpeptidase with acivicin
    • Stole, E., Smith, T. K., Manning, J. M., and Meister, A. (1994) Interaction of gamma-glutamyl transpeptidase with acivicin. J. Biol. Chem. 269, 21435-21439.
    • (1994) J. Biol. Chem , vol.269 , pp. 21435-21439
    • Stole, E.1    Smith, T.K.2    Manning, J.M.3    Meister, A.4
  • 17
    • 0025240043 scopus 로고
    • Identification of a highly reactive threonine residue at the active site of gamma-glutamyl transpeptidase
    • Stole, E., Seddon, A. P., Wellner, D., and Meister, A. (1990) Identification of a highly reactive threonine residue at the active site of gamma-glutamyl transpeptidase. Proc. Natl. Acad. Sci. U.S.A. 87, 1706-1709.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 1706-1709
    • Stole, E.1    Seddon, A.P.2    Wellner, D.3    Meister, A.4
  • 18
    • 33646244528 scopus 로고    scopus 로고
    • Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate
    • Okada, T., Suzuki, H., Wada, K., Kumagai, H., and Fukuyama, K. (2006) Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate. Proc. Natl. Acad. Sci. U.S.A. 103, 6471- 6476.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 6471-6476
    • Okada, T.1    Suzuki, H.2    Wada, K.3    Kumagai, H.4    Fukuyama, K.5
  • 19
    • 33846965940 scopus 로고    scopus 로고
    • Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad
    • Boanca, G., Sand, A., Okada, T., Suzuki, H., Kumagai, H., Fukuyama, K., and Barycki, J. J. (2007) Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad. J. Biol. Chem. 282, 534-541.
    • (2007) J. Biol. Chem , vol.282 , pp. 534-541
    • Boanca, G.1    Sand, A.2    Okada, T.3    Suzuki, H.4    Kumagai, H.5    Fukuyama, K.6    Barycki, J.J.7
  • 20
    • 36248940234 scopus 로고    scopus 로고
    • Characterization of Helicobacter pylori gammaglutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis
    • Morrow, A. L., Williams, K., Sand, A., Boanca, G., and Barycki, J. J. (2007) Characterization of Helicobacter pylori gammaglutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis. Biochemistry 46, 13407-13414.
    • (2007) Biochemistry , vol.46 , pp. 13407-13414
    • Morrow, A.L.1    Williams, K.2    Sand, A.3    Boanca, G.4    Barycki, J.J.5
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter, J., and Merritt, E. A. (2006) TLSMD web server for the generation of multi-group TLS models. J. Appl. Crystallogr. 39, 109-111.
    • (2006) J. Appl. Crystallogr , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 25
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N., and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr., Sect. D: Biol. Crystallogr. 57, 122-133.
    • (2001) Acta Crystallogr., Sect. D: Biol. Crystallogr , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 26
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D 50, 760-763.
    • Collaborative (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D 50, 760-763.
  • 29
    • 0021679512 scopus 로고
    • Affinity labeling of the allosteric ADP activation site of NAD-dependent isocitrate dehydrogenase by 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-diphosphate
    • Huang, Y. C., and Colman, R. F. (1984) Affinity labeling of the allosteric ADP activation site of NAD-dependent isocitrate dehydrogenase by 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-diphosphate. J. Biol. Chem. 259, 12481-12488.
    • (1984) J. Biol. Chem , vol.259 , pp. 12481-12488
    • Huang, Y.C.1    Colman, R.F.2
  • 30
    • 33846845012 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of gamma-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of gamma-glutamyl transpeptidase
    • Han, L., Hiratake, J., Kamiyama, A., and Sakata, K. (2007) Design, synthesis, and evaluation of gamma-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of gamma-glutamyl transpeptidase. Biochemistry 46, 1432-1447.
    • (2007) Biochemistry , vol.46 , pp. 1432-1447
    • Han, L.1    Hiratake, J.2    Kamiyama, A.3    Sakata, K.4
  • 31
    • 33746047636 scopus 로고    scopus 로고
    • gamma-(Monophenyl)phosphono glutamate analogues as mechanism-based inhibitors of gamma-glutamyl transpeptidase
    • Han, L., Hiratake, J., Tachi, N., Suzuki, H., Kumagai, H., and Sakata, K. (2006) gamma-(Monophenyl)phosphono glutamate analogues as mechanism-based inhibitors of gamma-glutamyl transpeptidase. Bioorg. Med. Chem. 14, 6043-6054.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 6043-6054
    • Han, L.1    Hiratake, J.2    Tachi, N.3    Suzuki, H.4    Kumagai, H.5    Sakata, K.6
  • 32
    • 35648962831 scopus 로고    scopus 로고
    • Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase
    • Castonguay, R., Halim, D., Morin, M., Furtos, A., Lherbet, C., Bonneil, E., Thibault, P., and Keillor, J. W. (2007) Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase. Biochemistry 46, 12253-12262.
    • (2007) Biochemistry , vol.46 , pp. 12253-12262
    • Castonguay, R.1    Halim, D.2    Morin, M.3    Furtos, A.4    Lherbet, C.5    Bonneil, E.6    Thibault, P.7    Keillor, J.W.8
  • 33
    • 44849096813 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: Novel mechanistic implication for inhibition by glutamine antagonists
    • Wada, K., Hiratake, J., Irie, M., Okada, T., Yamada, C., Kumagai, H., Suzuki, H., and Fukuyama, K. (2008) Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: novel mechanistic implication for inhibition by glutamine antagonists. J. Mol. Biol. 380, 361-372.
    • (2008) J. Mol. Biol , vol.380 , pp. 361-372
    • Wada, K.1    Hiratake, J.2    Irie, M.3    Okada, T.4    Yamada, C.5    Kumagai, H.6    Suzuki, H.7    Fukuyama, K.8
  • 34
    • 0037040295 scopus 로고    scopus 로고
    • Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin
    • Miles, B. W., Thoden, J. B., Holden, H. M., and Raushel, F. M. (2002) Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin. J. Biol. Chem. 277, 4368-4373.
    • (2002) J. Biol. Chem , vol.277 , pp. 4368-4373
    • Miles, B.W.1    Thoden, J.B.2    Holden, H.M.3    Raushel, F.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.