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Volumn 51, Issue 6, 2012, Pages 1199-1212

Probing the donor and acceptor substrate specificity of the γ-glutamyl transpeptidase

Author keywords

[No Author keywords available]

Indexed keywords

ACCEPTOR SITES; BACILLUS ANTHRACIS; BINDING SPECIFICITIES; BURKHOLDERIA; COMPUTATIONAL APPROACH; DONOR AND ACCEPTOR; DONOR SUBSTRATES; DRUG DESIGN; FRANCISELLA TULARENSIS; GLUTATHIONE METABOLISM; HELICOBACTER PYLORI; KINETIC ANALYSIS; L-AMINO ACIDS; MD SIMULATION; PROTEIN-LIGAND INTERACTIONS; SITE DIRECTED MUTAGENESIS; STEREOSPECIFICITY; STRUCTURAL BASIS; SUBSTRATE BINDING; SUBSTRATE SPECIFICITY; YERSINIA PESTIS;

EID: 84863171498     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200987b     Document Type: Article
Times cited : (44)

References (52)
  • 1
    • 0019888435 scopus 로고
    • γ-Glutamyl transpeptidase: Catalytic, structural and functional aspects
    • Tate, S. S. and Meister, A. (1981) γ-Glutamyl transpeptidase: Catalytic, structural and functional aspects Mol. Cell. Biochem. 39, 357-368
    • (1981) Mol. Cell. Biochem. , vol.39 , pp. 357-368
    • Tate, S.S.1    Meister, A.2
  • 2
    • 0031627519 scopus 로고    scopus 로고
    • γ-Glutamyl transpeptidase: Catalytic mechanism and gene expression
    • Taniguchi, N. and Ikeda, Y. (1998) γ-Glutamyl transpeptidase: Catalytic mechanism and gene expression Adv. Enzymol. Relat. Areas Mol. Biol. 72, 239-278
    • (1998) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.72 , pp. 239-278
    • Taniguchi, N.1    Ikeda, Y.2
  • 3
    • 22644436621 scopus 로고    scopus 로고
    • Bacillus anthracis CapD, belonging to the γ-glutamyltranspeptidase family, is required for the covalent anchoring of capsule to peptidoglycan
    • DOI 10.1111/j.1365-2958.2005.04718.x
    • Candela, T. and Fouet, A. (2005) Bacillus anthracis CapD, belonging to the γ-glutamyltranspeptidase family, is required for the covalent anchoring of capsule to peptidoglycan Mol. Microbiol. 57, 717-726 (Pubitemid 41025954)
    • (2005) Molecular Microbiology , vol.57 , Issue.3 , pp. 717-726
    • Candela, T.1    Fouet, A.2
  • 4
    • 0028817509 scopus 로고
    • Expression of γ-glutamyl transpeptidase provides tumor cells with a selective growth advantage at physiologic concentrations of cyst(e)ine
    • Hanigan, M. H. (1995) Expression of γ-glutamyl transpeptidase provides tumor cells with a selective growth advantage at physiologic concentrations of cyst(e)ine Carcinogenesis 16, 181-185
    • (1995) Carcinogenesis , vol.16 , pp. 181-185
    • Hanigan, M.H.1
  • 5
    • 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
  • 7
    • 0032982703 scopus 로고    scopus 로고
    • Essential role of Helicobacter pylori γ-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 γ-glutamyltranspeptidase for the colonization of the gastric mucosa of mice Mol. Microbiol. 31, 1359-1372 (Pubitemid 29110095)
    • (1999) Molecular Microbiology , vol.31 , Issue.5 , pp. 1359-1372
    • Chevalier, C.1    Thiberge, J.-M.2    Ferrero, R.L.3    Labigne, A.4
  • 11
    • 59249084463 scopus 로고    scopus 로고
    • Glutathione provides a source of cysteine essential for intracellular multiplication of Francisella tularensis
    • Alkhuder, K., Meibom, K. L., Dubail, I., Dupuis, M., and Charbit, A. (2009) Glutathione provides a source of cysteine essential for intracellular multiplication of Francisella tularensis PLoS Pathog. 5, e1000284
    • (2009) PLoS Pathog. , vol.5 , pp. 1000284
    • Alkhuder, K.1    Meibom, K.L.2    Dubail, I.3    Dupuis, M.4    Charbit, A.5
  • 12
    • 0014670232 scopus 로고
    • Mechanism of action of guinea pig liver transglutaminase. VI. Order of substrate addition
    • Folk, J. E. (1969) Mechanism of action of guinea pig liver transglutaminase. VI. Order of substrate addition J. Biol. Chem. 244, 3707-3713
    • (1969) J. Biol. Chem. , vol.244 , pp. 3707-3713
    • Folk, J.E.1
  • 13
    • 0022272471 scopus 로고
    • γ-Glutamyl transpeptidase: Kinetics and mechanism
    • Allison, R. D. (1985) γ-Glutamyl transpeptidase: Kinetics and mechanism Methods Enzymol. 113, 419-437
    • (1985) Methods Enzymol. , vol.113 , pp. 419-437
    • Allison, R.D.1
  • 14
    • 0141483289 scopus 로고    scopus 로고
    • Kinetic studies of rat kidney γ-glutamyltranspeptidase deacylation reveal a general base-catalyzed mechanism
    • DOI 10.1021/bi035064b
    • Castonguay, R., Lherbet, C., and Keillor, J. W. (2003) Kinetic studies of rat kidney γ-glutamyltranspeptidase deacylation reveal a general base-catalyzed mechanism Biochemistry 42, 11504-11513 (Pubitemid 37205745)
    • (2003) Biochemistry , vol.42 , Issue.39 , pp. 11504-11513
    • Castonguay, R.1    Lherbet, C.2    Keillor, J.W.3
  • 16
    • 35648962831 scopus 로고    scopus 로고
    • Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human γ-glutamyltranspeptidase
    • DOI 10.1021/bi700956c
    • 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 γ-glutamyltranspeptidase Biochemistry 46, 12253-12262 (Pubitemid 350022380)
    • (2007) Biochemistry , vol.46 , Issue.43 , 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
  • 17
    • 0035940466 scopus 로고    scopus 로고
    • Nonlinear free energy relationship in the general-acid-catalyzed acylation of rat kidney γ-glutamyl transpeptidase by a series of γ-glutamyl anilide substrate analogues
    • DOI 10.1021/bi011234d
    • Menard, A., Castonguay, R., Lherbet, C., Rivard, C., Roupioz, Y., and Keillor, J. W. (2001) Nonlinear free energy relationship in the general-acid-catalyzed acylation of rat kidney γ-glutamyl transpeptidase by a series of γ-glutamyl anilide substrate analogues Biochemistry 40, 12678-12685 (Pubitemid 32979720)
    • (2001) Biochemistry , vol.40 , Issue.42 , pp. 12678-12685
    • Menardnard, A.1    Castonguay, R.2    Lherbet, C.3    Rivard, C.4    Roupioz, Y.5    Keillor, J.W.6
  • 18
    • 33746047636 scopus 로고    scopus 로고
    • γ-(Monophenyl)phosphono glutamate analogues as mechanism-based inhibitors of γ-glutamyl transpeptidase
    • DOI 10.1016/j.bmc.2006.05.008, PII S0968089606003592
    • Han, L., Hiratake, J., Tachi, N., Suzuki, H., Kumagai, H., and Sakata, K. (2006) γ-(Monophenyl)phosphono glutamate analogues as mechanism-based inhibitors of γ-glutamyl transpeptidase Bioorg. Med. Chem. 14, 6043-6054 (Pubitemid 44080576)
    • (2006) Bioorganic and Medicinal Chemistry , vol.14 , Issue.17 , pp. 6043-6054
    • Han, L.1    Hiratake, J.2    Tachi, N.3    Suzuki, H.4    Kumagai, H.5    Sakata, K.6
  • 19
    • 0022891712 scopus 로고
    • γ-Glutamyltranspeptidase from Escherichia coli K-12: Purification and properties
    • Suzuki, H., Kumagai, H., and Tochikura, T. (1986) γ- Glutamyltranspeptidase from Escherichia coli K-12: Purification and properties J. Bacteriol. 168, 1325-1331 (Pubitemid 17226822)
    • (1986) Journal of Bacteriology , vol.168 , Issue.3 , pp. 1325-1331
    • Suzuki, H.1    Kumagai, H.2    Tochikura, T.3
  • 20
    • 33646244528 scopus 로고    scopus 로고
    • Crystal structures of γ-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 γ-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
  • 21
    • 33846965940 scopus 로고    scopus 로고
    • Autoprocessing of Helicobacter pylori γ-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad
    • DOI 10.1074/jbc.M607694200
    • Boanca, G., Sand, A., Okada, T., Suzuki, H., Kumagai, H., Fukuyama, K., and Barycki, J. J. (2007) Autoprocessing of Helicobacter pylori γ-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad J. Biol. Chem. 282, 534-541 (Pubitemid 47086261)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.1 , 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
  • 22
    • 36248940234 scopus 로고    scopus 로고
    • Characterization of Helicobacter pylori γ-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis
    • DOI 10.1021/bi701599e
    • Morrow, A. L., Williams, K., Sand, A., Boanca, G., and Barycki, J. J. (2007) Characterization of Helicobacter pylori γ-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis Biochemistry 46, 13407-13414 (Pubitemid 350136379)
    • (2007) Biochemistry , vol.46 , Issue.46 , pp. 13407-13414
    • Morrow, A.L.1    Williams, K.2    Sand, A.3    Boanca, G.4    Barycki, J.J.5
  • 23
    • 64849086541 scopus 로고    scopus 로고
    • Crystal structure of acivicin-inhibited γ-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis
    • Williams, K., Cullati, S., Sand, A., Biterova, E. I., and Barycki, J. J. (2009) Crystal structure of acivicin-inhibited γ-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis Biochemistry 48, 2459-2467
    • (2009) Biochemistry , vol.48 , pp. 2459-2467
    • Williams, K.1    Cullati, S.2    Sand, A.3    Biterova, E.I.4    Barycki, J.J.5
  • 24
    • 44849096813 scopus 로고    scopus 로고
    • Crystal Structures of Escherichia coli γ-Glutamyltranspeptidase in Complex with Azaserine and Acivicin: Novel Mechanistic Implication for Inhibition by Glutamine Antagonists
    • DOI 10.1016/j.jmb.2008.05.007, PII S0022283608005603
    • Wada, K., Hiratake, J., Irie, M., Okada, T., Yamada, C., Kumagai, H., Suzuki, H., and Fukuyama, K. (2008) Crystal structures of Escherichia coli γ-glutamyltranspeptidase in complex with azaserine and acivicin: Novel mechanistic implication for inhibition by glutamine antagonists J. Mol. Biol. 380, 361-372 (Pubitemid 351799764)
    • (2008) Journal of Molecular Biology , vol.380 , Issue.2 , 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
  • 26
    • 0017666965 scopus 로고
    • Interrelationships between the binding sites for amino acids, dipeptides, and γ-glutamyl donors in γ-glutamyl transpeptidase
    • Thompson, G. A. and Meister, A. (1977) Interrelationships between the binding sites for amino acids, dipeptides, and γ-glutamyl donors in γ-glutamyl transpeptidase J. Biol. Chem. 252, 6792-6798 (Pubitemid 8200439)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.19 , pp. 6792-6798
    • Thompson, G.A.1    Meister, A.2
  • 27
    • 0242573478 scopus 로고    scopus 로고
    • Use of Bacterial γ-Glutamyltranspeptidase for Enzymatic Synthesis of γ-D-Glutamyl Compounds
    • DOI 10.1128/AEM.69.11.6399-6404.2003
    • Suzuki, H., Izuka, S., Minami, H., Miyakawa, N., Ishihara, S., and Kumagai, H. (2003) Use of bacterial γ-glutamyltranspeptidase for enzymatic synthesis of γ- d -glutamyl compounds Appl. Environ. Microbiol. 69, 6399-6404 (Pubitemid 37420169)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.11 , pp. 6399-6404
    • Suzuki, H.1    Izuka, S.2    Minami, H.3    Miyakawa, N.4    Ishihara, S.5    Kumagai, H.6
  • 28
    • 0028926374 scopus 로고
    • Expression of an active glycosylated human γ-glutamyl transpeptidase mutant that lacks a membrane anchor domain
    • Ikeda, Y., Fujii, J., Taniguchi, N., and Meister, A. (1995) Expression of an active glycosylated human γ-glutamyl transpeptidase mutant that lacks a membrane anchor domain Proc. Natl. Acad. Sci. U.S.A. 92, 126-130
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 126-130
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3    Meister, A.4
  • 29
    • 0029082677 scopus 로고
    • Involvement of Ser-451 and Ser-452 in the catalysis of human γ-glutamyl transpeptidase
    • Ikeda, Y., Fujii, J., Anderson, M. E., Taniguchi, N., and Meister, A. (1995) Involvement of Ser-451 and Ser-452 in the catalysis of human γ-glutamyl transpeptidase J. Biol. Chem. 270, 22223-22228
    • (1995) J. Biol. Chem. , vol.270 , pp. 22223-22228
    • Ikeda, Y.1    Fujii, J.2    Anderson, M.E.3    Taniguchi, N.4    Meister, A.5
  • 30
    • 33745818526 scopus 로고    scopus 로고
    • Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori γ-glutamyltranspeptidase
    • DOI 10.1074/jbc.M603381200
    • Boanca, G., Sand, A., and Barycki, J. J. (2006) Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori γ- glutamyltranspeptidase J. Biol. Chem. 281, 19029-19037 (Pubitemid 44035406)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.28 , pp. 19029-19037
    • Boanca, G.1    Sand, A.2    Barycki, J.J.3
  • 31
    • 0035969949 scopus 로고    scopus 로고
    • Mechanism for acivicin inactivation of triad glutamine amidotransferases
    • DOI 10.1021/bi0014047
    • Chittur, S. V., Klem, T. J., Shafer, C. M., and Davisson, V. J. (2001) Mechanism for acivicin inactivation of triad glutamine amidotransferases Biochemistry 40, 876-887 (Pubitemid 32108579)
    • (2001) Biochemistry , vol.40 , Issue.4 , pp. 876-887
    • Chittur, S.V.1    Klem, T.J.2    Shafer, C.M.3    Jo Davisson, V.4
  • 32
    • 0035862175 scopus 로고    scopus 로고
    • Development and evaluation of a boronate inhibitor of γ-glutamyl transpeptidase
    • DOI 10.1006/abbi.2000.2169
    • London, R. E. and Gabel, S. A. (2001) Development and evaluation of a boronate inhibitor of γ-glutamyl transpeptidase Arch. Biochem. Biophys. 385, 250-258 (Pubitemid 32989281)
    • (2001) Archives of Biochemistry and Biophysics , vol.385 , Issue.2 , pp. 250-258
    • London, R.E.1    Gabel, S.A.2
  • 33
    • 33846845012 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of γ-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of γ-glutamyl transpeptidase
    • DOI 10.1021/bi061890j
    • Han, L., Hiratake, J., Kamiyama, A., and Sakata, K. (2007) Design, synthesis, and evaluation of γ-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of γ-glutamyl transpeptidase Biochemistry 46, 1432-1447 (Pubitemid 46208491)
    • (2007) Biochemistry , vol.46 , Issue.5 , pp. 1432-1447
    • Han, L.1    Hiratake, J.2    Kamiyama, A.3    Sakata, K.4
  • 34
    • 66149155033 scopus 로고    scopus 로고
    • A novel, species-specific class of uncompetitive inhibitors of γ-glutamyl transpeptidase
    • King, J. B., West, M. B., Cook, P. F., and Hanigan, M. H. (2009) A novel, species-specific class of uncompetitive inhibitors of γ-glutamyl transpeptidase J. Biol. Chem. 284, 9059-9065
    • (2009) J. Biol. Chem. , vol.284 , pp. 9059-9065
    • King, J.B.1    West, M.B.2    Cook, P.F.3    Hanigan, M.H.4
  • 35
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., and von, H. G. (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites Protein Eng. 10, 1-6
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von, H.G.4
  • 36
    • 7444261494 scopus 로고    scopus 로고
    • Anthrax capsule vaccine protects against experimental infection
    • DOI 10.1016/j.vaccine.2004.05.029, PII S0264410X04004402
    • Chabot, D. J., Scorpio, A., Tobery, S. A., Little, S. F., Norris, S. L., and Friedlander, A. M. (2004) Anthrax capsule vaccine protects against experimental infection Vaccine 23, 43-47 (Pubitemid 39446358)
    • (2004) Vaccine , vol.23 , Issue.1 , pp. 43-47
    • Chabot, D.J.1    Scorpio, A.2    Tobery, S.A.3    Little, S.F.4    Norris, S.L.5    Friedlander, A.M.6
  • 37
    • 30144443591 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase substrate specificity and catalytic mechanism
    • DOI 10.1016/S0076-6879(05)01027-X, PII S007668790501027X, 27, Gluthione Transferases and Gamma-Glutamyl Transpeptidases
    • Keillor, J. W., Castonguay, R., and Lherbet, C. (2005) γ-Glutamyl transpeptidase substrate specificity and catalytic mechanism Methods Enzymol. 401, 449-467 (Pubitemid 43052408)
    • (2005) Methods in Enzymology , vol.401 , pp. 449-467
    • Keillor, J.W.1    Castonguay, R.2    Lherbet, C.3
  • 38
    • 0012963984 scopus 로고
    • Interconversion of leukotrienes catalyzed by purified γ-glutamyl transpeptidase: Concomitant formation of leukotriene D4 and γ-glutamyl amino acids
    • DOI 10.1073/pnas.79.4.1088
    • Anderson, M. E., Allison, R. D., and Meister, A. (1982) Interconversion of leukotrienes catalyzed by purified γ-glutamyl transpeptidase: Concomitant formation of leukotriene D4 and γ-glutamyl amino acids Proc. Natl. Acad. Sci. U.S.A. 79, 1088-1091 (Pubitemid 12114070)
    • (1982) Proceedings of the National Academy of Sciences of the United States of America , vol.79 , Issue.4 , pp. 1088-1091
    • Anderson, M.E.1    Allison, R.D.2    Meister, A.3
  • 39
  • 40
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • DOI 10.1002/prot.340170404
    • Sippl, M. J. (1993) Recognition of errors in three-dimensional structures of proteins Proteins 17, 355-362 (Pubitemid 23358545)
    • (1993) Proteins: Structure, Function and Genetics , vol.17 , Issue.4 , pp. 355-362
    • Sippl, M.J.1
  • 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. (1993) Procheck: A Program to Check the Stereochemical Quality of Protein Structures J. Appl. Crystallogr. 26, 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
  • 43
    • 52249109585 scopus 로고    scopus 로고
    • DOVIS 2.0: An efficient and easy to use parallel virtual screening tool based on AutoDock 4.0
    • Jiang, X., Kumar, K., Hu, X., Wallqvist, A., and Reifman, J. (2008) DOVIS 2.0: An efficient and easy to use parallel virtual screening tool based on AutoDock 4.0 Chem. Cent. J. 2, 18
    • (2008) Chem. Cent. J. , vol.2 , pp. 18
    • Jiang, X.1    Kumar, K.2    Hu, X.3    Wallqvist, A.4    Reifman, J.5
  • 44
    • 20644449471 scopus 로고    scopus 로고
    • Modification of the generalized Born model suitable for macromolecules
    • Onufriev, A., Bashford, D., and Case, D. A. (2000) Modification of the generalized Born model suitable for macromolecules J. Phys. Chem. B 104, 3712-3720
    • (2000) J. Phys. Chem. B , vol.104 , pp. 3712-3720
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 45
    • 33847090263 scopus 로고
    • Directional Preferences of Nonbonded Atomic Contacts with Divalent Sulfur. 1. Electrophiles and Nucleophiles
    • Rosenfield, R. E., Parthasarathy, R., and Dunitz, J. D. (1977) Directional Preferences of Nonbonded Atomic Contacts with Divalent Sulfur. 1. Electrophiles and Nucleophiles J. Am. Chem. Soc. 99, 4860-4862
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 4860-4862
    • Rosenfield, R.E.1    Parthasarathy, R.2    Dunitz, J.D.3
  • 47
    • 34249823367 scopus 로고    scopus 로고
    • a of the bound dihydrofolate
    • DOI 10.1110/ps.062724307
    • Khavrutskii, I. V., Price, D. J., Lee, J., and Brooks, C. L., III (2007) Conformational change of the methionine 20 loop of Escherichia coli dihydrofolate reductase modulates pKa of the bound dihydrofolate Protein Sci. 16, 1087-1100 (Pubitemid 46849218)
    • (2007) Protein Science , vol.16 , Issue.6 , pp. 1087-1100
    • Khavrutskii, I.V.1    Price, D.J.2    Lee, J.3    Brooks III, C.L.4
  • 48
    • 76149143966 scopus 로고    scopus 로고
    • Crystal structure of the halotolerant γ-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket
    • Wada, K., Irie, M., Suzuki, H., and Fukuyama, K. (2010) Crystal structure of the halotolerant γ-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket FEBS J. 277, 1000-1009
    • (2010) FEBS J. , vol.277 , pp. 1000-1009
    • Wada, K.1    Irie, M.2    Suzuki, H.3    Fukuyama, K.4
  • 49
    • 0029998145 scopus 로고    scopus 로고
    • Identification, sequence, and expression of the gene encoding γ- glutamyltranspeptidase in Bacillus subtilis
    • Xu, K. and Strauch, M. A. (1996) Identification, sequence, and expression of the gene encoding γ-glutamyltranspeptidase in Bacillus subtilis J. Bacteriol. 178, 4319-4322 (Pubitemid 26240919)
    • (1996) Journal of Bacteriology , vol.178 , Issue.14 , pp. 4319-4322
    • Xu, K.1    Strauch, M.A.2
  • 50
    • 0028977997 scopus 로고
    • Human γ-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit
    • Ikeda, Y., Fujii, J., Taniguchi, N., and Meister, A. (1995) Human γ-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit J. Biol. Chem. 270, 12471-12475
    • (1995) J. Biol. Chem. , vol.270 , pp. 12471-12475
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3    Meister, A.4
  • 51
    • 0019887846 scopus 로고
    • Evidence that transpeptidation is a significant function of γ-glutamyl transpeptidase
    • Allison, R. D. and Meister, A. (1981) Evidence that transpeptidation is a significant function of γ-glutamyl transpeptidase J. Biol. Chem. 256, 2988-2992
    • (1981) J. Biol. Chem. , vol.256 , pp. 2988-2992
    • Allison, R.D.1    Meister, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.