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Volumn 47, Issue 4, 2008, Pages 1228-1239

γ-glutamyl hydrolase: Kinetic characterization of isopeptide hydrolysis using fluorogenic substrates

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFOLATE DRUGS; CYSTEINE PEPTIDASE; GLUTAMYL HYDROLASE; MICHAELIS-MENTEN KINETICS; SCISSILE ISOPEPTIDE BOND;

EID: 38549084117     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701607v     Document Type: Article
Times cited : (9)

References (61)
  • 1
    • 0033622009 scopus 로고    scopus 로고
    • Glutamyl hydrolase: Pharmacological role and enzymatic characterization
    • Galivan, J., Ryan, T. J., Chave, K., Rhee, M., Yao, R., and Yin, D. (2000) Glutamyl hydrolase: pharmacological role and enzymatic characterization, Pharmacol. Ther. 85, 207-215.
    • (2000) Pharmacol. Ther , vol.85 , pp. 207-215
    • Galivan, J.1    Ryan, T.J.2    Chave, K.3    Rhee, M.4    Yao, R.5    Yin, D.6
  • 2
    • 0024511031 scopus 로고
    • Interaction of Folylpolyglutamates with Enzymes in One-Carbon Metabolism
    • Schirch, V., and Strong, W. B. (1989) Interaction of Folylpolyglutamates with Enzymes in One-Carbon Metabolism, Arch. Biochem. Biophys. 269, 371-380.
    • (1989) Arch. Biochem. Biophys , vol.269 , pp. 371-380
    • Schirch, V.1    Strong, W.B.2
  • 3
    • 0033841497 scopus 로고    scopus 로고
    • The fascinating world of folate and one-carbon metabolism
    • Cossins, E. A. (2000) The fascinating world of folate and one-carbon metabolism, Can. J. Bot. 78, 691-708.
    • (2000) Can. J. Bot , vol.78 , pp. 691-708
    • Cossins, E.A.1
  • 4
    • 0003675766 scopus 로고
    • Folates and Pterins
    • Blakley, R. L, and Benkovic, S.J, Ed, pp, John Wiley and Sons
    • McGuire, J. J., and Coward, J. K. (1984) Folates and Pterins, in Folates and Pterins (Blakley, R. L., and Benkovic, S.J., Ed.) pp 135-190, John Wiley and Sons, 1984.
    • (1984) Folates and Pterins , pp. 135-190
    • McGuire, J.J.1    Coward, J.K.2
  • 5
  • 6
    • 0242321228 scopus 로고    scopus 로고
    • Identification of single nucleotide polymorphisms in the human γ-glutamyl hydrolase gene and characterization of promoter
    • Chave, K. J., Ryan, T. J., Chmura, S. E., and Galivan, J. (2003) Identification of single nucleotide polymorphisms in the human γ-glutamyl hydrolase gene and characterization of promoter, Gene 319, 167-175.
    • (2003) Gene , vol.319 , pp. 167-175
    • Chave, K.J.1    Ryan, T.J.2    Chmura, S.E.3    Galivan, J.4
  • 7
    • 4143124340 scopus 로고    scopus 로고
    • A substrate specific functional polymorphism of human γ-glutamyl hydrolase alters catalytic activity and methotrexate polyglutamate accumulation in acute lymphoblastic leukaemia cells
    • Cheng, Q., Wu, B., Kager, L., Panetta, J. C., Zheng, J., Pui, C.-H., Relling, M., and Evans, W. E. (2004) A substrate specific functional polymorphism of human γ-glutamyl hydrolase alters catalytic activity and methotrexate polyglutamate accumulation in acute lymphoblastic leukaemia cells, Pharmacogenetics 14, 557-567.
    • (2004) Pharmacogenetics , vol.14 , pp. 557-567
    • Cheng, Q.1    Wu, B.2    Kager, L.3    Panetta, J.C.4    Zheng, J.5    Pui, C.-H.6    Relling, M.7    Evans, W.E.8
  • 8
    • 0001403860 scopus 로고    scopus 로고
    • Fluoroamino Acid Containing Analogues of Folic Acid and Methotrexate
    • Ojima, I. M, J. R, Welch, J. T, Ed, American Chemical Society, Washington
    • Tsukamoto, T., Coward, J. K., and McGuire, J. K. (1996) Fluoroamino Acid Containing Analogues of Folic Acid and Methotrexate, in Biomedical Frontiers of Fluorine Chemistry (Ojima, I. M., J. R.; Welch, J. T., Ed.) American Chemical Society, Washington.
    • (1996) Biomedical Frontiers of Fluorine Chemistry
    • Tsukamoto, T.1    Coward, J.K.2    McGuire, J.K.3
  • 9
    • 0025218665 scopus 로고
    • Synthesis of N-[N-(4-Deoxy-4-amino-10-methylpteroyl)- 4-fluoroglutamyl]-γ-glutamate, an Unusual Substrate for Folylpoly-γ-glutamate Synthetase and γ-Glutamyl Hydrolase
    • Licato, N. J., Coward, J. K., Nimec, Z., Galivan, J., Bolanowska, W. E., and McGuire, J. J. (1990) Synthesis of N-[N-(4-Deoxy-4-amino-10-methylpteroyl)- 4-fluoroglutamyl]-γ-glutamate, an Unusual Substrate for Folylpoly-γ-glutamate Synthetase and γ-Glutamyl Hydrolase, J. Med. Chem. 33, 1022-1027.
    • (1990) J. Med. Chem , vol.33 , pp. 1022-1027
    • Licato, N.J.1    Coward, J.K.2    Nimec, Z.3    Galivan, J.4    Bolanowska, W.E.5    McGuire, J.J.6
  • 10
    • 0001523313 scopus 로고
    • Stereospecific syntheses of all four stereoisomers of 4-fluoroglutamic acid
    • Hudlicky, M. (1993) Stereospecific syntheses of all four stereoisomers of 4-fluoroglutamic acid, J. Fluorine Chem. 60, 193-210.
    • (1993) J. Fluorine Chem , vol.60 , pp. 193-210
    • Hudlicky, M.1
  • 11
    • 0030052336 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of DL-4,4-difluoroglutamic acid and DL-γ,γ-difluoromethotrexate
    • Tsukamoto, T., Kitazume, T., McGuire, J. J., and Coward, J. K. (1996) Synthesis and biological evaluation of DL-4,4-difluoroglutamic acid and DL-γ,γ-difluoromethotrexate, J. Med. Chem. 39, 66-72.
    • (1996) J. Med. Chem , vol.39 , pp. 66-72
    • Tsukamoto, T.1    Kitazume, T.2    McGuire, J.J.3    Coward, J.K.4
  • 14
    • 0027164635 scopus 로고
    • The Properties of the Secreted γ-Glutamyl Hydrolases From H35-Hepatoma Cells
    • Wang, Y., Nimec, Z., Ryan, T. J., Dias, J. A., and Galivan, J. (1993) The Properties of the Secreted γ-Glutamyl Hydrolases From H35-Hepatoma Cells, Biochim. Biophys. Acta 1164, 227-235.
    • (1993) Biochim. Biophys. Acta , vol.1164 , pp. 227-235
    • Wang, Y.1    Nimec, Z.2    Ryan, T.J.3    Dias, J.A.4    Galivan, J.5
  • 15
    • 0030004570 scopus 로고    scopus 로고
    • Identification, Cloning, and Sequencing of a cDNA Coding for Rat γ-Glutamyl Hydrolase
    • Yao, R. N., Z., Ryan, T. J., and Galivan, J. (1996) Identification, Cloning, and Sequencing of a cDNA Coding for Rat γ-Glutamyl Hydrolase, J. Biol. Chem. 271, 8525-8528.
    • (1996) J. Biol. Chem , vol.271 , pp. 8525-8528
    • Yao, R.N.Z.1    Ryan, T.J.2    Galivan, J.3
  • 17
    • 0019829059 scopus 로고
    • High-Pressure Liquid Chromatography Analysis of Methotrexate Polyglutamates in Cultured Human Breast Cancer Cells
    • Jolivet, J., and Schilsky, R. L. (1981) High-Pressure Liquid Chromatography Analysis of Methotrexate Polyglutamates in Cultured Human Breast Cancer Cells, Biochem. Pharmacol. 30, 1387-1390.
    • (1981) Biochem. Pharmacol , vol.30 , pp. 1387-1390
    • Jolivet, J.1    Schilsky, R.L.2
  • 18
    • 0021984649 scopus 로고
    • Determination of folylpoly-γ-glutamate carboxypeptidase (folacin conjugase) activity using reversed-phase high-performance liquid chromatography
    • Day, B. P. F., and Gregory, J. F., III (1985) Determination of folylpoly-γ-glutamate carboxypeptidase (folacin conjugase) activity using reversed-phase high-performance liquid chromatography, J. Chromatogr. 318, 387-392.
    • (1985) J. Chromatogr , vol.318 , pp. 387-392
    • Day, B.P.F.1    Gregory III, J.F.2
  • 19
    • 0024433256 scopus 로고
    • Determination of Tissue Folate Composition by Affinity Chromatography Followed by High-Pressure Ion Pair Liquid Chromatography
    • Selhub, J. (1989) Determination of Tissue Folate Composition by Affinity Chromatography Followed by High-Pressure Ion Pair Liquid Chromatography, Anal. Biochem. 182, 84-93.
    • (1989) Anal. Biochem , vol.182 , pp. 84-93
    • Selhub, J.1
  • 20
    • 23844449939 scopus 로고    scopus 로고
    • Plant γ-Glutamyl Hydrolases and Folate Polyglutamates: Characterization, Compartmentation, and Co-Occurrence in Vacuoles
    • Orsomando, G., Diaz de la Garza, R., Green, B. J., Peng, M., Rea, P. A., Ryan, T. J., Gregory, J. F., III, and Hanson, A. D. (2005) Plant γ-Glutamyl Hydrolases and Folate Polyglutamates: Characterization, Compartmentation, and Co-Occurrence in Vacuoles, J. Biol. Chem. 280, 28877-28884.
    • (2005) J. Biol. Chem , vol.280 , pp. 28877-28884
    • Orsomando, G.1    Diaz de la Garza, R.2    Green, B.J.3    Peng, M.4    Rea, P.A.5    Ryan, T.J.6    Gregory III, J.F.7    Hanson, A.D.8
  • 21
    • 0030997685 scopus 로고    scopus 로고
    • γ-Glutamyl hydrolase from human sarcoma HT-1080 cells: Characterization and inhibition by glutamine antagonists
    • Waltham, M. C., Li, W. W., Gritsman, H., Tong, W. P., and Bertino, J. R. (1997) γ-Glutamyl hydrolase from human sarcoma HT-1080 cells: Characterization and inhibition by glutamine antagonists, Mol. Pharmacol. 51, 825-832.
    • (1997) Mol. Pharmacol , vol.51 , pp. 825-832
    • Waltham, M.C.1    Li, W.W.2    Gritsman, H.3    Tong, W.P.4    Bertino, J.R.5
  • 23
    • 0035907460 scopus 로고    scopus 로고
    • 2): An Internally Quenched Fluorogenic γ-Glutamyl Hydrolase Substrate
    • 2): An Internally Quenched Fluorogenic γ-Glutamyl Hydrolase Substrate, Bioorg. Med. Chem. Lett. 11, 1561-1564.
    • (2001) Bioorg. Med. Chem. Lett , vol.11 , pp. 1561-1564
    • Pankuch, J.J.1    Coward, J.K.2
  • 25
    • 0036459076 scopus 로고    scopus 로고
    • The Synthesis of (2S)-4,4-Difluoroglutamyl γ-Peptides Based on Garner's Aldehyde and Fluoro-Reformatsky Chemistry
    • Konas, D. W., Pankuch, J. J., and Coward, J. K. (2002) The Synthesis of (2S)-4,4-Difluoroglutamyl γ-Peptides Based on Garner's Aldehyde and Fluoro-Reformatsky Chemistry, Synthesis 17, 2616-2626.
    • (2002) Synthesis , vol.17 , pp. 2616-2626
    • Konas, D.W.1    Pankuch, J.J.2    Coward, J.K.3
  • 26
    • 0017184389 scopus 로고
    • A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
    • Bradford, M. M. (1976) A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0014056388 scopus 로고
    • α-Chymotrypsin: Enzyme Concentration and Kinetics
    • Bender, M. L., Kezdy, F. J., and Wedler, F. C. (1967) α-Chymotrypsin: Enzyme Concentration and Kinetics, J. Chem. Educ. 44, 84-88.
    • (1967) J. Chem. Educ , vol.44 , pp. 84-88
    • Bender, M.L.1    Kezdy, F.J.2    Wedler, F.C.3
  • 28
    • 0642315208 scopus 로고
    • Transient State Kinetic Analysis of Enzyme Reaction Pathways
    • Sigman, D. S, Ed, 3rd ed, pp, Academic Press, Inc, San Diego
    • Johnson, K. (1992) Transient State Kinetic Analysis of Enzyme Reaction Pathways, in Mechanisms of Catalysis (Sigman, D. S., Ed.) 3rd ed., pp 1-61, Academic Press, Inc., San Diego.
    • (1992) Mechanisms of Catalysis , pp. 1-61
    • Johnson, K.1
  • 29
    • 33947488464 scopus 로고
    • A New Synthesis of p-Methylaminobenzoyl-L- Glutamic Acid
    • Fu, S. C. J. (1965) A New Synthesis of p-Methylaminobenzoyl-L- Glutamic Acid, J. Org. Chem. 30, 1277.
    • (1965) J. Org. Chem , vol.30 , pp. 1277
    • Fu, S.C.J.1
  • 30
    • 0024782366 scopus 로고
    • Tryptophan Participation in Melanogenesis-Modification of Raper-Mason-Pawelek Scheme of Melanin Formation
    • Chakraborty, D. P., Roy, S., Chakraborty, A. K., and Rakshit, R. (1989) Tryptophan Participation in Melanogenesis-Modification of Raper-Mason-Pawelek Scheme of Melanin Formation, J. Indian Chem. Soc. 66, 699-702.
    • (1989) J. Indian Chem. Soc , vol.66 , pp. 699-702
    • Chakraborty, D.P.1    Roy, S.2    Chakraborty, A.K.3    Rakshit, R.4
  • 32
    • 0032562223 scopus 로고    scopus 로고
    • Stereochemical Course of Enzymatic Enolpyruvyl Transfer and Catalytic Conformation of the Active Site Revealed by the Crystal Structure of the Fluorinated Analogue of the Reaction Intermediate Bound to the Active Site of the C115A Mutant of MurA
    • Skarzynski, T. K., D. H., Lees, W. J., Walsh, C. T., and Duncan, K. (1998) Stereochemical Course of Enzymatic Enolpyruvyl Transfer and Catalytic Conformation of the Active Site Revealed by the Crystal Structure of the Fluorinated Analogue of the Reaction Intermediate Bound to the Active Site of the C115A Mutant of MurA, Biochemistry 37, 2572-2577.
    • (1998) Biochemistry , vol.37 , pp. 2572-2577
    • Skarzynski, T.K.D.H.1    Lees, W.J.2    Walsh, C.T.3    Duncan, K.4
  • 33
    • 38549088930 scopus 로고    scopus 로고
    • Woessner, F, Rawlings, N, and Barrett, A, Eds, 2nd ed, pp, Academic Press, New York
    • Chave, K. J., Galivan, J., and Ryan, T. J. (2003) γ-Glutamyl hydrolase, (Woessner, F., Rawlings, N., and Barrett, A., Eds.) 2nd ed., pp 1396-1399, Academic Press, New York.
    • (2003) γ-Glutamyl hydrolase , pp. 1396-1399
    • Chave, K.J.1    Galivan, J.2    Ryan, T.J.3
  • 34
    • 0036388875 scopus 로고    scopus 로고
    • The one-bead two-compound assay for solid phase screening of combinatorial libraries
    • Meldal, M. (2002) The one-bead two-compound assay for solid phase screening of combinatorial libraries, Biopolymers 66, 93-100.
    • (2002) Biopolymers , vol.66 , pp. 93-100
    • Meldal, M.1
  • 35
    • 3042737431 scopus 로고    scopus 로고
    • Recent advances in enzyme assays
    • Goddard, J. P., and Reymond, J. L. (2004) Recent advances in enzyme assays, Trends Biotechnol. 22, 363-370.
    • (2004) Trends Biotechnol , vol.22 , pp. 363-370
    • Goddard, J.P.1    Reymond, J.L.2
  • 36
    • 0034636841 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies of signal peptidase I from Escherichia coli
    • Stein, R. L., Barbosa, M. D. F. S., and Bruckner, R. (2000) Kinetic and mechanistic studies of signal peptidase I from Escherichia coli, Biochemistry 39, 7973-7983.
    • (2000) Biochemistry , vol.39 , pp. 7973-7983
    • Stein, R.L.1    Barbosa, M.D.F.S.2    Bruckner, R.3
  • 37
    • 0842346118 scopus 로고    scopus 로고
    • Development of a high-performance liquid chromatography assay and revision of kinetic parameters for the Staphlococcus aureus sortase transpeptidase SrtA
    • Kruger, R. G. D., P., and McCafferty, D. G. (2004) Development of a high-performance liquid chromatography assay and revision of kinetic parameters for the Staphlococcus aureus sortase transpeptidase SrtA, Anal. Biochem. 326, 42-48.
    • (2004) Anal. Biochem , vol.326 , pp. 42-48
    • Kruger, R.G.D.P.1    McCafferty, D.G.2
  • 38
    • 0037199423 scopus 로고    scopus 로고
    • Kinetic characterization of the peptidase activity of Escherichia coli Lon reveals the mechanistic similarities of ATP-dependent hydrolysis of peptide and protein substrates
    • Thomas-Wohler, J., and Lee, I. (2002) Kinetic characterization of the peptidase activity of Escherichia coli Lon reveals the mechanistic similarities of ATP-dependent hydrolysis of peptide and protein substrates, Biochemistry 41, 9418-9425.
    • (2002) Biochemistry , vol.41 , pp. 9418-9425
    • Thomas-Wohler, J.1    Lee, I.2
  • 39
    • 0029969542 scopus 로고    scopus 로고
    • Facile synthesis of DL-4,4-difluoroornithine, DL-4,4-difluoroglutamine, and γ-DL-4,4- difluoroglutamyl-containing peptides: Regiospecific addition of nucleophiles to N-Cbz-di-tert-butyl-DL-4,4-difluoroglutamate
    • Tsukamoto, T., and Coward, J. K. (1996) Facile synthesis of DL-4,4-difluoroornithine, DL-4,4-difluoroglutamine, and γ-DL-4,4- difluoroglutamyl-containing peptides: regiospecific addition of nucleophiles to N-Cbz-di-tert-butyl-DL-4,4-difluoroglutamate, J. Org. Chem. 61, 2497-2500.
    • (1996) J. Org. Chem , vol.61 , pp. 2497-2500
    • Tsukamoto, T.1    Coward, J.K.2
  • 40
    • 0001599898 scopus 로고
    • The reaction of p- nitrophenyl esters with chymotrypsin and insulin
    • Hartley, B. S., and Kilby, B. A. (1954) The reaction of p- nitrophenyl esters with chymotrypsin and insulin, Biochem. J. 56, 288-297.
    • (1954) Biochem. J , vol.56 , pp. 288-297
    • Hartley, B.S.1    Kilby, B.A.2
  • 41
    • 33748470343 scopus 로고    scopus 로고
    • Characterization of human γ-glutamyl hydrolase in solution demonstrates that the enzyme is a non-dissociating homodimer
    • Eisele, L. E., Chave, K. J., Lehning, A. C., and Ryan, T. J. (2006) Characterization of human γ-glutamyl hydrolase in solution demonstrates that the enzyme is a non-dissociating homodimer, Biochem. Biophys. Acta 1764, 1479-1486.
    • (2006) Biochem. Biophys. Acta , vol.1764 , pp. 1479-1486
    • Eisele, L.E.1    Chave, K.J.2    Lehning, A.C.3    Ryan, T.J.4
  • 42
    • 0037025325 scopus 로고    scopus 로고
    • Three-dimensional structure of human γ-glutamyl hydrolase: A class I glutamine amidotransferase adapted for a complex substrate
    • Li, H. M., Ryan, T. J., Chave, K. J., and Van Roey, P. (2002) Three-dimensional structure of human γ-glutamyl hydrolase: A class I glutamine amidotransferase adapted for a complex substrate, J. Biol. Chem. 277, 24522-24529.
    • (2002) J. Biol. Chem , vol.277 , pp. 24522-24529
    • Li, H.M.1    Ryan, T.J.2    Chave, K.J.3    Van Roey, P.4
  • 43
    • 0034704177 scopus 로고    scopus 로고
    • Molecular Modeling and Site-directed Mutagenesis Define the Catalytic Motif in Human γ-Glutamyl Hydrolase
    • Chave, K. J., Auger, I. E., Galivan, J., and Ryan, T. J. (2000) Molecular Modeling and Site-directed Mutagenesis Define the Catalytic Motif in Human γ-Glutamyl Hydrolase, J. Biol. Chem. 275, 40365-40370.
    • (2000) J. Biol. Chem , vol.275 , pp. 40365-40370
    • Chave, K.J.1    Auger, I.E.2    Galivan, J.3    Ryan, T.J.4
  • 45
    • 0031039519 scopus 로고    scopus 로고
    • Tubulin post-translational modifications - Enzymes and their mechanisms of action
    • MacRae, T. H. (1997) Tubulin post-translational modifications - Enzymes and their mechanisms of action, European J. Biochem. 244, 265-278.
    • (1997) European J. Biochem , vol.244 , pp. 265-278
    • MacRae, T.H.1
  • 46
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann, S., and Weber, K. (2003) Post-translational modifications regulate microtubule function, Nat. Rev. Mol. Cell Biol. 4, 938-947.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 47
    • 0032499669 scopus 로고    scopus 로고
    • Tubulin polyglutamylase: Partial purification and enzymatic properties
    • Regnard, C., Audebert, S., Desbruyeres, E., Denoulet, P., and Edde, B. (1998) Tubulin polyglutamylase: Partial purification and enzymatic properties, Biochemistry 37, 8395-8404.
    • (1998) Biochemistry , vol.37 , pp. 8395-8404
    • Regnard, C.1    Audebert, S.2    Desbruyeres, E.3    Denoulet, P.4    Edde, B.5
  • 48
    • 0037115726 scopus 로고    scopus 로고
    • Identification of CfNek, a novel member of the NIMA family of cell cycle regulators, as a polypeptide copurifying with tubulin polyglutamylation activity in Crithidia
    • Westermann, S., and Weber, K. (2002) Identification of CfNek, a novel member of the NIMA family of cell cycle regulators, as a polypeptide copurifying with tubulin polyglutamylation activity in Crithidia, J. Cell. Sci. 115, 5003-5012.
    • (2002) J. Cell. Sci , vol.115 , pp. 5003-5012
    • Westermann, S.1    Weber, K.2
  • 50
    • 30144443591 scopus 로고    scopus 로고
    • γ-glutamyl transpeptidase substrate specificity and catalytic mechanism
    • Keillor, J. W., Castonguay, R., and Lherbet, C. (2005) γ-glutamyl transpeptidase substrate specificity and catalytic mechanism, Methods Enzymol. 401, 449-467.
    • (2005) Methods Enzymol , vol.401 , pp. 449-467
    • Keillor, J.W.1    Castonguay, R.2    Lherbet, C.3
  • 52
    • 2942735409 scopus 로고    scopus 로고
    • Pre-steady-state kinetic studies of rat kidney γ-glutamyl transpeptidase confirm its ping-pong mechanism
    • Keillor, J. W., Menard, A., Castonguay, R., Lherbet, C., and Rivard, C. (2004) Pre-steady-state kinetic studies of rat kidney γ-glutamyl transpeptidase confirm its ping-pong mechanism, J. Phys. Org. Chem. 17, 529-536.
    • (2004) J. Phys. Org. Chem , vol.17 , pp. 529-536
    • Keillor, J.W.1    Menard, A.2    Castonguay, R.3    Lherbet, C.4    Rivard, C.5
  • 53
    • 0041570280 scopus 로고    scopus 로고
    • Kinetic Analysis of the Action of Tissue Transglutaminase on Peptide and Protein Substrates
    • Case, A., and Stein, R. L. (2003) Kinetic Analysis of the Action of Tissue Transglutaminase on Peptide and Protein Substrates, Biochemistry 42, 9466-9481.
    • (2003) Biochemistry , vol.42 , pp. 9466-9481
    • Case, A.1    Stein, R.L.2
  • 54
    • 1842454749 scopus 로고    scopus 로고
    • Tissue transglutaminase acylation: Proposed role of conserved active site Tyr and Trp residues revealed by molecular modeling of peptide substrate binding
    • Chica, R. A., Gagnon, P., Keillor, J. W., and Pelletier, J. N. (2004) Tissue transglutaminase acylation: Proposed role of conserved active site Tyr and Trp residues revealed by molecular modeling of peptide substrate binding, Protein Sci. 13, 979-991.
    • (2004) Protein Sci , vol.13 , pp. 979-991
    • Chica, R.A.1    Gagnon, P.2    Keillor, J.W.3    Pelletier, J.N.4
  • 55
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes
    • Dang, L. C., Melandri, F. D., and Stein, R. L. (1998) Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes, Biochemistry 37, 1868-1879.
    • (1998) Biochemistry , vol.37 , pp. 1868-1879
    • Dang, L.C.1    Melandri, F.D.2    Stein, R.L.3
  • 56
    • 33144481901 scopus 로고    scopus 로고
    • Mechanistic studies of ubiquitin C-terminal hydrolase L1
    • Case, A., and Stein, R. L. (2006) Mechanistic studies of ubiquitin C-terminal hydrolase L1, Biochemistry 45, 2443-2452.
    • (2006) Biochemistry , vol.45 , pp. 2443-2452
    • Case, A.1    Stein, R.L.2
  • 57
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson, K. D. (2000) Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome, Cell Dev. Biol. 11, 141-148.
    • (2000) Cell Dev. Biol , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 59
    • 13544266212 scopus 로고    scopus 로고
    • Involvement of individual subsites and secondary substrate binding sites in multiple attack on amylose by barley α-amylase
    • Kramhoft, B., Bak-Jensen, K. S., Mori, H., Juge, N., Nohr, J., and Svensson, B. (2005) Involvement of individual subsites and secondary substrate binding sites in multiple attack on amylose by barley α-amylase Biochemistry 44, 1824-1832.
    • (2005) Biochemistry , vol.44 , pp. 1824-1832
    • Kramhoft, B.1    Bak-Jensen, K.S.2    Mori, H.3    Juge, N.4    Nohr, J.5    Svensson, B.6
  • 60
    • 0014037680 scopus 로고
    • Environmentally Sensitive Tyrosyl Residues. Nitration with Tetranitromethane
    • Riordan, J. F., Sokolovsky, M., and Vallee, B. L. (1967) Environmentally Sensitive Tyrosyl Residues. Nitration with Tetranitromethane, Biochemistry 6, 358-361.
    • (1967) Biochemistry , vol.6 , pp. 358-361
    • Riordan, J.F.1    Sokolovsky, M.2    Vallee, B.L.3
  • 61
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the Analysis of Enzyme Kinetic Data: Application to HIV Proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the Analysis of Enzyme Kinetic Data: Application to HIV Proteinase, Anal. Biochem. 237, 260-273.
    • (1996) Anal. Biochem , vol.237 , pp. 260-273
    • Kuzmic, P.1


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