메뉴 건너뛰기




Volumn 119, Issue 6, 1996, Pages 1166-1170

Effects of substitutions of the conserved histidine residues in human γ-glutamyl transpeptidase

Author keywords

Histidine; glutamyl transpeptidase

Indexed keywords

ALANINE; GAMMA GLUTAMYLTRANSFERASE; HISTIDINE;

EID: 0029945142     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021363     Document Type: Article
Times cited : (16)

References (32)
  • 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
    • 0022272470 scopus 로고
    • γ-Glutamyl transpeptidase from kidney
    • Tate, S.S. and Meister, A. (1985) γ-Glutamyl transpeptidase from kidney. Methods Enzymol. 113, 400-419
    • (1985) Methods Enzymol. , vol.113 , pp. 400-419
    • Tate, S.S.1    Meister, A.2
  • 3
    • 0013853331 scopus 로고
    • The reaction of iodoacetamide with the active center of γ-glutamyl transpeptidase
    • Szewczuk, A. and Connell, G.E. (1965) The reaction of iodoacetamide with the active center of γ-glutamyl transpeptidase. Biochim. Biophys. Acta 105, 352-367
    • (1965) Biochim. Biophys. Acta , vol.105 , pp. 352-367
    • Szewczuk, A.1    Connell, G.E.2
  • 4
    • 0017614157 scopus 로고
    • Affinity labeling of rat-kidney γ-glutamyl transpeptidase
    • Inoue, M., Horiuchi, S., and Morino, Y. (1977) Affinity labeling of rat-kidney γ-glutamyl transpeptidase. Eur. J. Biochem. 73, 335-342
    • (1977) Eur. J. Biochem. , vol.73 , pp. 335-342
    • Inoue, M.1    Horiuchi, S.2    Morino, Y.3
  • 5
    • 0042033156 scopus 로고
    • Serine-borate complex as a transition state inhibitor of γ-glutamyl transpeptidase
    • Tate, S.S. and Meister, A. (1978) Serine-borate complex as a transition state inhibitor of γ-glutamyl transpeptidase. Proc. Natl. Acad. Sci. USA 75, 4806-4809
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4806-4809
    • Tate, S.S.1    Meister, A.2
  • 6
    • 0017859736 scopus 로고
    • Inactivation of γ-glutamyl transpeptidase by phenylmethanesulfonyl fluoride, a specific inactivator of serine enzymes
    • Inoue, M., Horiuchi, S., and Morino, Y. (1978) Inactivation of γ-glutamyl transpeptidase by phenylmethanesulfonyl fluoride, a specific inactivator of serine enzymes. Biochem. Biophys. Res. Commun. 82, 1183-1188
    • (1978) Biochem. Biophys. Res. Commun. , vol.82 , pp. 1183-1188
    • Inoue, M.1    Horiuchi, S.2    Morino, Y.3
  • 7
    • 0018972093 scopus 로고
    • The inhibition of γ-glutamyl transpeptidase and glutathione metabolism of isolated rat kidney cells by L-(αS,5S)-α-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid (AT-125; NSC-163501)
    • Reed, D.J., Ellis, W.W., and Meck, R.A. (1980) The inhibition of γ-glutamyl transpeptidase and glutathione metabolism of isolated rat kidney cells by L-(αS,5S)-α-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid (AT-125; NSC-163501). Biochem. Biophys. Res. Commun. 94, 1273-1277
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 1273-1277
    • Reed, D.J.1    Ellis, W.W.2    Meck, R.A.3
  • 8
    • 0018981291 scopus 로고
    • Active-site amino acid residues in γ-glutamyl-transferase and the nature of the γ-glutamyl-enzyme bond
    • Elce, J.S. (1980) Active-site amino acid residues in γ-glutamyl-transferase and the nature of the γ-glutamyl-enzyme bond. Biochem. J. 185, 473-481
    • (1980) Biochem. J. , vol.185 , pp. 473-481
    • Elce, J.S.1
  • 9
    • 0028168829 scopus 로고
    • Interaction of γ-glutamyl transpeptidase with acivicin
    • Stole, E., Smith, T.K., Manning, J.M., and Meister, A. (1994) Interaction of γ-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
  • 10
    • 0025240043 scopus 로고
    • Identification of a highly reactive threonine residue at the active site of γ-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 γ-glutamyl transpeptidase. Proc. Natl. Acad. Sci. USA 87, 1706-1709
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1706-1709
    • Stole, E.1    Seddon, A.P.2    Wellner, D.3    Meister, A.4
  • 11
    • 0026079734 scopus 로고
    • Interaction of γ-glutamyl transpeptidase with glutathione involves specific arginine and lysine residues of the heavy subunit
    • Stole, E. and Meister, A. (1991) Interaction of γ-glutamyl transpeptidase with glutathione involves specific arginine and lysine residues of the heavy subunit. J. Biol. Chem. 266, 17850-17857
    • (1991) J. Biol. Chem. , vol.266 , pp. 17850-17857
    • Stole, E.1    Meister, A.2
  • 12
    • 0027467423 scopus 로고
    • Significance of Arg-107 and Glu-108 in the catalytic mechanism of human γ-glutamyl transpeptidase: Identification by site-directed mutagenesis
    • Ikeda, Y., Fujii, J., and Taniguchi, N. (1993) Significance of Arg-107 and Glu-108 in the catalytic mechanism of human γ-glutamyl transpeptidase: Identification by site-directed mutagenesis. J. Biol. Chem. 268, 3980-3985
    • (1993) J. Biol. Chem. , vol.268 , pp. 3980-3985
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3
  • 13
    • 0028951183 scopus 로고
    • Different sites of acivicin binding and inactivation of γ-glutamyl transpeptidases
    • Smith, T.K., Ikeda, Y., Fujii, J., Taniguchi, N., and Meister, A. (1995) Different sites of acivicin binding and inactivation of γ-glutamyl transpeptidases. Proc. Natl. Acad. Sci. USA 92, 2360-2364
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2360-2364
    • Smith, T.K.1    Ikeda, Y.2    Fujii, J.3    Taniguchi, N.4    Meister, A.5
  • 14
    • 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
  • 15
    • 0029046968 scopus 로고
    • Chemical modification of active site residues in γ-glutamyl transpeptidase: Aspartate 422 and cysteine 453
    • Smith, T.K. and Meister, A. (1995) Chemical modification of active site residues in γ-glutamyl transpeptidase: Aspartate 422 and cysteine 453. J. Biol. Chem. 270, 12476-12480
    • (1995) J. Biol. Chem. , vol.270 , pp. 12476-12480
    • Smith, T.K.1    Meister, A.2
  • 16
    • 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
  • 17
    • 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
  • 18
    • 0642350495 scopus 로고
    • Affinity labeling of γ-glutamyl transpeptidase and location of the γ-glutamyl binding site on the light subunit
    • Tate, S.S. and Meister, A. (1977) Affinity labeling of γ-glutamyl transpeptidase and location of the γ-glutamyl binding site on the light subunit. Proc. Natl. Acad. Sci. USA 74, 931-935
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 931-935
    • Tate, S.S.1    Meister, A.2
  • 19
    • 0018801041 scopus 로고
    • Latent proteinase activity of γ-glutamyl transpeptidase light subunit
    • Gardell, S.J. and Tate, S.S. (1979) Latent proteinase activity of γ-glutamyl transpeptidase light subunit. J. Biol. Chem. 254, 4942-4945
    • (1979) J. Biol. Chem. , vol.254 , pp. 4942-4945
    • Gardell, S.J.1    Tate, S.S.2
  • 20
    • 0014689979 scopus 로고
    • Role of a buried acid group in the mechanism of action of chymotrypsin
    • Blow, D.M., Birktoft, J.J., and Hartley, B.S. (1969) Role of a buried acid group in the mechanism of action of chymotrypsin. Nature 221, 337-340
    • (1969) Nature , vol.221 , pp. 337-340
    • Blow, D.M.1    Birktoft, J.J.2    Hartley, B.S.3
  • 21
    • 0024728303 scopus 로고
    • DNA sequence of the Escherichia coli K-12 γ-glutamyltranspeptidase gene, ggt
    • Suzuki, H., Kumagai, H., Echigo, T., and Tochikura, T. (1989) DNA sequence of the Escherichia coli K-12 γ-glutamyltranspeptidase gene, ggt. J. Bacteriol. 171, 5169-5172
    • (1989) J. Bacteriol. , vol.171 , pp. 5169-5172
    • Suzuki, H.1    Kumagai, H.2    Echigo, T.3    Tochikura, T.4
  • 23
    • 2642699794 scopus 로고
    • Rapid and eificient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A. (1985) Rapid and eificient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 24
    • 0002542580 scopus 로고
    • Expression of proteins in insect cells using baculovirus vectors
    • (Ausubel, F.M. et al., eds.) Greene Publishing Associates and Wiley-Interscience, New York
    • Piwnica-Worms, H. (1987) Expression of proteins in insect cells using baculovirus vectors in Current Protocols in Molecular Biology (Ausubel, F.M. et al., eds.) pp. 16.8.1-16.11.7, Greene Publishing Associates and Wiley-Interscience, New York
    • (1987) Current Protocols in Molecular Biology
    • Piwnica-Worms, H.1
  • 26
    • 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. USA 92, 126-130
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 126-130
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3    Meister, A.4
  • 27
    • 0000544299 scopus 로고
    • A simplified silver stain for detecting proteins in polyacrylamide gels
    • Oakley, B.R., Kirsch, D.R., and Morris, N.R. (1980) A simplified silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 105, 361-363
    • (1980) Anal. Biochem. , vol.105 , pp. 361-363
    • Oakley, B.R.1    Kirsch, D.R.2    Morris, N.R.3
  • 30
    • 0029123664 scopus 로고
    • Effects of site-directed mutations on processing and activity of γ-glutamyltranspeptidase of Escherichia coli K-12
    • Hashimoto, W., Suzuki, H., Yamamoto, K., and Kumagai, H. (1995) Effects of site-directed mutations on processing and activity of γ-glutamyltranspeptidase of Escherichia coli K-12. J. Biochem. 118, 75-80
    • (1995) J. Biochem. , vol.118 , pp. 75-80
    • Hashimoto, W.1    Suzuki, H.2    Yamamoto, K.3    Kumagai, H.4
  • 31
    • 0011877042 scopus 로고
    • The basic equations of enzyme kinetics
    • W.H. Freeman and Company, New York
    • Fersht, A. (1984) The basic equations of enzyme kinetics in Enzyme Structure and Mechanism, 2nd ed., pp. 98-120, W.H. Freeman and Company, New York
    • (1984) Enzyme Structure and Mechanism, 2nd Ed. , pp. 98-120
    • Fersht, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.