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Volumn 224, Issue 2, 2003, Pages 169-173

A mutant Bacillus subtilis γ-glutamyltranspeptidase specialized in hydrolysis activity

Author keywords

Bacillus subtilis; Glutaminase; Hydrolysis; Salt tolerant; Site directed mutagenesis; Glutamyltranspeptidase

Indexed keywords

AMINO ACID; GAMMA GLUTAMYLTRANSFERASE; GLUTAMINE; PEPTIDE;

EID: 0041707747     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00456-7     Document Type: Article
Times cited : (41)

References (20)
  • 1
    • 0019888435 scopus 로고
    • γ-Glutamyl transpeptidase: Catalytic, structural and functional aspects
    • Tate S.S., Meister A. γ-Glutamyl transpeptidase: catalytic, structural and functional aspects. Mol. Cell. Biochem. 39:1981;357-368.
    • (1981) Mol. Cell. Biochem. , vol.39 , pp. 357-368
    • Tate, S.S.1    Meister, A.2
  • 2
    • 0023686906 scopus 로고
    • Synthesis of γ-glutamyl-DOPA from L-glutamine and L-DOPA by γ-glutamyltranspeptidase from Escherichia coli K-12
    • Kumagai H., Echigo T., Suzuki H., Tochikura T. Synthesis of γ-glutamyl-DOPA from L-glutamine and L-DOPA by γ-glutamyltranspeptidase from Escherichia coli K-12. Agric. Biol. Chem. 52:1988;1741-1745.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 1741-1745
    • Kumagai, H.1    Echigo, T.2    Suzuki, H.3    Tochikura, T.4
  • 3
    • 0012795027 scopus 로고
    • Enzymatic synthesis of γ-glutamyltyrosine methyl ester from L-glutamine and L-tyrosine methyl ester with Escherichia coli K-12 γ-glutamyltranspeptidase
    • Kumagai H., Echigo T., Suzuki H., Tochikura T. Enzymatic synthesis of γ-glutamyltyrosine methyl ester from L-glutamine and L-tyrosine methyl ester with Escherichia coli K-12 γ-glutamyltranspeptidase. Agric. Biol. Chem. 53:1989;1429-1430.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 1429-1430
    • Kumagai, H.1    Echigo, T.2    Suzuki, H.3    Tochikura, T.4
  • 4
    • 84985345649 scopus 로고
    • Enzymatic synthesis of γ-glutamyl-L-histidine by γ-glutamyltranspeptidase from Escherichia coli K-12
    • Kumagai H., Echigo T., Suzuki H., Tochikura T. Enzymatic synthesis of γ-glutamyl-L-histidine by γ-glutamyltranspeptidase from Escherichia coli K-12. Lett. Appl. Microbiol. 8:1989;143-146.
    • (1989) Lett. Appl. Microbiol. , vol.8 , pp. 143-146
    • Kumagai, H.1    Echigo, T.2    Suzuki, H.3    Tochikura, T.4
  • 5
    • 0024303282 scopus 로고
    • Utilization of the γ-glutamyltranspeptidase reaction for glutathione synthesis
    • Kumagai H., Suzuki H., Shimizu M., Tochikura T. Utilization of the γ-glutamyltranspeptidase reaction for glutathione synthesis. J. Biotechnol. 9:1989;129-138.
    • (1989) J. Biotechnol. , vol.9 , pp. 129-138
    • Kumagai, H.1    Suzuki, H.2    Shimizu, M.3    Tochikura, T.4
  • 6
    • 0037116432 scopus 로고    scopus 로고
    • Improvement of the bitter taste of amino acids through the transpeptidation reaction of bacterial γ-glutamyltranspeptidase
    • Suzuki H., Kajimoto Y., Kumagai H. Improvement of the bitter taste of amino acids through the transpeptidation reaction of bacterial γ-glutamyltranspeptidase. J. Agric. Food Chem. 50:2002;313-318.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 313-318
    • Suzuki, H.1    Kajimoto, Y.2    Kumagai, H.3
  • 7
    • 0037018893 scopus 로고    scopus 로고
    • Enzymatic production of γ-L-glutamyltaurine through the transpeptidation reaction of γ-glutamyltranspeptidase from Escherichia coli K-12
    • Suzuki H., Miyakawa N., Kumagai H. Enzymatic production of γ-L-glutamyltaurine through the transpeptidation reaction of γ-glutamyltranspeptidase from Escherichia coli K-12. Enzyme Microb. Technol. 30:2002;883-888.
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 883-888
    • Suzuki, H.1    Miyakawa, N.2    Kumagai, H.3
  • 8
    • 0036843218 scopus 로고    scopus 로고
    • Enzymatic production of theanine, an 'umami' component of tea, from glutamine and ethylamine with bacterial γ-glutamyltranspeptidase
    • Suzuki H., Izuka S., Miyakawa N., Kumagai H. Enzymatic production of theanine, an 'umami' component of tea, from glutamine and ethylamine with bacterial γ-glutamyltranspeptidase. Enzyme Microb. Technol. 31:2002;884-889.
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 884-889
    • Suzuki, H.1    Izuka, S.2    Miyakawa, N.3    Kumagai, H.4
  • 9
    • 0037416735 scopus 로고    scopus 로고
    • Salt-tolerant γ-glutamyltranspeptidase from Bacillus subtilis 168 with glutaminase activity
    • Minami H., Suzuki H., Kumagai H. Salt-tolerant γ-glutamyltranspeptidase from Bacillus subtilis 168 with glutaminase activity. Enzyme Microb. Technol. 32:2003;431-438.
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 431-438
    • Minami, H.1    Suzuki, H.2    Kumagai, H.3
  • 10
    • 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., Meister A. Human γ-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. J. Biol. Chem. 270:1995;12471-12475.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12471-12475
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3    Meister, A.4
  • 11
    • 0027467423 scopus 로고
    • Significance of Arg-107 and Glu-108 in the catalytic mechanism of human γ-glutamyl transpeptidase
    • Ikeda Y., Fujii J., Taniguchi N. Significance of Arg-107 and Glu-108 in the catalytic mechanism of human γ-glutamyl transpeptidase. J. Biol. Chem. 268:1993;3980-3985.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3980-3985
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3
  • 12
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue H., Nojima H., Okayama H. High efficiency transformation of Escherichia coli with plasmids. Gene. 96:1990;23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 13
    • 0022908614 scopus 로고
    • γ-Glutamyltranspeptidase from Escherichia coli K-12: Formation and localization
    • Suzuki H., Kumagai H., Tochikura T. γ-Glutamyltranspeptidase from Escherichia coli K-12: formation and localization. J. Bacteriol. 168:1986;1332-1335.
    • (1986) J. Bacteriol. , vol.168 , pp. 1332-1335
    • Suzuki, H.1    Kumagai, H.2    Tochikura, T.3
  • 14
    • 0022891712 scopus 로고
    • γ-Glutamyltranspeptidase from Escherichia coli K-12: Purification and properties
    • Suzuki H., Kumagai H., Tochikura T. γ-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties. J. Bacteriol. 168:1986;1325-1331.
    • (1986) J. Bacteriol. , vol.168 , pp. 1325-1331
    • Suzuki, H.1    Kumagai, H.2    Tochikura, T.3
  • 16
    • 0020356610 scopus 로고
    • Inhibition by glutamate of phosphate-dependent glutaminase of rat kidney
    • Shapiro R.A., Morehouse R.F., Curthoys N.P. Inhibition by glutamate of phosphate-dependent glutaminase of rat kidney. Biochem. J. 207:1982;561-566.
    • (1982) Biochem. J. , vol.207 , pp. 561-566
    • Shapiro, R.A.1    Morehouse, R.F.2    Curthoys, N.P.3
  • 17
    • 0022416657 scopus 로고
    • Comparison of the phosphate-dependent glutaminases obtained from rat brain and kidney
    • Haser W.G., Shapiro R.A., Curthoys N.P. Comparison of the phosphate-dependent glutaminases obtained from rat brain and kidney. Biochem. J. 229:1985;399-408.
    • (1985) Biochem. J. , vol.229 , pp. 399-408
    • Haser, W.G.1    Shapiro, R.A.2    Curthoys, N.P.3
  • 18
    • 0037024085 scopus 로고    scopus 로고
    • Purification and characterisation of a glutaminase from Debaryomyces spp
    • Dura M.A., Flores M., Toldra F. Purification and characterisation of a glutaminase from Debaryomyces spp. Int. J. Food Microbiol. 76:2002;117-126.
    • (2002) Int. J. Food Microbiol. , vol.76 , pp. 117-126
    • Dura, M.A.1    Flores, M.2    Toldra, F.3
  • 19
    • 0023835701 scopus 로고
    • Molecular cloning of Escherichia coli K-12 ggt and rapid isolation of γ-glutamyltranspeptidase
    • Suzuki H., Kumagai H., Echigo T., Tochikura T. Molecular cloning of Escherichia coli K-12 ggt and rapid isolation of γ-glutamyltranspeptidase. Biochem. Biophys. Res. Commun. 150:1988;33-38.
    • (1988) Biochem. Biophys. Res. Commun. , vol.150 , pp. 33-38
    • Suzuki, H.1    Kumagai, H.2    Echigo, T.3    Tochikura, T.4
  • 20
    • 0021681129 scopus 로고
    • New shuttle vectors for Escherichia coli and Bacillus subtilis. I. Construction and characterization of plasmid pHY460 with twelve unique cloning sites
    • Ishiwa H., Tsuchida N. New shuttle vectors for Escherichia coli and Bacillus subtilis. I. Construction and characterization of plasmid pHY460 with twelve unique cloning sites. Gene. 32:1984;129-134.
    • (1984) Gene , vol.32 , pp. 129-134
    • Ishiwa, H.1    Tsuchida, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.