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Volumn 69, Issue 11, 2003, Pages 6399-6404

Use of Bacterial γ-Glutamyltranspeptidase for Enzymatic Synthesis of γ-D-Glutamyl Compounds

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOSYNTHESIS; ENVIRONMENTAL IMPACT; ENZYMES;

EID: 0242573478     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.69.11.6399-6404.2003     Document Type: Article
Times cited : (61)

References (32)
  • 1
    • 0025780937 scopus 로고
    • Excretion and rapid purification of γ-glutamyltranspeptidase from Escherichia coli K-12
    • Claudio, J. O., H. Suzuki, H. Kumagai, and T. Tochikura. 1991. Excretion and rapid purification of γ-glutamyltranspeptidase from Escherichia coli K-12. J. Ferment. Bioeng. 72:125-127.
    • (1991) J. Ferment. Bioeng. , vol.72 , pp. 125-127
    • Claudio, J.O.1    Suzuki, H.2    Kumagai, H.3    Tochikura, T.4
  • 2
    • 0020324491 scopus 로고
    • Differential activation and blockade of excitatory amino acid receptors in the mammalian and amphibian central nervous systems
    • Davies, J., R. H. Evans, A. W. Jones, D. A. Smith, and J. C. Watkins. 1982. Differential activation and blockade of excitatory amino acid receptors in the mammalian and amphibian central nervous systems. Comp. Biochem. Physiol. C. 72:211-224.
    • (1982) Comp. Biochem. Physiol. C , vol.72 , pp. 211-224
    • Davies, J.1    Evans, R.H.2    Jones, A.W.3    Smith, D.A.4    Watkins, J.C.5
  • 3
    • 0642271563 scopus 로고    scopus 로고
    • Varietal differences in the total and enantiomeric composition of theanine in tea
    • Ekborg-Ott, K. H., A. Taylor, and D. W. Armstrong. 1997. Varietal differences in the total and enantiomeric composition of theanine in tea. J. Agric. Food Chem. 45:353-363.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 353-363
    • Ekborg-Ott, K.H.1    Taylor, A.2    Armstrong, D.W.3
  • 4
    • 0002405792 scopus 로고    scopus 로고
    • Chemical composition of commercially available Japanese green tea
    • Goto, T., Y. Yoshida, I. Amano, and H. Horie. 1996. Chemical composition of commercially available Japanese green tea. Foods Food Ingredients J. Jpn. 170:46-51.
    • (1996) Foods Food Ingredients J. Jpn. , vol.170 , pp. 46-51
    • Goto, T.1    Yoshida, Y.2    Amano, I.3    Horie, H.4
  • 5
    • 0007636159 scopus 로고
    • Potential of γ-L-glutamyl-L-cystine and bis-γ -L-glutamyl-L-cystine as a cystine-containing peptide for parenteral nutrition
    • K. Takai (ed.). Elsevier, Amsterdam, The Netherlands
    • Hara, T., Y. Yokoo, and T. Furukawa. 1992. Potential of γ-L-glutamyl-L-cystine and bis-γ-L-glutamyl-L-cystine as a cystine-containing peptide for parenteral nutrition, p. 607-611. In K. Takai (ed.), Frontiers and new horizons in amino acid research. Elsevier, Amsterdam, The Netherlands.
    • (1992) Frontiers and New Horizons in Amino Acid Research , pp. 607-611
    • Hara, T.1    Yokoo, Y.2    Furukawa, T.3
  • 6
    • 0030944510 scopus 로고    scopus 로고
    • Analysis of low temperature inducible mechanism of γ -glutamyltranspeptidase of Escherichia coli K-12
    • Hashimoto, W., H. Suzuki, K. Yamamoto, and H. Kumagai. 1997. Analysis of low temperature inducible mechanism of γ-glutamyltranspeptidase of Escherichia coli K-12. Biosci. Biotechnol. Biochem. 61:34-39.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 34-39
    • Hashimoto, W.1    Suzuki, H.2    Yamamoto, K.3    Kumagai, H.4
  • 7
    • 0005848920 scopus 로고
    • Simple peptides. Part 7. The chemical conversions of C-terminal α-amino acids in peptides into unsubstituted or 2-substituted taurines via S-acetylthio- or halogeno-intermediates
    • Higashiura, K., and K. Ienaga. 1992. Simple peptides. Part 7. The chemical conversions of C-terminal α-amino acids in peptides into unsubstituted or 2-substituted taurines via S-acetylthio- or halogeno-intermediates. J. Chem. Res. 1992(S):250-251, 1992(M):1901-1921.
    • (1992) J. Chem. Res. , Issue.S , pp. 250-251
    • Higashiura, K.1    Ienaga, K.2
  • 8
    • 0242437744 scopus 로고
    • Higashiura, K., and K. Ienaga. 1992. Simple peptides. Part 7. The chemical conversions of C-terminal α-amino acids in peptides into unsubstituted or 2-substituted taurines via S-acetylthio- or halogeno-intermediates. J. Chem. Res. 1992(S):250-251, 1992(M):1901-1921.
    • (1992) J. Chem. Res. , Issue.M , pp. 1901-1921
  • 9
    • 0023407702 scopus 로고
    • Increase of catecholamines in mouse brain by systemic administration of γ-glutamyl L-3, 4-dihydroxyphenylalanine
    • Ichinose, H., A. Togari, H. Suzuki, H. Kumagai, and T. Nagatsu. 1987. Increase of catecholamines in mouse brain by systemic administration of γ-glutamyl L-3, 4-dihydroxyphenylalanine. J. Neurochem. 49:928-932.
    • (1987) J. Neurochem. , vol.49 , pp. 928-932
    • Ichinose, H.1    Togari, A.2    Suzuki, H.3    Kumagai, H.4    Nagatsu, T.5
  • 10
    • 0034604269 scopus 로고    scopus 로고
    • Identification of catalytic nucleophile of Escherichia coli γ-glutamyltranspeptidase by γ-monofluorophosphono derivative of glutamic acid: N-terminal thr-391 in small subunit is the nucleophile
    • Inoue, M., J. Hiratake, H. Suzuki, H. Kumagai, and K. Sakata. 2000. Identification of catalytic nucleophile of Escherichia coli γ -glutamyltranspeptidase by γ-monofluorophosphono derivative of glutamic acid: N-terminal thr-391 in small subunit is the nucleophile. Biochemistry 39:7764-7771.
    • (2000) Biochemistry , vol.39 , pp. 7764-7771
    • Inoue, M.1    Hiratake, J.2    Suzuki, H.3    Kumagai, H.4    Sakata, K.5
  • 11
    • 0023783312 scopus 로고
    • A comparison of the renal actions of γ-glutamyl-L-tyrosine in normal man
    • Jeffrey, R. F., T. M. MacDonald, and M. R. Lee. 1988. A comparison of the renal actions of γ-glutamyl-L-tyrosine in normal man. Clin. Sci. 74:37-40.
    • (1988) Clin. Sci. , vol.74 , pp. 37-40
    • Jeffrey, R.F.1    MacDonald, T.M.2    Lee, M.R.3
  • 12
    • 0021738761 scopus 로고
    • Structure-activity relations of dipeptide antagonists of excitatory amino acids
    • Jones, A. W., D. A. Smith, and J. C. Watkins. 1984. Structure-activity relations of dipeptide antagonists of excitatory amino acids. Neuroscience 13: 573-581.
    • (1984) Neuroscience , vol.13 , pp. 573-581
    • Jones, A.W.1    Smith, D.A.2    Watkins, J.C.3
  • 14
    • 84985345649 scopus 로고
    • Enzymatic synthesis of γ-glutamyl-L-histidine by γ-glutamyltranspeptidase from Escherichia coli K-12
    • Kumagai, H., T. Echigo, H. Suzuki, and T. Tochikura. 1989. Enzymatic synthesis of γ-glutamyl-L-histidine by γ-glutamyltranspeptidase from Escherichia coli K-12. Lett. Appl. Microbiol. 8:143-146.
    • (1989) Lett. Appl. Microbiol. , vol.8 , pp. 143-146
    • Kumagai, H.1    Echigo, T.2    Suzuki, H.3    Tochikura, T.4
  • 15
    • 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., T. Echigo, H. Suzuki, and T. Tochikura. 1989. 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. 53:1429-1430.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 1429-1430
    • Kumagai, H.1    Echigo, T.2    Suzuki, H.3    Tochikura, T.4
  • 16
    • 0023686906 scopus 로고
    • Synthesis of γ-glutamyl-DOPA from L-glutamine and L-DOPA by γ-glutamyltranspeptidase of Escherichia coli K-12
    • Kumagai, H., T. Echigo, H. Suzuki, and T. Tochikura. 1988. Synthesis of γ-glutamyl-DOPA from L-glutamine and L-DOPA by γ -glutamyltranspeptidase of Escherichia coli K-12. Agric. Biol. Chem. 52:1377-1382.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 1377-1382
    • Kumagai, H.1    Echigo, T.2    Suzuki, H.3    Tochikura, T.4
  • 17
    • 0025657462 scopus 로고
    • Syntheses of γ-glutamyl peptides by γ-glutamyltranspeptidase from E. coli
    • Kumagai, H., H. Suzuki, T. Echigo, and T. Tochikura. 1990. Syntheses of γ-glutamyl peptides by γ-glutamyltranspeptidase from E. coli. Ann. N. Y. Acad. Sci. 613:647-651.
    • (1990) Ann. N. Y. Acad. Sci. , vol.613 , pp. 647-651
    • Kumagai, H.1    Suzuki, H.2    Echigo, T.3    Tochikura, T.4
  • 18
    • 0024303282 scopus 로고
    • Utilization of the γ-glutamyltranspeptidase reaction for glutathione synthesis
    • Kumagai, H., H. Suzuki, M. Shimizu, and T. Tochikura. 1989. Utilization of the γ-glutamyltranspeptidase reaction for glutathione synthesis. J. Biotechnol. 9:129-138.
    • (1989) J. Biotechnol. , vol.9 , pp. 129-138
    • Kumagai, H.1    Suzuki, H.2    Shimizu, M.3    Tochikura, T.4
  • 20
    • 0002220885 scopus 로고
    • Constituents in tea leaf and their contribution to the taste of green tea liquor
    • Nakagawa, M. 1970. Constituents in tea leaf and their contribution to the taste of green tea liquor. Jpn. Agric. Res. Q. 5:43-47.
    • (1970) Jpn. Agric. Res. Q , vol.5 , pp. 43-47
    • Nakagawa, M.1
  • 21
    • 85024258028 scopus 로고
    • Studies on the chemical constituents of tea. Part III. On a new amide theanine
    • In Japanese
    • Sakato, Y. 1949. Studies on the chemical constituents of tea. Part III. On a new amide theanine. Nippon Nogeikagaku Kaishi. 23:262-267. (In Japanese.)
    • (1949) Nippon Nogeikagaku Kaishi , vol.23 , pp. 262-267
    • Sakato, Y.1
  • 22
    • 0036843218 scopus 로고    scopus 로고
    • Enzymatic production of theanine, an "umami" component of tea, from glutamine and ethylamine with bacterial γ-glutamyltranspeptidase
    • Suzuki, H., S. Izuka, N. Miyakawa, and H. Kumagai. 2002. Enzymatic production of theanine, an "umami" component of tea, from glutamine and ethylamine with bacterial γ-glutamyltranspeptidase. Enzyme Microb. Technol. 31:884-889.
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 884-889
    • Suzuki, H.1    Izuka, S.2    Miyakawa, N.3    Kumagai, H.4
  • 23
    • 0037116432 scopus 로고    scopus 로고
    • Improvement of the bitter taste of amino acids through the transpeptidation reaction of bacterial γ-glutamyltranspeptidase
    • Suzuki, H., Y. Kajimoto, and H. Kumagai. 2002. Improvement of the bitter taste of amino acids through the transpeptidation reaction of bacterial γ-glutamyltranspeptidase. J. Agric. Food Chem. 50:313-318.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 313-318
    • Suzuki, H.1    Kajimoto, Y.2    Kumagai, H.3
  • 24
    • 0023835701 scopus 로고
    • Molecular cloning of Escherichia coli K-12 ggt and rapid isolation of γ-glutamyltranspeptidase
    • Suzuki, H., H. Kumagai, T. Echigo, and T. Tochikura. 1988. Molecular cloning of Escherichia coli K-12 ggt and rapid isolation of γ -glutamyltranspeptidase. Biochem. Biophys. Res. Commun. 150:33-38.
    • (1988) Biochem. Biophys. Res. Commun. , vol.150 , pp. 33-38
    • Suzuki, H.1    Kumagai, H.2    Echigo, T.3    Tochikura, T.4
  • 25
    • 0022908614 scopus 로고
    • γ-glutamyltranspeptidase from Escherichia coli K-12: Formation and localization
    • Suzuki, H., H. Kumagai, and T. Tochikura. 1986. γ -Glutamyltranspeptidase from Escherichia coli K-12: formation and localization. J. Bacteriol. 168: 1332-1335.
    • (1986) J. Bacteriol. , vol.168 , pp. 1332-1335
    • Suzuki, H.1    Kumagai, H.2    Tochikura, T.3
  • 26
    • 0022891712 scopus 로고
    • γ-glutamyltranspeptidase from Escherichia coli K-12: Purification and properties
    • Suzuki, H., H. Kumagai, and T. Tochikura. 1986. γ -Glutamyltranspeptidase from Escherichia coli K-12: purification and properties. J. Bacteriol. 168: 1325-1331.
    • (1986) J. Bacteriol. , vol.168 , pp. 1325-1331
    • Suzuki, H.1    Kumagai, H.2    Tochikura, T.3
  • 27
    • 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., N. Miyakawa, and H. Kumagai. 2002. Enzymatic production of γ-L-glutamyltaurine through the transpeptidation reaction of γ-glutamyltranspeptidase from Escherichia coli K-12. Enzyme Microb. Technol. 30:883-888.
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 883-888
    • Suzuki, H.1    Miyakawa, N.2    Kumagai, H.3
  • 28
    • 0019888435 scopus 로고
    • γ-glutamyl transpeptidase: Catalytic, structural and functional aspects
    • Tate, S. S., and A. Meister. 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
  • 29
    • 0016389670 scopus 로고
    • Interaction of γ-glutamyl transpeptidase with amino acids, dipeptides, and derivatives and analogs of glutathione
    • Tate, S. S., and A. Meister. 1974. Interaction of γ-glutamyl transpeptidase with amino acids, dipeptides, and derivatives and analogs of glutathione. J. Biol. Chem. 249:7593-7602.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7593-7602
    • Tate, S.S.1    Meister, A.2
  • 30
    • 0017666965 scopus 로고
    • Interrelationships between the binding sites for amino acids, dipeptides, and γ-glutamyl donors in γ-glutamyl transpeptidase
    • Thompson, G. A., and A. Meister. 1977. Interrelationships between the binding sites for amino acids, dipeptides, and γ-glutamyl donors in γ-glutamyl transpeptidase. J. Biol. Chem. 252:6792-6798.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6792-6798
    • Thompson, G.A.1    Meister, A.2
  • 31
    • 0018117844 scopus 로고
    • γ-glutamyl dopa: Kidney-specific dopamine precursor
    • Wilk, S., H. Mizoguchi, and M. Orlowski. 1977. γ-Glutamyl dopa: kidney-specific dopamine precursor. J. Pharmacol. Exp. Ther. 206:227-232.
    • (1977) J. Pharmacol. Exp. Ther. , vol.206 , pp. 227-232
    • Wilk, S.1    Mizoguchi, H.2    Orlowski, M.3
  • 32
    • 0242437735 scopus 로고
    • The synthesis of γ-alkylamides of L-glutamic acid. The reactions of metallic salts of L-pyrrolidonecarboxylic acid with primary alkylamines
    • Yamada, Y., M. Sakurai, and Y. Tsuchiya. 1966. The synthesis of γ-alkylamides of L-glutamic acid. The reactions of metallic salts of L-pyrrolidonecarboxylic acid with primary alkylamines. Bull. Chem. Soc. Jpn. 39:1999-2000.
    • (1966) Bull. Chem. Soc. Jpn. , vol.39 , pp. 1999-2000
    • Yamada, Y.1    Sakurai, M.2    Tsuchiya, Y.3


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