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Volumn 352, Issue 2, 2007, Pages 351-359

Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum

Author keywords

Glutamylcysteine synthetase; Glutamylpeptide; Clostridium acetobutylicum; Glutathione; Glutathione synthetase; Streptococcus agalactiae

Indexed keywords

AMINO ACID; GAMMA GLUTAMYLTRIPEPTIDE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE SYNTHASE; HYBRID PROTEIN; PEPTIDE;

EID: 33751538620     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.11.016     Document Type: Article
Times cited : (21)

References (26)
  • 3
    • 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
    • Takai K. (Ed), Elsevier Science Publishers B.V., Amsterdam, The Netherlands
    • Hara T., Yokoo Y., and Furukawa T. Potential of γ-l-glutamyl-l-cystine and bis-γ-l-glutamyl-l-cystine as a Cystine Containing Peptide for Parenteral Nutrition. In: Takai K. (Ed). Frontiers and New Horizons in Amino Acid Research (1992), Elsevier Science Publishers B.V., Amsterdam, The Netherlands 607-611
    • (1992) Frontiers and New Horizons in Amino Acid Research , pp. 607-611
    • Hara, T.1    Yokoo, Y.2    Furukawa, T.3
  • 4
    • 0023783312 scopus 로고
    • A comparison of the rental actions of γ-l-glutamyl-l-dopa and γ-l-glutamyl-l-tyrosine in normal man
    • Jeffrey R.F., MacDonald T.M., and Lee M.R. A comparison of the rental actions of γ-l-glutamyl-l-dopa and γ-l-glutamyl-l-tyrosine in normal man. Clin. Sci. 74 (1988) 37-40
    • (1988) Clin. Sci. , vol.74 , pp. 37-40
    • Jeffrey, R.F.1    MacDonald, T.M.2    Lee, M.R.3
  • 5
    • 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., and 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
    • 84985345649 scopus 로고
    • Enzymatic synthesis of γ-glutamyl-l-histidine by γ-glutamyltranspeptidase from Escherichia coli K-12
    • Kumagai H., Echigo T., Suzuki H., and Tochikura T. Enzymatic synthesis of γ-glutamyl-l-histidine by γ-glutamyltranspeptidase from Escherichia coli K-12. Lett. Appl. Microbial. 8 (1989) 143-146
    • (1989) Lett. Appl. Microbial. , vol.8 , pp. 143-146
    • Kumagai, H.1    Echigo, T.2    Suzuki, H.3    Tochikura, T.4
  • 8
    • 0012795027 scopus 로고
    • Enzymatic synthesis of γ-glutamyl-tyrosine methyl ester from l-glutamine and l-tyrosine methyl ester with Escherichia coli K-12 γ-glutamyltranspeptidase
    • Kumagai H., Echigo T., Suzuki H., and Tochikura T. Enzymatic synthesis of γ-glutamyl-tyrosine 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
  • 10
  • 11
    • 0035834745 scopus 로고    scopus 로고
    • Structure prediction and active site analysis of the metal binding determinants in γ-glutamylcysteine synthetase
    • Abbott J.J., Pei J., Ford J.L., Qi Y., Grishin V.N., Picher L.A., Phillips M.A., and Grishin N.V. Structure prediction and active site analysis of the metal binding determinants in γ-glutamylcysteine synthetase. J. Biol. Chem. 276 (2001) 42099-42107
    • (2001) J. Biol. Chem. , vol.276 , pp. 42099-42107
    • Abbott, J.J.1    Pei, J.2    Ford, J.L.3    Qi, Y.4    Grishin, V.N.5    Picher, L.A.6    Phillips, M.A.7    Grishin, N.V.8
  • 12
    • 15744398210 scopus 로고    scopus 로고
    • Glutathione synthetase in Streptococcus agalactiae
    • Janowiak B.E., and Griffith O.W. Glutathione synthetase in Streptococcus agalactiae. J. Biol. Chem. 280 (2005) 11829-11839
    • (2005) J. Biol. Chem. , vol.280 , pp. 11829-11839
    • Janowiak, B.E.1    Griffith, O.W.2
  • 13
    • 18944397128 scopus 로고    scopus 로고
    • A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis
    • Gopal S., Borovok I., Ofer A., Yanku M., Cohen G., Goebel W., Kreft J., and Aharonowitz Y. A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis. J. Bacteriol. 187 (2005) 3839-3847
    • (2005) J. Bacteriol. , vol.187 , pp. 3839-3847
    • Gopal, S.1    Borovok, I.2    Ofer, A.3    Yanku, M.4    Cohen, G.5    Goebel, W.6    Kreft, J.7    Aharonowitz, Y.8
  • 14
    • 33645224817 scopus 로고    scopus 로고
    • Characterization of the bifunctional g-glutamate-cysteine ligase/glutathione synthetase (GshF) of Pasteurella multocida
    • Vergauwen B., Vos D.D., and Van Beeumen J.J. Characterization of the bifunctional g-glutamate-cysteine ligase/glutathione synthetase (GshF) of Pasteurella multocida. J. Biol. Chem. 281 (2006) 4380-4394
    • (2006) J. Biol. Chem. , vol.281 , pp. 4380-4394
    • Vergauwen, B.1    Vos, D.D.2    Van Beeumen, J.J.3
  • 15
    • 0032126145 scopus 로고    scopus 로고
    • Expression and purification of human γ-glutamylcysteine synthetase
    • Misra I., and Griffith O.W. Expression and purification of human γ-glutamylcysteine synthetase. Protein Expression Purif. 13 (1998) 268-276
    • (1998) Protein Expression Purif. , vol.13 , pp. 268-276
    • Misra, I.1    Griffith, O.W.2
  • 16
    • 51849181148 scopus 로고
    • Determination of d-amino acids. II. use of a bifunctional reagent, 1,5-difluoro-2,4-dinitrobenzene
    • Marfey P. Determination of d-amino acids. II. use of a bifunctional reagent, 1,5-difluoro-2,4-dinitrobenzene. Carlsberg Res. Commun. 49 (1984) 591-596
    • (1984) Carlsberg Res. Commun. , vol.49 , pp. 591-596
    • Marfey, P.1
  • 17
    • 0141960038 scopus 로고    scopus 로고
    • The glutathione synthetase of Schizosaccharomyces pombe is synthesized as a homodimer but retains full activity when present as a heterotetramer
    • Phlippen N., Hoffmann K., Fischer R., Wolf K., and Zimmermann M. The glutathione synthetase of Schizosaccharomyces pombe is synthesized as a homodimer but retains full activity when present as a heterotetramer. J. Biol. Chem. 278 (2003) 40152-40161
    • (2003) J. Biol. Chem. , vol.278 , pp. 40152-40161
    • Phlippen, N.1    Hoffmann, K.2    Fischer, R.3    Wolf, K.4    Zimmermann, M.5
  • 18
    • 0142213311 scopus 로고    scopus 로고
    • Interdomain communications in bifunctional enzymes: how are different activities coordinated?
    • Nagradova N. Interdomain communications in bifunctional enzymes: how are different activities coordinated?. IUBMB Life 55 (2003) 459-466
    • (2003) IUBMB Life , vol.55 , pp. 459-466
    • Nagradova, N.1
  • 19
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang X., Holden H.M., and Raushel F.M. Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu. Rev. Biochem. 70 (2001) 149-180
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 149-180
    • Huang, X.1    Holden, H.M.2    Raushel, F.M.3
  • 21
    • 0342276613 scopus 로고
    • The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis
    • Hyde C.C., and Miles E.W. The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis. Bio/Technol. 8 (1990) 27-32
    • (1990) Bio/Technol. , vol.8 , pp. 27-32
    • Hyde, C.C.1    Miles, E.W.2
  • 23
    • 0037938734 scopus 로고    scopus 로고
    • Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase
    • Myers R.S., Jensen J.R., Deras I.L., Smith J.L., and Davisson V.J. Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase. Biochemistry 42 (2003) 7013-7022
    • (2003) Biochemistry , vol.42 , pp. 7013-7022
    • Myers, R.S.1    Jensen, J.R.2    Deras, I.L.3    Smith, J.L.4    Davisson, V.J.5
  • 25
    • 0022891712 scopus 로고
    • γ-Glutamyltranspeptidase from Escherichia coli: purification and properties
    • Suzuki H., Kumagai H., and Tochikura T. γ-Glutamyltranspeptidase from Escherichia coli: 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
  • 26
    • 33748256537 scopus 로고    scopus 로고
    • γ-Glutamylcysteine synthetase-glutathione synthetase: domain structure and identification of residues important in substrate and glutathione binding
    • Janowiak B.E., Hayward M.A., Peterson F.C., Volkman B.F., and Griffith O.W. γ-Glutamylcysteine synthetase-glutathione synthetase: domain structure and identification of residues important in substrate and glutathione binding. Biochemistry 45 (2006) 10461-10473
    • (2006) Biochemistry , vol.45 , pp. 10461-10473
    • Janowiak, B.E.1    Hayward, M.A.2    Peterson, F.C.3    Volkman, B.F.4    Griffith, O.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.