메뉴 건너뛰기




Volumn 66, Issue 7, 2002, Pages 1500-1514

Recognition of a Cysteine Substrate by E. coliγ-Glutamylcysteine Synthetase Probed by Sulfoximine-based Transition-state Analogue Inhibitors

Author keywords

E. coli glutamylcysteine synthetase; Substrate specificity; Sulfoximine; Transition state analogue inhibitor; Transition state stabilization

Indexed keywords

BUTHIONINE SULFOXIMINE; CYSTEINE; DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS; ENZYME INHIBITOR; GLUTAMATE CYSTEINE LIGASE;

EID: 0036654787     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.1500     Document Type: Article
Times cited : (16)

References (21)
  • 2
    • 0032617250 scopus 로고    scopus 로고
    • The enzymes of glutathione synthesis: G-glutamylcysteine synthetase
    • Griffith, O. W., and Mulcahy, R. T., The enzymes of glutathione synthesis: g-glutamylcysteine synthetase. Adv. Enzymol. Rel. Areas of Mol. Biol., 73, 209-267 (1999).
    • (1999) Adv. Enzymol. Rel. Areas of Mol. Biol. , vol.73 , pp. 209-267
    • Griffith, O.W.1    Mulcahy, R.T.2
  • 3
    • 0026343403 scopus 로고
    • Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy
    • Meister, A., Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy. Pharmac. Ther., 51, 155-194 (1991).
    • (1991) Pharmac. Ther. , vol.51 , pp. 155-194
    • Meister, A.1
  • 4
    • 4243987802 scopus 로고    scopus 로고
    • L-S, R-Buthionine sulfoximine: Historical development and clinical issues
    • Bailey, H. H., L-S, R-Buthionine sulfoximine: historical development and clinical issues. Chemico-Biol. Interactions, 111-112, 239-254 (1998).
    • (1998) Chemico-Biol. Interactions , vol.111-112 , pp. 239-254
    • Bailey, H.H.1
  • 5
    • 0035834745 scopus 로고    scopus 로고
    • Structure prediction and active site analysis of the metal binding determinants in g-glutamylcysteine synthetase
    • Abbott, J. J., Pei, J., Ford, J. L., Qi, Y., Grishin, V. N., Pitcher, L. A., Phillips, M. A., and Grishin, N. V., Structure prediction and active site analysis of the metal binding determinants in g-glutamylcysteine synthetase. J. Biol. Chem., 276, 42099-42107 (2001).
    • (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    Pitcher, L.A.6    Phillips, M.A.7    Grishin, N.V.8
  • 6
    • 0015218939 scopus 로고
    • Partial reactions catalyzed by g-glutamylcysteine synthetase and evidence for an activated glutamate intermediate
    • Orlowski, M. and Meister, A., Partial reactions catalyzed by g-glutamylcysteine synthetase and evidence for an activated glutamate intermediate. J. Biol. Chem., 246, 7095-7105 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 7095-7105
    • Orlowski, M.1    Meister, A.2
  • 7
    • 0023987919 scopus 로고
    • On the active site thiol of g-glutamylcysteine synthetase: Relationships to catalysis, inhibition, and regulation
    • Huang, C.-S., Moore, W. R., and Meister, A., On the active site thiol of g-glutamylcysteine synthetase: Relationships to catalysis, inhibition, and regulation. Proc. Natl. Acad. Sci. USA, 85, 2464-2468 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2464-2468
    • Huang, C.-S.1    Moore, W.R.2    Meister, A.3
  • 8
    • 0017187544 scopus 로고
    • The kinetic mechanism of rat kidney g-glutamylcysteine synthetase
    • Yip, B. and Rudolph, F. B., The kinetic mechanism of rat kidney g-glutamylcysteine synthetase. J. Biol. Chem., 251, 3563-3568 (1976).
    • (1976) J. Biol. Chem. , vol.251 , pp. 3563-3568
    • Yip, B.1    Rudolph, F.B.2
  • 9
    • 0019888280 scopus 로고
    • Isotope exchange at equilibrium studies with rat kidney g-glutamylcysteine synthetase
    • Schandle, V. B. and Rudolph, F. B., Isotope exchange at equilibrium studies with rat kidney g-glutamylcysteine synthetase. J. Biol. Chem., 256, 7590-7594 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 7590-7594
    • Schandle, V.B.1    Rudolph, F.B.2
  • 10
    • 0018666729 scopus 로고
    • Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine)
    • Griffith, O. W. and Meister, A., Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine). J. Biol. Chem., 254, 7558-7560 (1979).
    • (1979) J. Biol. Chem. , vol.254 , pp. 7558-7560
    • Griffith, O.W.1    Meister, A.2
  • 11
    • 0020444895 scopus 로고
    • Mechanism of action, metabolism, and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis
    • Griffith, O. W., Mechanism of action, metabolism, and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis. J. Biol. Chem., 257, 13704-13712 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 13704-13712
    • Griffith, O.W.1
  • 12
    • 0027226399 scopus 로고
    • Purification and biochemical characterization of g-glutamylcysteine synthetase from a human malignant astrocytoma cell line
    • Sriram, R. and Ali-Osman, F., Purification and biochemical characterization of g-glutamylcysteine synthetase from a human malignant astrocytoma cell line. Biochem. Mol. Biol. Int., 30, 1053-1060 (1993).
    • (1993) Biochem. Mol. Biol. Int. , vol.30 , pp. 1053-1060
    • Sriram, R.1    Ali-Osman, F.2
  • 13
    • 0037016697 scopus 로고    scopus 로고
    • E. Coli g-Glutamyl cysteine synthetase: Two active site metal ions affect substrate and inhibitor binding
    • Kelly, B. S., Antholine, W. E., and Griffith, O. W., E. coli g-Glutamyl cysteine synthetase: Two active site metal ions affect substrate and inhibitor binding. J. Biol. Chem., 277, 50-58 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 50-58
    • Kelly, B.S.1    Antholine, W.E.2    Griffith, O.W.3
  • 14
    • 0010214035 scopus 로고
    • Purification and characterization of g-glutamylcysteine synthetase of Escherichia coli B
    • Watanabe, K., Murata, K., and Kimura, A., Purification and characterization of g-glutamylcysteine synthetase of Escherichia coli B. Agric. Biol. Chem., 50, 1925-1930 (1986).
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 1925-1930
    • Watanabe, K.1    Murata, K.2    Kimura, A.3
  • 15
    • 0031755549 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of transition-state analogue inhibitors of Escherichia coli g-glutamylcysteine synthetase
    • Tokutake, N., Hiratake, J., Katoh, M., Irie, T., Kato, H., and Oda, J., Design, synthesis and evaluation of transition-state analogue inhibitors of Escherichia coli g-glutamylcysteine synthetase. Bioorg. Med. Chem., 6, 1935-1953 (1998).
    • (1998) Bioorg. Med. Chem. , vol.6 , pp. 1935-1953
    • Tokutake, N.1    Hiratake, J.2    Katoh, M.3    Irie, T.4    Kato, H.5    Oda, J.6
  • 16
    • 0001784072 scopus 로고
    • A novel method of preparing alpha-substituted hydracrylate and acrylate esters
    • Herrmann, J. L. and Schlessinger, R. H., A novel method of preparing alpha-substituted hydracrylate and acrylate esters. Tetrahedron Lett., 2429-2432 (1973).
    • (1973) Tetrahedron Lett. , pp. 2429-2432
    • Herrmann, J.L.1    Schlessinger, R.H.2
  • 17
    • 84989750757 scopus 로고
    • Wittig-Horner reaction in heterogeneous media; 1. An easy synthesis of ethyl a-hydroxymethylacrylate and ethyl a-halomethylacrylates using formaldehyde in water
    • Villieras, J. and Rambaud, M., Wittig-Horner reaction in heterogeneous media; 1. An easy synthesis of ethyl a-hydroxymethylacrylate and ethyl a-halomethylacrylates using formaldehyde in water. Synthesis, 924-926 (1982).
    • (1982) Synthesis , pp. 924-926
    • Villieras, J.1    Rambaud, M.2
  • 19
    • 0000012935 scopus 로고
    • Synthesis of optically active sulfoximines from optically active sulfoxides
    • Johnson, C. R., Kirchhoff, R. A., and Corkins, H. G., Synthesis of optically active sulfoximines from optically active sulfoxides. J. Org. Chem., 39, 2458-2459 (1974).
    • (1974) J. Org. Chem. , vol.39 , pp. 2458-2459
    • Johnson, C.R.1    Kirchhoff, R.A.2    Corkins, H.G.3
  • 20
    • 0003443852 scopus 로고
    • Bergmeyer, H. U., Bergmeyer, J., and Grassl, M., vol. 3, 3rd ed., Verlag Chemie, Weinheim, pp
    • Brolin, S. E. In “Methods of Enzymatic Analysis,” eds. Bergmeyer, H. U., Bergmeyer, J., and Grassl, M., vol. 3, 3rd ed., Verlag Chemie, Weinheim, pp. 540-559 (1983).
    • (1983) Methods of Enzymatic Analysis , pp. 540-559
    • Brolin, S.E.1
  • 21
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Meister, A., Wiley, New York, pp
    • Morrison, J. F. and Walsh, C. T., The behavior and significance of slow-binding enzyme inhibitors. In “Advances in Enzymology,” ed. Meister, A., Wiley, New York, pp. 201-301 (1988).
    • (1988) Advances in Enzymology , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.