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Volumn 94, Issue 6, 2012, Pages 1327-1333

Glutathione synthetase promotes the reduction of arsenate via arsenolysis of glutathione

Author keywords

ADP arsenate; Arsenolysis; Glutathione; Glutathione synthetase; Reduction

Indexed keywords

ARSENIC ACID; ARSENIC TRIOXIDE; GLUTATHIONE; GLUTATHIONE SYNTHASE; GLYCINE; PHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84860489518     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.02.033     Document Type: Article
Times cited : (17)

References (26)
  • 2
    • 0034759637 scopus 로고    scopus 로고
    • The cellular metabolism and systemic toxicity of arsenic
    • DOI 10.1006/taap.2001.9258
    • D.J. Thomas, M. Styblo, and S. Lin The cellular metabolism and systemic toxicity of arsenic Toxicol. Appl. Pharmacol. 176 2001 127 144 (Pubitemid 33015863)
    • (2001) Toxicology and Applied Pharmacology , vol.176 , Issue.2 , pp. 127-144
    • Thomas, D.J.1    Styblo, M.2    Lin, S.3
  • 3
    • 0027248786 scopus 로고
    • A chemical hypothesis for arsenic methylation in mammals
    • D.J. Thompson A chemical hypothesis for arsenic methylation in mammals Chem. Biol. Interact. 88 1993 89 114 (Pubitemid 23278019)
    • (1993) Chemico-Biological Interactions , vol.88 , Issue.2-3 , pp. 89-114
    • Thompson, D.J.1
  • 4
    • 39549101455 scopus 로고    scopus 로고
    • The role of protein binding of trivalent arsenicals in arsenic carcinogenesis and toxicity
    • K.T. Kitchin, and K. Wallace The role of protein binding of trivalent arsenicals in arsenic carcinogenesis and toxicity J. Inorg. Biochem. 102 2008 532 539
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 532-539
    • Kitchin, K.T.1    Wallace, K.2
  • 6
    • 0037010116 scopus 로고    scopus 로고
    • Biochemistry of arsenic detoxification
    • DOI 10.1016/S0014-5793(02)03186-1, PII S0014579302031861
    • B.P. Rosen Biochemistry of arsenic detoxification FEBS Lett. 529 2002 86 92 (Pubitemid 35283916)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 86-92
    • Rosen, B.P.1
  • 7
    • 67650708885 scopus 로고    scopus 로고
    • Mechanism of thiol-supported arsenate reduction mediated by phosphorolytic-arsenolytic enzymes. II. Enzymatic formation of arsenylated products susceptible for reduction to arsenite by thiols
    • Z. Gregus, G. Roos, P. Geerlings, and B. Németi Mechanism of thiol-supported arsenate reduction mediated by phosphorolytic-arsenolytic enzymes. II. Enzymatic formation of arsenylated products susceptible for reduction to arsenite by thiols Toxicol. Sci. 110 2009 282 292
    • (2009) Toxicol. Sci. , vol.110 , pp. 282-292
    • Gregus, Z.1    Roos, G.2    Geerlings, P.3    Németi, B.4
  • 8
    • 67650727412 scopus 로고    scopus 로고
    • Mechanism of thiol-supported arsenate reduction mediated by phosphorolytic-arsenolytic enzymes. I. The role of arsenolysis
    • B. Németi, and Z. Gregus Mechanism of thiol-supported arsenate reduction mediated by phosphorolytic-arsenolytic enzymes. I. The role of arsenolysis Toxicol. Sci. 110 2009 270 281
    • (2009) Toxicol. Sci. , vol.110 , pp. 270-281
    • Németi, B.1    Gregus, Z.2
  • 9
    • 77956937844 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase and mitochondrial ATP synthase mediate reduction of arsenate to the more toxic arsenite by forming arsenylated analogs of ADP and ATP
    • B. Németi, M.E. Regonesi, P. Tortora, and Z. Gregus Polynucleotide phosphorylase and mitochondrial ATP synthase mediate reduction of arsenate to the more toxic arsenite by forming arsenylated analogs of ADP and ATP Toxicol. Sci. 117 2010 270 281
    • (2010) Toxicol. Sci. , vol.117 , pp. 270-281
    • Németi, B.1    Regonesi, M.E.2    Tortora, P.3    Gregus, Z.4
  • 10
    • 79951515537 scopus 로고    scopus 로고
    • The mechanism of the polynucleotide phosphorylase-catalyzed arsenolysis of ADP
    • B. Németi, M.E. Regonesi, P. Tortora, and Z. Gregus The mechanism of the polynucleotide phosphorylase-catalyzed arsenolysis of ADP Biochimie 93 2011 624 627
    • (2011) Biochimie , vol.93 , pp. 624-627
    • Németi, B.1    Regonesi, M.E.2    Tortora, P.3    Gregus, Z.4
  • 11
    • 10044268245 scopus 로고    scopus 로고
    • Role of glutathione in reduction of arsenate and of γ- glutamyltranspeptidase in disposition of arsenite in rats
    • DOI 10.1016/j.tox.2004.09.002, PII S0300483X0400561X
    • I. Csanaky, and Z. Gregus Role of glutathione in reduction of arsenate and of γ-glutamyltranspeptidase in disposition of arsenite in rats Toxicology 207 2005 91 104 (Pubitemid 39601689)
    • (2005) Toxicology , vol.207 , Issue.1 , pp. 91-104
    • Csanaky, I.1    Gregus, Z.2
  • 12
    • 77956912564 scopus 로고
    • Glutathione synthesis
    • A. Meister Glutathione synthesis Enzym. 22 1974 671 697
    • (1974) Enzym. , vol.22 , pp. 671-697
    • Meister, A.1
  • 14
    • 0001040277 scopus 로고
    • Intermediate formation of dipeptide-phosphate anhydride in enzymatic tripeptide synthesis
    • J.S. Nishimura, E.A. Dodd, and A. Meister Intermediate formation of dipeptide-phosphate anhydride in enzymatic tripeptide synthesis J. Biol. Chem. 239 1964 2553 2558
    • (1964) J. Biol. Chem. , vol.239 , pp. 2553-2558
    • Nishimura, J.S.1    Dodd, E.A.2    Meister, A.3
  • 15
    • 0018801016 scopus 로고
    • Glutathione synthetase - Purification from rat kidney and mapping of the substrate binding sites
    • L. Oppenheimer, V.P. Wellner, O.W. Griffith, and A. Meister Glutathione synthetase - Purification from rat kidney and mapping of the substrate binding sites J. Biol. Chem. 254 1979 5184 5190
    • (1979) J. Biol. Chem. , vol.254 , pp. 5184-5190
    • Oppenheimer, L.1    Wellner, V.P.2    Griffith, O.W.3    Meister, A.4
  • 16
    • 0037291506 scopus 로고    scopus 로고
    • Dose-dependent biotransformation of arsenite in rats - Not S-adenosylmethionine depletion impairs arsenic methylation at high dose
    • DOI 10.1016/S0300-483X(02)00444-4, PII S0300483X02004444
    • I. Csanaky, B. Németi, and Z. Gregus Dose-dependent biotransformation of arsenite in rats - not S-adenosylmethionine depletion impairs arsenic methylation at high dose Toxicology 183 2003 77 91 (Pubitemid 36005391)
    • (2003) Toxicology , vol.183 , Issue.1-3 , pp. 77-91
    • Csanaky, I.1    Nemeti, B.2    Gregus, Z.3
  • 17
    • 0036387147 scopus 로고    scopus 로고
    • Mitochondria work as reactors in reducing arsenate to arsenite
    • B. Németi, and Z. Gregus Mitochondria work as reactors in reducing arsenate to arsenite Toxicol. Appl. Pharmacol. 182 2002 208 218
    • (2002) Toxicol. Appl. Pharmacol. , vol.182 , pp. 208-218
    • Németi, B.1    Gregus, Z.2
  • 18
    • 2542463862 scopus 로고    scopus 로고
    • Function of conserved residues of human glutathione synthetase: Implications for the ATP-grasp enzymes
    • DOI 10.1074/jbc.M401334200
    • A. Dinescu, T.R. Cundari, V.S. Bhansali, J.L. Luo, and M.E. Anderson Function of conserved residues of human glutathione synthetase: implications for the ATP-grasp enzymes J. Biol. Chem. 279 2004 22412 22421 (Pubitemid 38679439)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , pp. 22412-22421
    • Dinescu, A.1    Cundari, T.R.2    Bhansali, V.S.3    Luo, J.-L.4    Anderson, M.E.5
  • 20
    • 10044259621 scopus 로고    scopus 로고
    • Glutathione-dependent reduction of arsenate in human erythrocytes - A process independent of purine nucleoside phosphorylase
    • DOI 10.1093/toxsci/kfh301
    • B. Németi, and Z. Gregus Glutathione-dependent reduction of arsenate in human erythrocytes - a process independent of purine nucleoside phosphorylase Toxicol. Sci. 82 2004 419 428 (Pubitemid 39600068)
    • (2004) Toxicological Sciences , vol.82 , Issue.2 , pp. 419-428
    • Nemeti, B.1    Gregus, Z.2
  • 21
    • 0024566928 scopus 로고
    • γ-Aminobutyric acid, glutamate, glycine and taurine analysis using reversed-phase high-performance liquid chromatography and ultraviolet detection of dansyl chloride derivatives
    • DOI 10.1016/S0378-4347(00)83020-0
    • C.F. Saller, and M.J. Czupryna γ-Amino-butyric acid, glutamate, glycine, and taurine analysis using reversed-phase high-performance liquid chromatography and ultraviolet detection of dansyl chloride derivations J. Chromatogr. 487 1989 167 172 (Pubitemid 19122061)
    • (1989) Journal of Chromatography - Biomedical Applications , vol.487 , Issue.1 , pp. 167-172
    • Saller, C.F.1    Czupryna, M.J.2
  • 22
    • 0033936088 scopus 로고    scopus 로고
    • Biliary and urinary excretion of inorganic arsenic: Monomethylarsonous acid as a major biliary metabolite in rats
    • Z. Gregus, Á. Gyurasics, and I. Csanaky Biliary and urinary excretion of inorganic arsenic: monomethylarsonous acid as a major biliary metabolite in rats Toxicol. Sci. 56 2000 18 25 (Pubitemid 30441461)
    • (2000) Toxicological Sciences , vol.56 , Issue.1 , pp. 18-25
    • Gregus, Z.1    Gyurasics, A.2    Csanaky, I.3
  • 23
    • 20544448672 scopus 로고    scopus 로고
    • The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase works as an arsenate reductase in human red blood cells and rat liver cytosol
    • DOI 10.1093/toxsci/kfi158
    • Z. Gregus, and B. Németi The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase works as an arsenate reductase in human red blood cells and rat liver cytosol Toxicol. Sci. 85 2005 859 869 (Pubitemid 40846860)
    • (2005) Toxicological Sciences , vol.85 , Issue.2 , pp. 859-869
    • Gregus, Z.1    Nemeti, B.2
  • 24
    • 67650767084 scopus 로고    scopus 로고
    • Glutathione-supported arsenate reduction coupled to arsenolysis catalyzed by ornithine carbamoyl transferase
    • B. Németi, and Z. Gregus Glutathione-supported arsenate reduction coupled to arsenolysis catalyzed by ornithine carbamoyl transferase Toxicol. Appl. Pharmacol. 239 2009 154 161
    • (2009) Toxicol. Appl. Pharmacol. , vol.239 , pp. 154-161
    • Németi, B.1    Gregus, Z.2
  • 25
    • 0036905245 scopus 로고    scopus 로고
    • Large conformational changes in the catalytic cycle of glutathione synthase
    • DOI 10.1016/S0969-2126(02)00906-1, PII S0969212602009061
    • A. Gogos, and L. Shapiro Large conformational changes in the catalytic cycle of glutathione synthase Structure 10 2002 1669 1676 (Pubitemid 35452574)
    • (2002) Structure , vol.10 , Issue.12 , pp. 1669-1676
    • Gogos, A.1    Shapiro, L.2
  • 26
    • 0037140394 scopus 로고    scopus 로고
    • A spectrophotometric assay of γ-glutamylcysteine synthetase and glutathione synthetase in crude extracts from tissues and cultured mammalian cells
    • DOI 10.1016/S0009-2797(02)00017-0, PII S0009279702000170
    • G. Volohonsky, C.N.Y.H. Tuby, N. Porat, M. Wellman-Rousseau, A. Visvikis, P. Leroy, S. Rashi, P. Steinberg, and A.A. Stark A spectrophotometric assay of γ-glutamylcysteine synthetase and glutathione synthetase in crude extracts from tissues and cultured mammalian cells Chem. Biol. Interact. 140 2002 49 65 (Pubitemid 34606851)
    • (2002) Chemico-Biological Interactions , vol.140 , Issue.1 , pp. 49-65
    • Volohonsky, G.1    Tuby, C.N.Y.H.2    Porat, N.3    Wellman-Rousseau, M.4    Visvikis, A.5    Leroy, P.6    Rashi, S.7    Steinberg, P.8    Stark, A.-A.9


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