메뉴 건너뛰기




Volumn 21, Issue 7, 1996, Pages 955-964

Metal-catalyzed oxidation and cleavage of octopus glutathione transferase by the Cu(II)-ascorbate system

Author keywords

Affinity cleavage; Cephalopods; Cu(II) ascorbate; Detoxification; Glutathione transferase; Oxidative modification

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; ASCORBIC ACID; COPPER ION; GLUTATHIONE TRANSFERASE; HEMOCYANIN; OXYGEN;

EID: 0029858367     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(96)00230-4     Document Type: Article
Times cited : (24)

References (46)
  • 1
    • 0024269217 scopus 로고
    • Glutathione transferases -Structure and catalytic activity
    • 1. Mannervik, B.; Danielson, U. H. Glutathione transferases -Structure and catalytic activity. CRC Crit. Rev. Biochem. 23:283-337; 1988.
    • (1988) Crc Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 2
    • 0025611278 scopus 로고
    • The enzymes of detoxication
    • 2. Jakoby, W. B.; Ziegler, D. M. The enzymes of detoxication. J. Biol. Chem. 265:20715-20718; 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20715-20718
    • Jakoby, W.B.1    Ziegler, D.M.2
  • 3
    • 0025971827 scopus 로고
    • Glutathione S-transferases: Reaction mechanism, structure, and function
    • 3. Armstrong, R. N. Glutathione S-transferases: Reaction mechanism, structure, and function. Chem. Res. Toxicol. 4:131-140; 1991.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 131-140
    • Armstrong, R.N.1
  • 4
    • 0027300033 scopus 로고
    • Glutathione S-transferases, structure, regulation, and therapeutic implications
    • 4. Rushmore, T. H.; Pickett, C. B. Glutathione S-transferases, structure, regulation, and therapeutic implications. J. Biol. Chem. 268:11475-11478; 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11475-11478
    • Rushmore, T.H.1    Pickett, C.B.2
  • 5
    • 0028224013 scopus 로고
    • X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function
    • 5. Dirr, H.; Reinemer, P.; Huber, R. X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function. Eur. J. Biochem. 220:645-661; 1994.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 645-661
    • Dirr, H.1    Reinemer, P.2    Huber, R.3
  • 6
    • 0028327862 scopus 로고
    • Glutathione S-transferases: Structure and mechanism of an archetypical detoxication enzyme
    • 6. Armstrong, R. N. Glutathione S-transferases: Structure and mechanism of an archetypical detoxication enzyme. Adv. Enzymol. Relat. Areas Mol. Biol. 69:1-44; 1994.
    • (1994) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.69 , pp. 1-44
    • Armstrong, R.N.1
  • 8
    • 0028263070 scopus 로고
    • Structure and function of glutathione S-transferases
    • 8. Wilce, M. C. J.; Parker, M. W. Structure and function of glutathione S-transferases. Biochim. Biophys. Acta 1205:1-18; 1994.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 1-18
    • Wilce, M.C.J.1    Parker, M.W.2
  • 9
    • 0029003807 scopus 로고
    • Crystal structure of a theta-class glutathione transferase
    • 9. Wilce, M. C. J.; Board, P. G.; Feil, S. C.; Parker, M. W. Crystal structure of a theta-class glutathione transferase. EMBO J. 14:2133-2143; 1995.
    • (1995) EMBO J. , vol.14 , pp. 2133-2143
    • Wilce, M.C.J.1    Board, P.G.2    Feil, S.C.3    Parker, M.W.4
  • 10
    • 0029064985 scopus 로고
    • Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods
    • 10. Ji, X.; von Rosenvinge, E. C.: Johnson, W. W.; Tomarev, S. I.; Piatigorsky, J.; Armstrong, R. N.; Gilliland, G. L. Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochemistry 34:5317-5328; 1995.
    • (1995) Biochemistry , vol.34 , pp. 5317-5328
    • Ji, X.1    Von Rosenvinge, E.C.2    Johnson, W.W.3    Tomarev, S.I.4    Piatigorsky, J.5    Armstrong, R.N.6    Gilliland, G.L.7
  • 13
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: Biological mechanism and biological consequences
    • 13. Stadtman, E. R. Metal ion-catalyzed oxidation of proteins: Biological mechanism and biological consequences. Free Radic. Biol. Med. 9:315-325; 1990.
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 315-325
    • Stadtman, E.R.1
  • 14
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • 14. Stadtman, E. R. Protein oxidation and aging. Science 257:1220-1224; 1992.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 15
    • 0026063519 scopus 로고
    • Site-specific DNA damage induced by hydrazine in the presence of manganese and copper ions
    • 15. Yamamoto, K.; Kawanishi, S. Site-specific DNA damage induced by hydrazine in the presence of manganese and copper ions. J. Biol. Chem. 266:1509-1515; 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1509-1515
    • Yamamoto, K.1    Kawanishi, S.2
  • 16
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • 16. Stohs, S. J.; Bagchi, D. Oxidative mechanisms in the toxicity of metal ions. Free Radic. Biol. Med. 18:321-336; 1995.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 321-336
    • Stohs, S.J.1    Bagchi, D.2
  • 17
    • 0001193904 scopus 로고
    • Functions of Pi-class glutathione S-transferase, roles in carcinogenesis and suppression by oxidative stress
    • Tew, K. D.; Pickett, C. B.; Mantle, T. J.; Mannervik, B.; Hayes, J. D. eds. Boca Raton, FL: CRC Press
    • 17. Tsuchida, S.; Sato, K.; Satoh, K.; Hatayama, I.; Yokoyama, Y.; Yamada, Y.; Shen, H.; Nishimura, S.; Suzuki, S.; Nakano, H. Functions of Pi-class glutathione S-transferase, roles in carcinogenesis and suppression by oxidative stress. In: Tew, K. D.; Pickett, C. B.; Mantle, T. J.; Mannervik, B.; Hayes, J. D. eds. Structure and function of glutathione transferases. Boca Raton, FL: CRC Press; 1993:223-233.
    • (1993) Structure and Function of Glutathione Transferases , pp. 223-233
    • Tsuchida, S.1    Sato, K.2    Satoh, K.3    Hatayama, I.4    Yokoyama, Y.5    Yamada, Y.6    Shen, H.7    Nishimura, S.8    Suzuki, S.9    Nakano, H.10
  • 18
    • 0025899026 scopus 로고
    • Modulation of class pi glutathione transferase by sulfyhydryl group modification
    • 18. Shen, H.; Tamai, K.; Satoh, K.; Hatayama, I.; Tsuchida, S.; Sato, K. Modulation of class pi glutathione transferase by sulfyhydryl group modification. Arch. Biochem. Biophys. 286:178-182; 1991.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 178-182
    • Shen, H.1    Tamai, K.2    Satoh, K.3    Hatayama, I.4    Tsuchida, S.5    Sato, K.6
  • 19
    • 0028589424 scopus 로고
    • Isolation and characterization of octopus hepatopancreatic glutathione S-transferase. Comparison of digestive gland enzyme with lens S-crystallin
    • 19. Tang, S. S.; Lin, C. C.; Chang, G. G. Isolation and characterization of octopus hepatopancreatic glutathione S-transferase. Comparison of digestive gland enzyme with lens S-crystallin. J. Protein Chem. 13:609-618; 1994.
    • (1994) J. Protein Chem. , vol.13 , pp. 609-618
    • Tang, S.S.1    Lin, C.C.2    Chang, G.G.3
  • 20
    • 0029031382 scopus 로고
    • Steady-state kinetics and chemical mechanism of octopus hepatopancreatic glutathione transferase
    • 20. Tang, S. S.; Chang, G. G. Steady-state kinetics and chemical mechanism of octopus hepatopancreatic glutathione transferase. Biochem. J. 309:347-353; 1995.
    • (1995) Biochem. J. , vol.309 , pp. 347-353
    • Tang, S.S.1    Chang, G.G.2
  • 21
    • 0000410616 scopus 로고
    • Nucleophilic aromatic substitution of glutathione and 1-chloro-2,4-dinitrobenzene in reverse micelles. A model system to assess the transition-state stabilization in glutathione transferase catalyzed conjugation
    • 21. Tang, S. S.; Chang, G. G. Nucleophilic aromatic substitution of glutathione and 1-chloro-2,4-dinitrobenzene in reverse micelles. A model system to assess the transition-state stabilization in glutathione transferase catalyzed conjugation. J. Org. Chem. 60:6183-6185; 1995.
    • (1995) J. Org. Chem. , vol.60 , pp. 6183-6185
    • Tang, S.S.1    Chang, G.G.2
  • 22
    • 0029872541 scopus 로고    scopus 로고
    • Kinetic mechanism of octopus hepatopancreatic glutathione transferase in reverse micelles
    • 22. Tang, S. S.; Chang, G. G. Kinetic mechanism of octopus hepatopancreatic glutathione transferase in reverse micelles. Biochem. J. 315:599-606; 1996.
    • (1996) Biochem. J. , vol.315 , pp. 599-606
    • Tang, S.S.1    Chang, G.G.2
  • 23
    • 0028279397 scopus 로고
    • Purification and kinetic mechanism of the glutathione S-transferase from C6/ 36, an Aedes albopictus cell line
    • 23. Chang, G. G.; Tsai, L. N.; Tang, S. S.; Wang, T. C. Purification and kinetic mechanism of the glutathione S-transferase from C6/ 36, an Aedes albopictus cell line. Arch. Biochem. Biophys. 310:134-143; 1994.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 134-143
    • Chang, G.G.1    Tsai, L.N.2    Tang, S.S.3    Wang, T.C.4
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein, utilizing the principle of protein-dye binding
    • 24. Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein, utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254; 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • 25. Habig, W. H.; Pabst, M. J.; Jacoby, W. B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249:7130-7139; 1974.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jacoby, W.B.3
  • 26
    • 0028057998 scopus 로고
    • A graphical method for determining the number of essential sites in enzymes with multiple binding sites for a ligand
    • 26. Wang, Z. X.; Srivastava, D. K. A graphical method for determining the number of essential sites in enzymes with multiple binding sites for a ligand. Anal. Biochem. 216:15-26; 1994.
    • (1994) Anal. Biochem. , vol.216 , pp. 15-26
    • Wang, Z.X.1    Srivastava, D.K.2
  • 27
    • 0027146667 scopus 로고
    • Oxidative polypeptide cleavage mediated by EDTA-Fe covalently linked to cysteine residues
    • 27. Platis, I. E.; Ermácora, M. R.; Fox, R. O. Oxidative polypeptide cleavage mediated by EDTA-Fe covalently linked to cysteine residues. Biochemistry 32:12761-12767; 1993.
    • (1993) Biochemistry , vol.32 , pp. 12761-12767
    • Platis, I.E.1    Ermácora, M.R.2    Fox, R.O.3
  • 28
    • 0025074680 scopus 로고
    • Site-specific cleavage of the protein calmodulin. Using a trifluoperazine-based affinity reagent
    • 28. Schepartz, A.; Cuenoud, B. Site-specific cleavage of the protein calmodulin. Using a trifluoperazine-based affinity reagent. J. Am. Chem. Soc. 112:3247-3249; 1990.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3247-3249
    • Schepartz, A.1    Cuenoud, B.2
  • 29
    • 0025042473 scopus 로고
    • A new strategy for selective protein cleavage
    • 29. Hoyer, D.; Cho, H.; Schultz, P. G. A new strategy for selective protein cleavage. J. Am. Chem. Soc. 112:3249-3250; 1990.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3249-3250
    • Hoyer, D.1    Cho, H.2    Schultz, P.G.3
  • 30
    • 0025718819 scopus 로고
    • Transfer of oxygen from an artificial protease to peptide carbon during proteolysis
    • 30. Rana, T. M.; Meares, C. F. Transfer of oxygen from an artificial protease to peptide carbon during proteolysis. Proc. Natl. Acad. Sci. USA 88:10578-10582; 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10578-10582
    • Rana, T.M.1    Meares, C.F.2
  • 31
    • 0027160740 scopus 로고
    • Effects of glutathione and chelating agents on copper-mediated DNA oxidation: Pro-oxidant and antioxidant properties of glutathione
    • 31. Milne, L.; Nicotera, P.; Orrenius, S.; Burkitt, M. J. Effects of glutathione and chelating agents on copper-mediated DNA oxidation: Pro-oxidant and antioxidant properties of glutathione. Arch. Biochem. Biophys. 304:102-109; 1993.
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 102-109
    • Milne, L.1    Nicotera, P.2    Orrenius, S.3    Burkitt, M.J.4
  • 32
    • 0027437209 scopus 로고
    • The centennial of the Fenton reaction
    • 32. Koppenol, W. H. The centennial of the Fenton reaction. Free Radic. Biol. Med. 15:645-651; 1993.
    • (1993) Free Radic. Biol. Med. , vol.15 , pp. 645-651
    • Koppenol, W.H.1
  • 33
  • 34
    • 0027303379 scopus 로고
    • New perspective on zinc biochemistry. Cocatalytic sites in multi-zinc enzymes
    • 34. Vallee, B. L.; Auld, D. S. New perspective on zinc biochemistry. Cocatalytic sites in multi-zinc enzymes. Biochemistry 32:6493-6500; 1993.
    • (1993) Biochemistry , vol.32 , pp. 6493-6500
    • Vallee, B.L.1    Auld, D.S.2
  • 37
    • 0026354479 scopus 로고
    • Crystallins of the octopus lens. Recruitment from detoxification enzymes
    • 37. Tomarev, S. I.; Zinovieva, R. D.; Piatigorsky, J. Crystallins of the octopus lens. Recruitment from detoxification enzymes. J. Biol. Chem. 266:24226-24231; 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24226-24231
    • Tomarev, S.I.1    Zinovieva, R.D.2    Piatigorsky, J.3
  • 38
    • 0029116553 scopus 로고
    • Octopus S-crystallins with endogenous glutathione S-transferase (GST) activity: Sequence comparison and evolutionary relationships with authentic GST enzymes
    • 38. Chiou, S. H.; Yu, C. W.; Lin, C. W.; Pan, F. M.; Lu, S. F.; Lee, H. J.; Chang, G. G. Octopus S-crystallins with endogenous glutathione S-transferase (GST) activity: Sequence comparison and evolutionary relationships with authentic GST enzymes. Biochem. J. 309:793-800; 1995.
    • (1995) Biochem. J. , vol.309 , pp. 793-800
    • Chiou, S.H.1    Yu, C.W.2    Lin, C.W.3    Pan, F.M.4    Lu, S.F.5    Lee, H.J.6    Chang, G.G.7
  • 39
    • 0027513157 scopus 로고
    • Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods
    • 39. Tomarev, S. I.; Zinovieva, R. D.; Guo, K.; Piatigorsky, J. Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods. J. Biol. Chem. 268:4534-4542; 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4534-4542
    • Tomarev, S.I.1    Zinovieva, R.D.2    Guo, K.3    Piatigorsky, J.4
  • 41
    • 0027289198 scopus 로고
    • The design of metal-binding sites in proteins
    • 41. Regan, L. The design of metal-binding sites in proteins. Annu. Rev. Biophys. Biomed. Struct. 22:257-281; 1993.
    • (1993) Annu. Rev. Biophys. Biomed. Struct. , vol.22 , pp. 257-281
    • Regan, L.1
  • 42
    • 0028132923 scopus 로고
    • Engineering of a metal coordinating site into human glutathione transferase M1-1 based on immobilized metal ion affinity chromatography of homologous rat enzymes
    • 42. Chaga, G.; Widersten, M.; Andersson, L.; Porath, J.; Danielson, U. H.; Mannervik, B. Engineering of a metal coordinating site into human glutathione transferase M1-1 based on immobilized metal ion affinity chromatography of homologous rat enzymes. Protein Eng. 7:1115-1119; 1994.
    • (1994) Protein Eng. , vol.7 , pp. 1115-1119
    • Chaga, G.1    Widersten, M.2    Andersson, L.3    Porath, J.4    Danielson, U.H.5    Mannervik, B.6
  • 43
    • 0011923885 scopus 로고
    • Glutathione-dependent enzymes - Glutathione S-transferases
    • Page, H. I.; William, A. eds. Cambridge: Royal Society of Chemistry
    • 43. Jakoby, W. B. Glutathione-dependent enzymes - Glutathione S-transferases. In: Page, H. I.; William, A. eds. Enzyme mechanism. Cambridge: Royal Society of Chemistry; 1987:468-476.
    • (1987) Enzyme Mechanism , pp. 468-476
    • Jakoby, W.B.1
  • 44
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • 44. Hilt, W.; Wolf, D. H. Proteasomes: Destruction as a programme. Trends Biochem. Sci. 21:96-102; 1996.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 45
    • 0029873387 scopus 로고    scopus 로고
    • Reactive oxygen species and programmed cell death
    • 45. Jacobson, M. D. Reactive oxygen species and programmed cell death. Trends Biochem. Sci. 21:83-86; 1996.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 83-86
    • Jacobson, M.D.1
  • 46
    • 0027209389 scopus 로고
    • Strategies of antioxidant defense
    • 46. Sies, H. Strategies of antioxidant defense. Eur. J. Biochem. 215:213-219; 1993.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 213-219
    • Sies, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.