메뉴 건너뛰기




Volumn 368, Issue 1, 2002, Pages 253-261

Mitochondrial aspartate aminotransferase catalyses cysteine S-conjugate β-lyase reactions

Author keywords

Halogenated alkenes; Mitochondrial toxicity; S (1,1,2,2 tetrafluoroethyl) L cysteine; S (1,2 dichlorovinyl) L cysteine; Thioacylating fragments

Indexed keywords

CATALYSIS; ENZYMES; HALOGENATION; TOXICITY;

EID: 0037113250     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020531     Document Type: Article
Times cited : (37)

References (47)
  • 1
    • 0026079136 scopus 로고
    • Bioactivation of xenobiotics by formation of toxic glutathione conjugates
    • Koob, M. and Dekant, W. (1991) Bioactivation of xenobiotics by formation of toxic glutathione conjugates. Chem. Biol. Interact. 77, 107-136
    • (1991) Chem. Biol. Interact. , vol.77 , pp. 107-136
    • Koob, M.1    Dekant, W.2
  • 2
    • 0028315145 scopus 로고
    • Enzymology of cysteine S-conjugate β-lyases
    • Cooper, A. J. L. (1994) Enzymology of cysteine S-conjugate β-lyases. Adv. Pharmacol. 27, 71-113
    • (1994) Adv. Pharmacol. , vol.27 , pp. 71-113
    • Cooper, A.J.L.1
  • 3
    • 0028190695 scopus 로고
    • Formation and fate of nephrotoxic and cytotoxic glutathione S-conjugates: Cysteine conjugate β-lyase pathway
    • Dekant, W., Vamvakas, S. and Anders, M. W. (1994) Formation and fate of nephrotoxic and cytotoxic glutathione S-conjugates: Cysteine conjugate β-lyase pathway. Adv. Pharmacol. 27, 115-162
    • (1994) Adv. Pharmacol. , vol.27 , pp. 115-162
    • Dekant, W.1    Vamvakas, S.2    Anders, M.W.3
  • 4
    • 0031616701 scopus 로고    scopus 로고
    • Mechanism of cysteine S-conjugate β-lyases
    • Cooper, A. J. L. (1998) Mechanism of cysteine S-conjugate β-lyases. Adv. Enzymol. 72, 199-238
    • (1998) Adv. Enzymol. , vol.72 , pp. 199-238
    • Cooper, A.J.L.1
  • 5
    • 0031748545 scopus 로고    scopus 로고
    • Glutathione-dependent bioactivation of haloalkenes
    • Anders, M. W. and Dekant, W. (1998) Glutathione-dependent bioactivation of haloalkenes. Annu. Rev Pharmacol. Toxicol. 38, 501-537
    • (1998) Annu. Rev Pharmacol. Toxicol. , vol.38 , pp. 501-537
    • Anders, M.W.1    Dekant, W.2
  • 6
    • 0037103561 scopus 로고    scopus 로고
    • Toxic halogenated cysteine S-conjugates and targeting of mitochondrial enzymes of energy metabolism
    • Cooper, A. J. L., Bruschi, S. A. and Anders, M. W. (2002) Toxic halogenated cysteine S-conjugates and targeting of mitochondrial enzymes of energy metabolism. Biochem. Pharmacol. 64, 553-564
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 553-564
    • Cooper, A.J.L.1    Bruschi, S.A.2    Anders, M.W.3
  • 7
    • 0027491608 scopus 로고
    • Mitochondrial HSP60 (P1 protein) and HSP70-like protein (mortalin) are major targets for modification during S-(1,1,2,2-tetrafluoroethyl)-L-cysteine-induced toxicity
    • Bruschi, S. A., West, K. A., Crabb, J. W., Gupta, R. S. and Stevens, J. L. (1993) Mitochondrial HSP60 (P1 protein) and HSP70-like protein (mortalin) are major targets for modification during S-(1,1,2,2-tetrafluoroethyl)-L-cysteine-induced toxicity. J. Biol. Chem. 268, 23157-23161
    • (1993) J. Biol. Chem. , vol.268 , pp. 23157-23161
    • Bruschi, S.A.1    West, K.A.2    Crabb, J.W.3    Gupta, R.S.4    Stevens, J.L.5
  • 8
    • 0032506133 scopus 로고    scopus 로고
    • Mitochondrial stress protein recognition of inactivated dehydrogenases during mammalian cell death
    • Bruschi, S. A., Lindsay, J. G. and Crabb, J. W. (1998) Mitochondrial stress protein recognition of inactivated dehydrogenases during mammalian cell death. Proc. Natl. Acad. Sci. U.S.A. 95, 13413-13418
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13413-13418
    • Bruschi, S.A.1    Lindsay, J.G.2    Crabb, J.W.3
  • 9
    • 0037188397 scopus 로고    scopus 로고
    • Mitochondrial aconitase modification, functional inhibition, and evidence for a supramolecular complex of the TCA cycle by the renal toxicant S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
    • James, E. A., Gygi, S. P., Adams, M. L., Pierce, R. H., Fausto, N., Aebersold, R. H., Nelson, S. D. and Bruschi, S. A. (2002) Mitochondrial aconitase modification, functional inhibition, and evidence for a supramolecular complex of the TCA cycle by the renal toxicant S-(1,1,2,2-tetrafluoroethyl)-L-cysteine. Biochemistry 41, 6789-6797
    • (2002) Biochemistry , vol.41 , pp. 6789-6797
    • James, E.A.1    Gygi, S.P.2    Adams, M.L.3    Pierce, R.H.4    Fausto, N.5    Aebersold, R.H.6    Nelson, S.D.7    Bruschi, S.A.8
  • 10
    • 0032879644 scopus 로고    scopus 로고
    • Inhibition of select mitochondrial enzymes in PC12 cells exposed to S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
    • Park, L. C. H., Gibson, G. E., Bunik, V. and Cooper, A. J. L. (1999) Inhibition of select mitochondrial enzymes in PC12 cells exposed to S-(1,1,2,2-tetrafluoroethyl)-L-cysteine. Biochem. Pharmacol, 58, 1557-1565
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 1557-1565
    • Park, L.C.H.1    Gibson, G.E.2    Bunik, V.3    Cooper, A.J.L.4
  • 11
    • 0015120455 scopus 로고
    • 2-Oxoacid dehydrogenases of rat liver mitochondria as the site of action of S-(1,2-dichlorovinyl)-L-cysteine and S-(1,2-dichlorovinyl)-3-propionic acid
    • Stonard, M. D. and Parker, V. H. (1971) 2-Oxoacid dehydrogenases of rat liver mitochondria as the site of action of S-(1,2-dichlorovinyl)-L-cysteine and S-(1,2-dichlorovinyl)-3-propionic acid. Biochem. Pharmacol. 20, 2417-2427
    • (1971) Biochem. Pharmacol. , vol.20 , pp. 2417-2427
    • Stonard, M.D.1    Parker, V.H.2
  • 12
    • 0019459812 scopus 로고
    • Renal transtubular transport of mercapturic acid in vivo
    • Inoue, M., Okajima, K. and Morino, Y. (1981) Renal transtubular transport of mercapturic acid in vivo. Biochim. Biophys. Acta 641, 122-128
    • (1981) Biochim. Biophys. Acta , vol.641 , pp. 122-128
    • Inoue, M.1    Okajima, K.2    Morino, Y.3
  • 13
    • 0020265930 scopus 로고
    • Metabolic coordination of liver and kidney in mercapturic acid biosynthesis in vivo
    • Inoue, M., Okajima, K. and Morino, Y. (1982) Metabolic coordination of liver and kidney in mercapturic acid biosynthesis in vivo. Hepatology (N.Y.) 2, 311-316
    • (1982) Hepatology (N.Y.) , vol.2 , pp. 311-316
    • Inoue, M.1    Okajima, K.2    Morino, Y.3
  • 14
    • 0034753085 scopus 로고    scopus 로고
    • Mercapturic acids (N-acetylcysteine S-conjugates) as endogenous substrates for the renal organic anion transporter-1
    • Pombrio, J. M., Giangreco, A., Li, L., Wempe, M. F., Anders, M. W., Sweet, D. H., Pritchard, J. B. and Ballatori, N. (2001) Mercapturic acids (N-acetylcysteine S-conjugates) as endogenous substrates for the renal organic anion transporter-1. Mol. Pharmacol 60, 1091-1099
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1091-1099
    • Pombrio, J.M.1    Giangreco, A.2    Li, L.3    Wempe, M.F.4    Anders, M.W.5    Sweet, D.H.6    Pritchard, J.B.7    Ballatori, N.8
  • 15
    • 0034084534 scopus 로고    scopus 로고
    • Immunohistochemical localization of the acylases that catalyze the deacetylation of haloalkene-derived mercapturates
    • Uttamsingh, V., Baggs, R. B., Krenitsky, D. M. and Anders, M. W. (2000) Immunohistochemical localization of the acylases that catalyze the deacetylation of haloalkene-derived mercapturates. Drug Metab. Dispos. 28, 625-632
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 625-632
    • Uttamsingh, V.1    Baggs, R.B.2    Krenitsky, D.M.3    Anders, M.W.4
  • 16
    • 0024268840 scopus 로고
    • Nephrotoxicity of mercapturic acids of three structurally related 2,2-difluoroethylenes in the rat. Indication for different bioactivation mechanisms
    • Commandeur, J. N. M., Brakenhoff, J. P., De Kanter, F. J. and Vermeulen, N. P. E. (1988) Nephrotoxicity of mercapturic acids of three structurally related 2,2-difluoroethylenes in the rat. Indication for different bioactivation mechanisms. Biochem. Pharmacol. 37, 4495-4504
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 4495-4504
    • Commandeur, J.N.M.1    Brakenhoff, J.P.2    De Kanter, F.J.3    Vermeulen, N.P.E.4
  • 17
    • 0031842003 scopus 로고    scopus 로고
    • The nephrotoxicity and hepatotoxicity of 1,1,2,2-tetrafluoroethyl)-L-cysteine in the rat
    • Lock, E. A. and Ishmael, J. (1998) The nephrotoxicity and hepatotoxicity of 1,1,2,2-tetrafluoroethyl)-L-cysteine in the rat. Arch. Toxicol. 72, 347-354
    • (1998) Arch. Toxicol. , vol.72 , pp. 347-354
    • Lock, E.A.1    Ishmael, J.2
  • 18
    • 0029801976 scopus 로고    scopus 로고
    • Inactivation of brain and kidney aspartate aminotransferases by S-(1,2-dichlorovinyl)-L-cysteine and by S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
    • Kato, Y., Asano, Y. and Cooper, A. J. L. (1996) Inactivation of brain and kidney aspartate aminotransferases by S-(1,2-dichlorovinyl)-L-cysteine and by S-(1,1,2,2-tetrafluoroethyl)-L-cysteine. Dev. Neurosci. (Basel) 18, 505-514
    • (1996) Dev. Neurosci. (Basel) , vol.18 , pp. 505-514
    • Kato, Y.1    Asano, Y.2    Cooper, A.J.L.3
  • 19
    • 0027535518 scopus 로고
    • Protein folding in a cell-free translation system. The fate of the precursor to mitochondrial aspartate aminotransferase
    • Mattingly, Jr, J. R., Youssef, J., Iriarte, A. and Martinez-Carrion, M. (1993) Protein folding in a cell-free translation system. The fate of the precursor to mitochondrial aspartate aminotransferase. J. Biol. Chem. 268, 3925-3937
    • (1993) J. Biol. Chem. , vol.268 , pp. 3925-3937
    • Mattingly J.R., Jr.1    Youssef, J.2    Iriarte, A.3    Martinez-Carrion, M.4
  • 21
    • 0025261923 scopus 로고
    • Cysteine conjugate toxicity, metabolism, and binding to macromolecules in isolated rat kidney mitochondria
    • Hayden, P. J. and Stevens, J. L. (1990) Cysteine conjugate toxicity, metabolism, and binding to macromolecules in isolated rat kidney mitochondria. Mol. Pharmacol. 37, 468-476
    • (1990) Mol. Pharmacol. , vol.37 , pp. 468-476
    • Hayden, P.J.1    Stevens, J.L.2
  • 24
    • 0001738080 scopus 로고
    • Kinetic studies of glutamic oxaloacetic transaminase isozymes
    • Henson, C. P. and Cleland, W. W. (1964) Kinetic studies of glutamic oxaloacetic transaminase isozymes. Biochemistry 3, 338-345
    • (1964) Biochemistry , vol.3 , pp. 338-345
    • Henson, C.P.1    Cleland, W.W.2
  • 25
    • 0014670822 scopus 로고
    • Distinctions in the equilibrium kinetic constants of the mitochondrial and supernatant isozymes of aspartate transaminase
    • Michuda, C. M. and Martinez-Carrion, M. (1969) Distinctions in the equilibrium kinetic constants of the mitochondrial and supernatant isozymes of aspartate transaminase. J. Biol. Chem. 244, 5920-5927
    • (1969) J. Biol. Chem. , vol.244 , pp. 5920-5927
    • Michuda, C.M.1    Martinez-Carrion, M.2
  • 26
    • 0014599101 scopus 로고
    • The reaction of L-serine O-sulfate with aspartate aminotransferase
    • John, R. A. and Fasella, P. (1969) The reaction of L-serine O-sulfate with aspartate aminotransferase. Biochemistry 8, 4477-4482
    • (1969) Biochemistry , vol.8 , pp. 4477-4482
    • John, R.A.1    Fasella, P.2
  • 27
    • 0015852240 scopus 로고
    • The protective effect of thiosulfate upon the inactivation of aspartate aminotransferase by aminoacrylic-acid-producing substrates
    • Cavallini, D., Federici, G., Bossa, F. and Granata, F. (1973) The protective effect of thiosulfate upon the inactivation of aspartate aminotransferase by aminoacrylic-acid-producing substrates. Eur. J. Biochem. 39, 301-304
    • (1973) Eur. J. Biochem. , vol.39 , pp. 301-304
    • Cavallini, D.1    Federici, G.2    Bossa, F.3    Granata, F.4
  • 28
    • 0027228292 scopus 로고
    • Cysteine conjugate toxicity in a human cell line: Correlation with C-S lyase activity in human hepatic tissues
    • Buckberry, L. D., Blagbrough, I. S. and Shaw, P. N. (1993) Cysteine conjugate toxicity in a human cell line: Correlation with C-S lyase activity in human hepatic tissues. Hum. Exp. Toxicol. 12, 329-335
    • (1993) Hum. Exp. Toxicol. , vol.12 , pp. 329-335
    • Buckberry, L.D.1    Blagbrough, I.S.2    Shaw, P.N.3
  • 33
    • 0021062309 scopus 로고
    • Use of β-methylene-DLaspartate to assess the role of aspartate aminotransferase in cerebral oxidative metabolism
    • Fitzpatrick, S. M., Cooper, A. J. L. and Duffy, T. E. (1983) Use of β-methylene-DLaspartate to assess the role of aspartate aminotransferase in cerebral oxidative metabolism. J. Neurochem. 41, 1370-1383
    • (1983) J. Neurochem. , vol.41 , pp. 1370-1383
    • Fitzpatrick, S.M.1    Cooper, A.J.L.2    Duffy, T.E.3
  • 34
    • 0034161474 scopus 로고    scopus 로고
    • Macromolecular interactions: Tracing the roots
    • Srere, P. A. (2000) Macromolecular interactions: Tracing the roots. Trends Biol. Sci. 25, 150-153
    • (2000) Trends Biol. Sci. , vol.25 , pp. 150-153
    • Srere, P.A.1
  • 35
    • 0019434980 scopus 로고
    • Role of the malate-aspartate shuttle in renal sodium transport in the rat
    • Ross, B., Silva, P. and Bullock, S. (1981) Role of the malate-aspartate shuttle in renal sodium transport in the rat. Clin. Sci. (London) 60, 419-426
    • (1981) Clin. Sci. (London) , vol.60 , pp. 419-426
    • Ross, B.1    Silva, P.2    Bullock, S.3
  • 36
    • 0015930539 scopus 로고
    • Labeling of the active site of cytoplasmic aspartate aminotransferase by β-chloro-L-alanine
    • Morino, Y. and Okamoto, M. (1973) Labeling of the active site of cytoplasmic aspartate aminotransferase by β-chloro-L-alanine. Biochem. Biophys. Res. Commun. 50, 1061-1067
    • (1973) Biochem. Biophys. Res. Commun. , vol.50 , pp. 1061-1067
    • Morino, Y.1    Okamoto, M.2
  • 37
    • 0016286734 scopus 로고
    • Formate-induced labeling of the active site of aspartate aminotransferase by β-chloro-L-alanine
    • Morino, Y., Osman, A. M. and Okamoto, M. (1974) Formate-induced labeling of the active site of aspartate aminotransferase by β-chloro-L-alanine. J. Biol. Chem. 249, 6684-6692
    • (1974) J. Biol. Chem. , vol.249 , pp. 6684-6692
    • Morino, Y.1    Osman, A.M.2    Okamoto, M.3
  • 38
    • 0015239516 scopus 로고
    • Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase
    • Miller, J. E. and Litwack, G. (1971) Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase. J. Biol. Chem. 246, 3234-3240
    • (1971) J. Biol. Chem. , vol.246 , pp. 3234-3240
    • Miller, J.E.1    Litwack, G.2
  • 39
    • 0015522899 scopus 로고
    • Evidence of phenylalanine transaminase activity in the isozymes of aspartate aminotransferase
    • Shrawder, E. and Martinez-Carrion, M. (1972) Evidence of phenylalanine transaminase activity in the isozymes of aspartate aminotransferase. J. Biol. Chem. 247, 2486-2492
    • (1972) J. Biol. Chem. , vol.247 , pp. 2486-2492
    • Shrawder, E.1    Martinez-Carrion, M.2
  • 40
    • 0017897372 scopus 로고
    • β-Elimination of β-halo substrates by D-amino acid transaminase associated with inactivation of the enzyme. Trapping of key intermediates in the reaction
    • Soper, T. S. and Manning, J. M. (1978) β-Elimination of β-halo substrates by D-amino acid transaminase associated with inactivation of the enzyme. Trapping of key intermediates in the reaction. Biochemistry 17, 3377-3384
    • (1978) Biochemistry , vol.17 , pp. 3377-3384
    • Soper, T.S.1    Manning, J.M.2
  • 41
    • 0020494539 scopus 로고
    • A novel reaction of the coenzyme of glutamate decarboxylase with serine O-sulfate
    • Likos, J. J., Ueno, H., Feldhaus, R. W. and Metzler, D. E. (1982) A novel reaction of the coenzyme of glutamate decarboxylase with serine O-sulfate. Biochemistry 21, 4377-4386
    • (1982) Biochemistry , vol.21 , pp. 4377-4386
    • Likos, J.J.1    Ueno, H.2    Feldhaus, R.W.3    Metzler, D.E.4
  • 42
    • 0020494540 scopus 로고
    • Chemistry of the inactivation of cytosolic aspartate aminotransferase by serine O-sulfate
    • Ueno, H., Likos, J. J. and Metzler, D. E. (1982) Chemistry of the inactivation of cytosolic aspartate aminotransferase by serine O-sulfate. Biochemistry 21, 4387-4393
    • (1982) Biochemistry , vol.21 , pp. 4387-4393
    • Ueno, H.1    Likos, J.J.2    Metzler, D.E.3
  • 43
    • 0023264679 scopus 로고
    • Separate enzymatic microassays for aspartate aminotransferase isozymes
    • Parli, J. A., Godfrey, D. A. and Ross, C. D. (1987) Separate enzymatic microassays for aspartate aminotransferase isozymes. Biochim. Biophys. Acta 925, 175-184
    • (1987) Biochim. Biophys. Acta , vol.925 , pp. 175-184
    • Parli, J.A.1    Godfrey, D.A.2    Ross, C.D.3
  • 44
    • 0018770465 scopus 로고
    • Distribution of two aminotransferases and D-amino acid oxidase within the nephron of young and adult rats
    • Chan, A. W., Perry, S. G., Burch, H. B., Fagioli, S., Alvey, T. R. and Lowry, O. H. (1979) Distribution of two aminotransferases and D-amino acid oxidase within the nephron of young and adult rats. J. Histochem. Cytochem. 27, 751-755
    • (1979) J. Histochem. Cytochem. , vol.27 , pp. 751-755
    • Chan, A.W.1    Perry, S.G.2    Burch, H.B.3    Fagioli, S.4    Alvey, T.R.5    Lowry, O.H.6
  • 45
    • 0022979951 scopus 로고
    • A purified cysteine conjugate β-lyase from rat kidney cytosol. Requirement for an α-keto acid or an amino acid oxidase for activity and identity with soluble glutamine transaminase K
    • Stevens, J. L., Robbins, J. D. and Byrd, R. A. (1986) A purified cysteine conjugate β-lyase from rat kidney cytosol. Requirement for an α-keto acid or an amino acid oxidase for activity and identity with soluble glutamine transaminase K. J. Biol. Chem. 261, 15529-15537
    • (1986) J. Biol. Chem. , vol.261 , pp. 15529-15537
    • Stevens, J.L.1    Robbins, J.D.2    Byrd, R.A.3
  • 46
    • 0026698788 scopus 로고
    • Glutamate-malate metabolism in liver mitochondria. A model constructed on the basis of mitochondrial levels of enzymes, specificity, dissociation constants, and the stoichiometry of hetero-enzyme complexes
    • Fahien, L. A. and Teller, J. K. (1992) Glutamate-malate metabolism in liver mitochondria. A model constructed on the basis of mitochondrial levels of enzymes, specificity, dissociation constants, and the stoichiometry of hetero-enzyme complexes. J. Biol. Chem. 267, 10411-10422
    • (1992) J. Biol. Chem. , vol.267 , pp. 10411-10422
    • Fahien, L.A.1    Teller, J.K.2
  • 47
    • 0036110361 scopus 로고    scopus 로고
    • Immunogold localization of mitochondrial aspartate aminotransferase in mitochondria and on the cell surface in normal rat tissues
    • Cechetto, J. D., Sadacharan, S. K., Berk, P. D. and Gupta, R. S. (2002) Immunogold localization of mitochondrial aspartate aminotransferase in mitochondria and on the cell surface in normal rat tissues. Histol. Histopathol. 17, 353-364
    • (2002) Histol. Histopathol. , vol.17 , pp. 353-364
    • Cechetto, J.D.1    Sadacharan, S.K.2    Berk, P.D.3    Gupta, R.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.