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Volumn 19, Issue 12, 2006, Pages 1643-1649

Oxidative metabolism of seleno-L-methionine to L-methionine selenoxide by flavin-containing monooxygenases

Author keywords

[No Author keywords available]

Indexed keywords

1 BENZYLIMIDAZOLE; BENZENE DERIVATIVE; COMPLEMENTARY DNA; DEFEROXAMINE; DIMETHYLANILINE MONOOXYGENASE; DNA; FLAVIN CONTAINING MONOOXYGENASE 3; FLAVIN CONTAINING MONOOXYGENASE 5; FLAVIN CONTAININH MONOOXYGENASE 1; METHIONINE DERIVATIVE; METHIONINE SELENOXIDE; NITRO DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SELENIUM DERIVATIVE; SELENOMETHIONINE; SUPEROXIDE DISMUTASE;

EID: 33845735514     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx0601915     Document Type: Article
Times cited : (36)

References (40)
  • 2
    • 13444293451 scopus 로고    scopus 로고
    • Selenomethionine induces sustained ERK phosphorylation leading to cell-cycle arrest in human colon cancer cells
    • Goulet, A.-C., Chigbrow, M., Frisk, P., and Nelson, M. A. (2005) Selenomethionine induces sustained ERK phosphorylation leading to cell-cycle arrest in human colon cancer cells. Carcinogenesis 26, 109-117.
    • (2005) Carcinogenesis , vol.26 , pp. 109-117
    • Goulet, A.-C.1    Chigbrow, M.2    Frisk, P.3    Nelson, M.A.4
  • 5
    • 0033947985 scopus 로고    scopus 로고
    • Chemical speciation influences comparative activity of selenium-enriched garlic and yeast in mammary cancer prevention
    • Ip, C., Birringer, M., Block, E., Kotrebai, M., Tyson, J. F., Uden, P. C., and Lisk, D. J. (2000) Chemical speciation influences comparative activity of selenium-enriched garlic and yeast in mammary cancer prevention. J. Agric. Food Chem. 48, 2062-2070.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 2062-2070
    • Ip, C.1    Birringer, M.2    Block, E.3    Kotrebai, M.4    Tyson, J.F.5    Uden, P.C.6    Lisk, D.J.7
  • 6
    • 0342803623 scopus 로고    scopus 로고
    • Antioxidant associated chemoprevention by selenomethionine in murine tumor model
    • Mukhopadhyay-Sardar, S., Pada Rana, M., and Chatterjee, M. (2000) Antioxidant associated chemoprevention by selenomethionine in murine tumor model. Mol. Cell. Biochem. 206, 17-25.
    • (2000) Mol. Cell. Biochem. , vol.206 , pp. 17-25
    • Mukhopadhyay-Sardar, S.1    Pada Rana, M.2    Chatterjee, M.3
  • 7
    • 0027102036 scopus 로고
    • Absorption, distribution and elimination of selenium as L-selenomethionine in non-human primates
    • Willhite, C. C., Hawkes, W. C., Omaye, S. T., Choy, W. N., Cox, D. N., and Cukierski, M. J. (1992) Absorption, distribution and elimination of selenium as L-selenomethionine in non-human primates. Food Chem. Toxicol. 30, 903-913.
    • (1992) Food Chem. Toxicol. , vol.30 , pp. 903-913
    • Willhite, C.C.1    Hawkes, W.C.2    Omaye, S.T.3    Choy, W.N.4    Cox, D.N.5    Cukierski, M.J.6
  • 8
    • 0033924449 scopus 로고    scopus 로고
    • Selenomethionine: A review of its nutritional significance, metabolism and toxicity
    • Schrauzer, G. N. (2000) Selenomethionine: a review of its nutritional significance, metabolism and toxicity. J. Nutr. 130, 1653-1656.
    • (2000) J. Nutr. , vol.130 , pp. 1653-1656
    • Schrauzer, G.N.1
  • 10
    • 0035475596 scopus 로고    scopus 로고
    • Contribution of enzymic α,γ-elimination reaction in detoxification pathway of selenomethionine in mouse liver
    • Okuno, T., Kubota, T., Kuroda, T., Ueno, H., and Nakamuro, K. (2001) Contribution of enzymic α,γ-elimination reaction in detoxification pathway of selenomethionine in mouse liver. Toxicol. Appl. Pharmacol. 176, 18-23.
    • (2001) Toxicol. Appl. Pharmacol. , vol.176 , pp. 18-23
    • Okuno, T.1    Kubota, T.2    Kuroda, T.3    Ueno, H.4    Nakamuro, K.5
  • 12
    • 0023033147 scopus 로고
    • Chemical forms of selenium in rat tissues after administration of selenite or selenomethionine
    • Beilstein, M. A., and Whanger, P. D. (1986) Chemical forms of selenium in rat tissues after administration of selenite or selenomethionine. J. Nutr. 116, 1711-1719.
    • (1986) J. Nutr. , vol.116 , pp. 1711-1719
    • Beilstein, M.A.1    Whanger, P.D.2
  • 13
    • 0028245447 scopus 로고
    • Flavin-containing monooxygenase (FMO)-dependent metabolism of methionine and evidence for FMO3 being the major FMO involved in methionine sulfoxidation in rabbit liver and kidney microsomes
    • Duescher, R. J., Lawton, M. P., Philpot, R. M., and Elfarra, A. A. (1994) Flavin-containing monooxygenase (FMO)-dependent metabolism of methionine and evidence for FMO3 being the major FMO involved in methionine sulfoxidation in rabbit liver and kidney microsomes. J. Biol. Chem. 269, 17525-17530.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17525-17530
    • Duescher, R.J.1    Lawton, M.P.2    Philpot, R.M.3    Elfarra, A.A.4
  • 14
    • 0030249888 scopus 로고    scopus 로고
    • Characterization of the methionine S-oxidase activity of rat liver and kidney microsomes: Immunochemical and kinetic evidence for FMO3 being the major catalyst
    • Krause, R. J., Ripp, S. L., Sausen, P. J., Overby, L. H., Philpot, R. M., and Elfarra, A. A. (1996) Characterization of the methionine S-oxidase activity of rat liver and kidney microsomes: immunochemical and kinetic evidence for FMO3 being the major catalyst. Arch. Biochem. Biophys. 333, 109-116.
    • (1996) Arch. Biochem. Biophys. , vol.333 , pp. 109-116
    • Krause, R.J.1    Ripp, S.L.2    Sausen, P.J.3    Overby, L.H.4    Philpot, R.M.5    Elfarra, A.A.6
  • 15
    • 0032969264 scopus 로고    scopus 로고
    • Species and sex differences in expression of flavin-containing monooxygenase form 3 in liver and kidney microsomes
    • Ripp, S. L., Itagaki, K., Philpot, R. M., and Elfarra, A. A. (1999) Species and sex differences in expression of flavin-containing monooxygenase form 3 in liver and kidney microsomes. Drug Metab. Dispos. 27, 46-52.
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 46-52
    • Ripp, S.L.1    Itagaki, K.2    Philpot, R.M.3    Elfarra, A.A.4
  • 16
    • 0033566143 scopus 로고    scopus 로고
    • Methionine S-oxidation in human and rabbit liver microsomes: Evidence for a high-affinity methionine S-oxidase activity that is distinct from flavin-containing monooxygenase 3
    • Ripp, S. L., Itagaki, K., Philpot, R. M., and Elfarra, A. A. (1999) Methionine S-oxidation in human and rabbit liver microsomes: evidence for a high-affinity methionine S-oxidase activity that is distinct from flavin-containing monooxygenase 3. Arch. Biochem. Biophys. 367, 322-332.
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 322-332
    • Ripp, S.L.1    Itagaki, K.2    Philpot, R.M.3    Elfarra, A.A.4
  • 17
    • 0025262447 scopus 로고
    • Cysteine conjugate S-oxidase: Characterization of a novel enzymatic activity in rat hepatic and renal microsomes
    • Sausen, P. J., and Elfarra, A. A. (1990) Cysteine conjugate S-oxidase: characterization of a novel enzymatic activity in rat hepatic and renal microsomes. J. Biol. Chem. 265, 6139-6145.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6139-6145
    • Sausen, P.J.1    Elfarra, A.A.2
  • 18
    • 0019557316 scopus 로고
    • The Raman spectra of selenomethionine and selenocystine
    • Lopez, J., Jao, T. C., and Rudzinski, W. E. (1981) The Raman spectra of selenomethionine and selenocystine. J. Inorg. Biochem. 14, 177-181.
    • (1981) J. Inorg. Biochem. , vol.14 , pp. 177-181
    • Lopez, J.1    Jao, T.C.2    Rudzinski, W.E.3
  • 19
    • 0037407590 scopus 로고    scopus 로고
    • Combination of LC-ICP-MS, LC-MS and NMR for investigation of the oxidative degradation of selenomethionine
    • Gammelgaard, B., Cornett, C., Olsen, J., Bendahl, L., and Hansen, S. H. (2003) Combination of LC-ICP-MS, LC-MS and NMR for investigation of the oxidative degradation of selenomethionine. Talanta 59, 1165-1171.
    • (2003) Talanta , vol.59 , pp. 1165-1171
    • Gammelgaard, B.1    Cornett, C.2    Olsen, J.3    Bendahl, L.4    Hansen, S.H.5
  • 20
    • 0003168231 scopus 로고
    • 1H NMR study of the reaction of gold (III) with DL-seleno-melhionine in aqueous solution
    • 1H NMR study of the reaction of gold (III) with DL-seleno-melhionine in aqueous solution. Inorg. Chim. Acta. 80, L3-L4.
    • (1983) Inorg. Chim. Acta. , vol.80
    • Isab, A.1
  • 21
    • 0032080109 scopus 로고    scopus 로고
    • An NMR spectroscopic investigation of the oxidation reactions of DL-selenomethionine
    • Zainal, H. A., Wolf, W. R., and Waters, R. M. (1998) An NMR spectroscopic investigation of the oxidation reactions of DL-selenomethionine. J. Chem. Technol. Biotechnol. 72, 38-44.
    • (1998) J. Chem. Technol. Biotechnol. , vol.72 , pp. 38-44
    • Zainal, H.A.1    Wolf, W.R.2    Waters, R.M.3
  • 23
    • 0028268997 scopus 로고
    • Roles of cysteine conjugate β-lyase and S-oxidase in nephrotoxicity: Sludies with S-(1,2-dichlorovinyl)-L-cysteine and S-(1,2-dichlorovinyl)-L- cysleine sulfoxide
    • Lash, L. H., Sausen, P. J., Duescher, R. J., Cooley, A. J., and Elfarra, A. A. (1994) Roles of cysteine conjugate β-lyase and S-oxidase in nephrotoxicity: sludies with S-(1,2-dichlorovinyl)-L-cysteine and S-(1,2-dichlorovinyl)-L-cysleine sulfoxide. J. Pharmacol. Exp. Ther. 269, 374-383.
    • (1994) J. Pharmacol. Exp. Ther. , vol.269 , pp. 374-383
    • Lash, L.H.1    Sausen, P.J.2    Duescher, R.J.3    Cooley, A.J.4    Elfarra, A.A.5
  • 24
    • 0007614624 scopus 로고
    • Asymmetric oxidation of simple selenides to selenoxides in high entantiopurity. Stereochemical aspects of the allyl selenoxide/allyl selenenate rearrangement
    • Davis, F. A., and Reddy, R. T. (1992) Asymmetric oxidation of simple selenides to selenoxides in high entantiopurity. Stereochemical aspects of the allyl selenoxide/allyl selenenate rearrangement. J. Org. Chem. 57, 2599-2606.
    • (1992) J. Org. Chem. , vol.57 , pp. 2599-2606
    • Davis, F.A.1    Reddy, R.T.2
  • 25
    • 0000122353 scopus 로고
    • Configurational stability of optically active selenoxides; racemization via achiral hydrate
    • Shimizu, T., Kobayashi, M., and Kamigata, N. (1988) Configurational stability of optically active selenoxides; racemization via achiral hydrate. Bull. Chem. Soc. Jpn. 61, 3761-3763.
    • (1988) Bull. Chem. Soc. Jpn. , vol.61 , pp. 3761-3763
    • Shimizu, T.1    Kobayashi, M.2    Kamigata, N.3
  • 26
    • 0343652996 scopus 로고
    • Organoselenium Oxidations
    • (Trahanovsky, W. S., Ed.), Academic Press, Inc., New York
    • Reich, H. J. (1978) Organoselenium Oxidations. In Oxidation in Organic Chemistry Part C (Trahanovsky, W. S., Ed.) pp 1-33, Academic Press, Inc., New York.
    • (1978) Oxidation in Organic Chemistry Part C , pp. 1-33
    • Reich, H.J.1
  • 27
    • 0000513110 scopus 로고
    • Theoretical and experimental studies of regioselectivity in selenoxide elimination
    • Kondo, N., Fueno, H., Fujimoto, H., Makino, M., Nakaoka, H., Aoki, I., and Uemura, S. (1994) Theoretical and experimental studies of regioselectivity in selenoxide elimination. J. Org. Chem. 59, 5254-5263.
    • (1994) J. Org. Chem. , vol.59 , pp. 5254-5263
    • Kondo, N.1    Fueno, H.2    Fujimoto, H.3    Makino, M.4    Nakaoka, H.5    Aoki, I.6    Uemura, S.7
  • 28
    • 12844253749 scopus 로고    scopus 로고
    • Potential roles of flavin-containing monooxygenases in sulfoxidation reactions of L-methionine, N-acetyl-L-methionine and peptides containing L-methionine
    • Elfarra, A. A., and Krause, R. J. (2005) Potential roles of flavin-containing monooxygenases in sulfoxidation reactions of L-methionine, N-acetyl-L-methionine and peptides containing L-methionine. Biochim. Biophys. Acta 1703, 183-189.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 183-189
    • Elfarra, A.A.1    Krause, R.J.2
  • 29
    • 0030893969 scopus 로고    scopus 로고
    • Oxidation of cysteine S-conjugates by rabbit liver microsomes and cDNA-expressed flavin-containing monooxygenases: Studies with S-(1,2-dichlorovinyl)-L-cysleine, S-(1,2,2-trichlorovinyl)-L-cysteine, S-allyl-L-cysteine, and S-benzyl-L-cysteine
    • Ripp, S. L., Overby, L. H., Philpot, R. M., and Elfarra, A. A. (1997) Oxidation of cysteine S-conjugates by rabbit liver microsomes and cDNA-expressed flavin-containing monooxygenases: studies with S-(1,2-dichlorovinyl)-L- cysleine, S-(1,2,2-trichlorovinyl)-L-cysteine, S-allyl-L-cysteine, and S-benzyl-L-cysteine. Mol. Pharmacol. 51, 507-515.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 507-515
    • Ripp, S.L.1    Overby, L.H.2    Philpot, R.M.3    Elfarra, A.A.4
  • 30
    • 0028147745 scopus 로고
    • Liver microsome and flavin-containing monooxygenase catalyzed oxidation of organic selenium compounds
    • Chen, G.-P., and Ziegler, D. M. (1994) Liver microsome and flavin-containing monooxygenase catalyzed oxidation of organic selenium compounds. Arch. Biochem. Biophys. 312, 566-572.
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 566-572
    • Chen, G.-P.1    Ziegler, D.M.2
  • 31
    • 0346880022 scopus 로고    scopus 로고
    • N-Glycosylation of pig flavin-containing monooxygenase form 1: Determination of the site of protein modification by mass spectrometry
    • Korsmeyer, K. K., Guan, S., Yang, Z.-C., Falick, A., Ziegler, D. M., and Cashman, J. R. (1998) N-Glycosylation of pig flavin-containing monooxygenase form 1: determination of the site of protein modification by mass spectrometry. Chem. Res. Toxicol. 9, 1183-1193.
    • (1998) Chem. Res. Toxicol. , vol.9 , pp. 1183-1193
    • Korsmeyer, K.K.1    Guan, S.2    Yang, Z.-C.3    Falick, A.4    Ziegler, D.M.5    Cashman, J.R.6
  • 33
    • 0019205736 scopus 로고
    • S-Adenosylmethionine synthetase from Escherichia coli
    • Markman, G. D., Hafner, E. W., Tabor, C. W., and Tabor, H. (1980) S-Adenosylmethionine synthetase from Escherichia coli. J. Biol. Chem. 255, 9082-9092.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9082-9092
    • Markman, G.D.1    Hafner, E.W.2    Tabor, C.W.3    Tabor, H.4
  • 34
    • 0000357778 scopus 로고
    • Interactions of methionine and selenomethionine with methionine adenosyltransferase and ethylene-generating systems
    • Konze, J. R., and Kende, H. (1979) Interactions of methionine and selenomethionine with methionine adenosyltransferase and ethylene-generating systems. Plant Physiol. 63, 507-510.
    • (1979) Plant Physiol. , vol.63 , pp. 507-510
    • Konze, J.R.1    Kende, H.2
  • 35
    • 0018782904 scopus 로고
    • Catalytic action of L-methionine γ-lyase on selenomethionine and selenols
    • Esaki, N., Tanaka, H., Uemura, S., Suzuki, T., and Soda, K. (1979) Catalytic action of L-methionine γ-lyase on selenomethionine and selenols. Biochemistry 18, 407-410.
    • (1979) Biochemistry , vol.18 , pp. 407-410
    • Esaki, N.1    Tanaka, H.2    Uemura, S.3    Suzuki, T.4    Soda, K.5
  • 36
    • 0026568910 scopus 로고
    • NADPH-dependent oxidation of reduced ebselen, 2-selenylbenzanilide, and 2-(methylseleno)benzanilide catalyzed by pig liver flavin-containing monooxygenase
    • Ziegler, D. M., Graf, P., Poulsen, L. L., Stahl, W., and Sies, H. (1992) NADPH-dependent oxidation of reduced ebselen, 2-selenylbenzanilide, and 2-(methylseleno)benzanilide catalyzed by pig liver flavin-containing monooxygenase. Chem. Res. Toxicol. 5, 163-166.
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 163-166
    • Ziegler, D.M.1    Graf, P.2    Poulsen, L.L.3    Stahl, W.4    Sies, H.5
  • 37
    • 0028225059 scopus 로고
    • Oxidation of dimethylselenide to dimethylselenoxide by microsomes from rat liver and lung and by flavin containing monooxygenase from pig liver
    • Goeger, D. E., and Ganther, H. E. (1994) Oxidation of dimethylselenide to dimethylselenoxide by microsomes from rat liver and lung and by flavin containing monooxygenase from pig liver. Arch. Biochem. Biophys. 310, 448-451.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 448-451
    • Goeger, D.E.1    Ganther, H.E.2
  • 38
    • 0035152383 scopus 로고    scopus 로고
    • Selenoxidation by flavin-containing monooxygenases as a novel pathway for β-elimination of selenocysteine Se-conjugates
    • Rooseboom, M., Commandeur, J. N. M., Floor, G. C., Rettie, A. E., and Vermeulen, N. P. E. (2001) Selenoxidation by flavin-containing monooxygenases as a novel pathway for β-elimination of selenocysteine Se-conjugates. Chem. Res. Toxicol. 14, 127-134.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 127-134
    • Rooseboom, M.1    Commandeur, J.N.M.2    Floor, G.C.3    Rettie, A.E.4    Vermeulen, N.P.E.5
  • 39
    • 0031819753 scopus 로고    scopus 로고
    • Reduction of methionine selenoxide to selenomethionine by glutathione
    • Assmann, A., Briviba, K., and Sies, H. (1998) Reduction of methionine selenoxide to selenomethionine by glutathione. Arch. Biochem. Biophys. 349, 201-203.
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 201-203
    • Assmann, A.1    Briviba, K.2    Sies, H.3


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