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Volumn 127, Issue 6, 2000, Pages 1041-1046

Inhibitory effects of 1,4-naphthoquinone derivatives on rat cytochrome P4501A1-dependent monooxygenase activity in recombinant yeast microsomes

Author keywords

1,4 naphthoquinone; Cytochrome P450; Inhibition; Monooxygenase; NADPH cytochrome P450 reductase

Indexed keywords

1,4 NAPHTHOQUINONE DERIVATIVE; 7 ETHOXYCOUMARIN DEETHYLASE; ETHOXYRESORUFIN DEETHYLASE; UNSPECIFIC MONOOXYGENASE;

EID: 0033938614     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022695     Document Type: Article
Times cited : (12)

References (24)
  • 2
    • 0006661112 scopus 로고
    • Antihemorrhagic activity of simple compounds
    • Tishler, M. and Sampson, W.L. (1939) Antihemorrhagic activity of simple compounds. J. Am. Chem. Soc. 61, 2563-2564
    • (1939) J. Am. Chem. Soc. , vol.61 , pp. 2563-2564
    • Tishler, M.1    Sampson, W.L.2
  • 4
    • 0014121439 scopus 로고
    • Specificity of naphthoquinones as cofactor for NADPH oxidation by liver microsomes
    • Nishibayashi, H., Nakai, N., and Sato, R. (1967) Specificity of naphthoquinones as cofactor for NADPH oxidation by liver microsomes. J. Biochem. 62, 215-222
    • (1967) J. Biochem. , vol.62 , pp. 215-222
    • Nishibayashi, H.1    Nakai, N.2    Sato, R.3
  • 5
    • 0014667960 scopus 로고
    • One-electron-transfer reactions in biochemical systems III. One-electron reduction of quinones by microsomal flavin enzymes
    • Iyanagi, T. and Yamasaki, I. (1969) One-electron-transfer reactions in biochemical systems III. One-electron reduction of quinones by microsomal flavin enzymes. Biochim. Biophys. Acta 172, 370-3826
    • (1969) Biochim. Biophys. Acta , vol.172 , pp. 370-3826
    • Iyanagi, T.1    Yamasaki, I.2
  • 7
    • 0024498044 scopus 로고
    • DT-diaphorase-catalyzed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates
    • Buffinton, G.D., Öllinger, K., Brunmark, A., and Cadenas, E. (1989) DT-diaphorase-catalyzed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates. Biochem. J. 257, 561-571
    • (1989) Biochem. J. , vol.257 , pp. 561-571
    • Buffinton, G.D.1    Öllinger, K.2    Brunmark, A.3    Cadenas, E.4
  • 8
    • 0033610054 scopus 로고    scopus 로고
    • Inhibitory effects of vitamin A and vitamin K on rat cytochrome P4501A1-dependent monooxygenase activity
    • Inouye, K., Mae, T., Kondo, S., and Ohkawa, H. (1999) Inhibitory effects of vitamin A and vitamin K on rat cytochrome P4501A1-dependent monooxygenase activity. Biochem. Biophys. Res. Commun. 262, 565-569
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 565-569
    • Inouye, K.1    Mae, T.2    Kondo, S.3    Ohkawa, H.4
  • 9
    • 0030006304 scopus 로고    scopus 로고
    • Induction of cytochrome P4501A1 by 2,3,7,8-tetrachloro dibenzo-p-dioxin or indolo(2,3-b)carbazole is associated with oxidative DNA damage
    • Park, J.-Y.K., Shigenaga, M.K., and Ames, B.N. (1996) Induction of cytochrome P4501A1 by 2,3,7,8-tetrachloro dibenzo-p-dioxin or indolo(2,3-b)carbazole is associated with oxidative DNA damage. Proc. Natl. Acad. Sci. USA 93, 2322-2327
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2322-2327
    • Park, J.-Y.K.1    Shigenaga, M.K.2    Ames, B.N.3
  • 11
    • 0025914145 scopus 로고
    • Genetic linkage of lung cancer-associated MspI polymorphisms with amino acid replacement in the heme binding region of the human cytochrome P4501A1 gene
    • Hayashi, S., Watanabe, J., Nakachi, K., and Kawajiri, K. (1991) Genetic linkage of lung cancer-associated MspI polymorphisms with amino acid replacement in the heme binding region of the human cytochrome P4501A1 gene. J. Biochem. 110, 407-411
    • (1991) J. Biochem. , vol.110 , pp. 407-411
    • Hayashi, S.1    Watanabe, J.2    Nakachi, K.3    Kawajiri, K.4
  • 12
    • 0028308783 scopus 로고
    • Kinetic studies on a genetically engineered fused enzyme between rat cytochrome P4501A1 and yeast NADPH-P450 reductase
    • Sakaki, T., Kominami, S., Takemori, S., Ohkawa, H., Akiyoshi-Shibata, M., and Yabusaki, Y. (1994) Kinetic studies on a genetically engineered fused enzyme between rat cytochrome P4501A1 and yeast NADPH-P450 reductase. Biochemistry 33, 4933-4939
    • (1994) Biochemistry , vol.33 , pp. 4933-4939
    • Sakaki, T.1    Kominami, S.2    Takemori, S.3    Ohkawa, H.4    Akiyoshi-Shibata, M.5    Yabusaki, Y.6
  • 13
    • 0025225573 scopus 로고
    • Expression of cloned yeast NADPH-cytochrome P450 reductase gene in Saccharomyces cerevisiae
    • Murakami, H., Yabusaki, Y., Sakaki, T., Shibata, M., and Ohkawa, H. (1990) Expression of cloned yeast NADPH-cytochrome P450 reductase gene in Saccharomyces cerevisiae. J. Biochem. 108, 859-865
    • (1990) J. Biochem. , vol.108 , pp. 859-865
    • Murakami, H.1    Yabusaki, Y.2    Sakaki, T.3    Shibata, M.4    Ohkawa, H.5
  • 14
    • 0033551262 scopus 로고    scopus 로고
    • Electrostatic interaction between cytochrome P450 and NADPH-P450 reductase: Comparison of mixed and fused systems consisting of cytochrome P4501A1 and yeast NADPH-P450 reductase
    • Kondo, S., Sakaki, T., Ohkawa, H. and Inouye, K. (1999) Electrostatic interaction between cytochrome P450 and NADPH-P450 reductase: Comparison of mixed and fused systems consisting of cytochrome P4501A1 and yeast NADPH-P450 reductase. Biochem. Biophys. Res. Commun. 257, 273-278
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 273-278
    • Kondo, S.1    Sakaki, T.2    Ohkawa, H.3    Inouye, K.4
  • 15
    • 0017190574 scopus 로고
    • Determination of the best-fit values of kinetic parameters of the Michelis-Menten equation by the method of least squares with the Taylor expansion
    • Sakoda, M. and Hiromi, K. (1976) Determination of the best-fit values of kinetic parameters of the Michelis-Menten equation by the method of least squares with the Taylor expansion. J. Biochem. 80, 547-555
    • (1976) J. Biochem. , vol.80 , pp. 547-555
    • Sakoda, M.1    Hiromi, K.2
  • 17
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura, T. and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239, 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 20
    • 0020440918 scopus 로고
    • The metabolism of menadione (2-methyl-1,4-naphthoquinone) by isolated hepatocytes. A study of the implications of oxidative stress in intact cells
    • Thor, H., Smith, M.T., Hartzell, P., Bellomo, G., Jewell, S.A., and Orrenius, S. (1982) The metabolism of menadione (2-methyl-1,4-naphthoquinone) by isolated hepatocytes. A study of the implications of oxidative stress in intact cells. J. Biol. Chem. 257, 12419-12425
    • (1982) J. Biol. Chem. , vol.257 , pp. 12419-12425
    • Thor, H.1    Smith, M.T.2    Hartzell, P.3    Bellomo, G.4    Jewell, S.A.5    Orrenius, S.6
  • 21
    • 0015497436 scopus 로고
    • The nature of the reverse type I (modified type II) spectral change in liver microsomes
    • Schenkman, J.B., Cinti, D.L., Orrenius, S., Moldeus, P., and Kraschniz, R. (1972) The nature of the reverse type I (modified type II) spectral change in liver microsomes. Biochemistry 11, 4243-4251
    • (1972) Biochemistry , vol.11 , pp. 4243-4251
    • Schenkman, J.B.1    Cinti, D.L.2    Orrenius, S.3    Moldeus, P.4    Kraschniz, R.5
  • 22
    • 0016709169 scopus 로고
    • Studies on the substrate-induced spectral change of cytochrome P-450 in liver microsomes
    • Yoshida, Y. and Kumaoka, H. (1975) Studies on the substrate-induced spectral change of cytochrome P-450 in liver microsomes. J. Biochem. 78, 455-468
    • (1975) J. Biochem. , vol.78 , pp. 455-468
    • Yoshida, Y.1    Kumaoka, H.2
  • 23
    • 0021806856 scopus 로고
    • Characterization of rat cytochrome P-450MC synthesized in Saccharomyces cerevisiae
    • Sakaki, T., Oeda, K., Miyoshi, M., and Ohkawa, H. (1985) Characterization of rat cytochrome P-450MC synthesized in Saccharomyces cerevisiae. J. Biochem. 98, 167-175
    • (1985) J. Biochem. , vol.98 , pp. 167-175
    • Sakaki, T.1    Oeda, K.2    Miyoshi, M.3    Ohkawa, H.4
  • 24
    • 0000574406 scopus 로고    scopus 로고
    • Evaluation of atypical cytochrome P450 kinetics with two-substrate models: Evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites
    • Korzekwa, K.R., Krishnamachary, N., Shou, M., Ogai, A., Praise, R.A., Rettie, A.E., Gonzalez, F.J., and Tracy, T.S. (1998) Evaluation of atypical cytochrome P450 kinetics with two-substrate models: Evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites. Biochemistry 37, 4137-4147
    • (1998) Biochemistry , vol.37 , pp. 4137-4147
    • Korzekwa, K.R.1    Krishnamachary, N.2    Shou, M.3    Ogai, A.4    Praise, R.A.5    Rettie, A.E.6    Gonzalez, F.J.7    Tracy, T.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.