메뉴 건너뛰기




Volumn 24, Issue 3, 2002, Pages 329-337

Roles of NADPH-P450 reductase and apo- and holo-cytochrome b5 on xenobiotic oxidations catalyzed by 12 recombinant human cytochrome P450s expressed in membranes of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; INSECTA;

EID: 0036447583     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2001.1578     Document Type: Article
Times cited : (223)

References (40)
  • 2
    • 0002888510 scopus 로고
    • Human cytochrome P450 enzymes
    • Oritiz de Montellano, P.R., Ed., Plenum, New York.
    • Guengerich, F.P. (1995) Human cytochrome P450 enzymes in "Cytochrome P450" (Oritiz de Montellano, P.R., Ed.), pp. 473-535, Plenum, New York.
    • (1995) Cytochrome P450 , pp. 473-535
    • Guengerich, F.P.1
  • 3
    • 0025992864 scopus 로고
    • Oxidation of toxic and carcinogenic chemicals by human cytochrome P-450 enzymes
    • Guengerich, F. P., and Shimada, T. (1991) Oxidation of toxic and carcinogenic chemicals by human cytochrome P-450 enzymes. Chem. Res. Toxicol. 4, 391-407.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 391-407
    • Guengerich, F.P.1    Shimada, T.2
  • 4
    • 0026082836 scopus 로고
    • cDNA-expressed human cytochrome P450s: A new age of molecular toxicology and human risk assessment
    • Gonzalez, F. J., Crespi, C. L., and Gelboin, H. V. (1991) cDNA-expressed human cytochrome P450s: A new age of molecular toxicology and human risk assessment. Mutat. Res. 247, 113-127.
    • (1991) Mutat. Res. , vol.247 , pp. 113-127
    • Gonzalez, F.J.1    Crespi, C.L.2    Gelboin, H.V.3
  • 5
    • 0028674392 scopus 로고
    • Xenobiotic-metabolizing human cells as tools for pharmacological and toxicological research
    • Crespi, C. L. (1995) Xenobiotic-metabolizing human cells as tools for pharmacological and toxicological research. Adv. Drug Res. 26, 179-235.
    • (1995) Adv. Drug Res. , vol.26 , pp. 179-235
    • Crespi, C.L.1
  • 7
    • 0029971798 scopus 로고    scopus 로고
    • Multiple forms of human P450 expressed in Saccharomyces cerevisiae. Systematic characterization and comparison with those of the rat
    • Imaoka, S., Yamada, T., Hiroi, T., Hayashi, K., Sakai, T., Yabusaki, Y., and Funae, Y. (1996) Multiple forms of human P450 expressed in Saccharomyces cerevisiae. Systematic characterization and comparison with those of the rat. Biochem. Pharmacol. 51, 1041-1050.
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 1041-1050
    • Imaoka, S.1    Yamada, T.2    Hiroi, T.3    Hayashi, K.4    Sakai, T.5    Yabusaki, Y.6    Funae, Y.7
  • 9
    • 0029012009 scopus 로고
    • CYP3A4 expressed by insect cells infected with a recombinant baculovirus containing both CYP3A4 and human NADPH-cytochrome P450 reductase is catalytically similar to human liver microsomal CYP3A4
    • Lee, C. A., Kadwell, S. H., Kost, T. A., and Serbjit-Singh, C. J. (1995) CYP3A4 expressed by insect cells infected with a recombinant baculovirus containing both CYP3A4 and human NADPH-cytochrome P450 reductase is catalytically similar to human liver microsomal CYP3A4. Arch. Biochem. Biophys. 319, 157-167.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 157-167
    • Lee, C.A.1    Kadwell, S.H.2    Kost, T.A.3    Serbjit-Singh, C.J.4
  • 10
    • 0030843652 scopus 로고    scopus 로고
    • Drug metabolism by Escherichia coli expressing human cytochromes P450
    • Parikh, A., Gillam, E. M. J., and Guengerich, F. P. (1997) Drug metabolism by Escherichia coli expressing human cytochromes P450. Nat. Biotechnol. 15, 784-788.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 784-788
    • Parikh, A.1    Gillam, E.M.J.2    Guengerich, F.P.3
  • 11
    • 0033854025 scopus 로고    scopus 로고
    • Phenytoin metabolism by human cytochrome P450: Involvement of P450 3A and 2C forms in secondary metabolism and drug-protein adduct formation
    • Cuttle, L., Munns, A. J., Hogg, N. A., Scott, J. R., Hooper, W. D., Dickinson, R. G., and Gillam, E. M. J. (2000) Phenytoin metabolism by human cytochrome P450: Involvement of P450 3A and 2C forms in secondary metabolism and drug-protein adduct formation. Drug Metab. Dispos. 28, 945-950.
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 945-950
    • Cuttle, L.1    Munns, A.J.2    Hogg, N.A.3    Scott, J.R.4    Hooper, W.D.5    Dickinson, R.G.6    Gillam, E.M.J.7
  • 12
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme
    • Gillam, E. M. J., Baba, T., Kim, B.-R., Ohmori, S., and Guengerich, F. P. (1993) Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch. Biochem. Biophys. 305, 123-131.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 123-131
    • Gillam, E.M.J.1    Baba, T.2    Kim, B.-R.3    Ohmori, S.4    Guengerich, F.P.5
  • 14
    • 0021823707 scopus 로고
    • Cytochrome P-450 isozyme/isozyme functional interactions and NADPH-cytochrome P-450 reductase concentrations as factors in microsomal metabolism of warfarin
    • Kaminsky, L. S., and Guengerich, F. P. (1985) Cytochrome P-450 isozyme/isozyme functional interactions and NADPH-cytochrome P-450 reductase concentrations as factors in microsomal metabolism of warfarin. Eur. J. Biochem. 149, 479-489.
    • (1985) Eur. J. Biochem. , vol.149 , pp. 479-489
    • Kaminsky, L.S.1    Guengerich, F.P.2
  • 15
    • 0033815520 scopus 로고    scopus 로고
    • Roles of NADPH-P450 reductase in the O-deethylation of 7-ethoxycoumarin by recombinant human cytochrome P450 1B1 variants in Escherichia coli
    • Shimada, T., Tsumura, F., Gillam, E. M. J., Guengerich, F. P., and Inoue, K. (2000) Roles of NADPH-P450 reductase in the O-deethylation of 7-ethoxycoumarin by recombinant human cyto-chrome P450 1B1 variants in Escherichia coli. Protein Express. Purif. 20, 73-80.
    • (2000) Protein Express. Purif. , vol.20 , pp. 73-80
    • Shimada, T.1    Tsumura, F.2    Gillam, E.M.J.3    Guengerich, F.P.4    Inoue, K.5
  • 18
    • 0032488666 scopus 로고    scopus 로고
    • 5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer
    • 5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer. J. Biol. Chem. 273, 3158-3165.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3158-3165
    • Auchus, R.J.1    Lee, T.C.2    Miller, W.L.3
  • 21
    • 0033787393 scopus 로고    scopus 로고
    • Formation of a dihydroxy metabolite of phenytoin by human liver microsomes/ cytosol: Roles of cytochrome P450 2C9, 2C19, and 3A4
    • Komatsu, T., Yamazaki, H., Asahi, S., Gillam, E. M. J., Guengerich, F. P., Nakajima, M., and Yokoi, T. (2000) Formation of a dihydroxy metabolite of phenytoin by human liver microsomes/ cytosol: Roles of cytochrome P450 2C9, 2C19, and 3A4. Drug Metab. Dispos. 28, 1361-1368.
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 1361-1368
    • Komatsu, T.1    Yamazaki, H.2    Asahi, S.3    Gillam, E.M.J.4    Guengerich, F.P.5    Nakajima, M.6    Yokoi, T.7
  • 23
    • 0029757089 scopus 로고    scopus 로고
    • Purification of functional recombinant P450s from bacteria
    • Guengerich, F. P., Martin, M. V., Guo, Z., and Chun, Y.-J. (1996) Purification of functional recombinant P450s from bacteria. Methods Enzymol. 272, 35-44.
    • (1996) Methods Enzymol. , vol.272 , pp. 35-44
    • Guengerich, F.P.1    Martin, M.V.2    Guo, Z.3    Chun, Y.-J.4
  • 24
    • 0030021995 scopus 로고    scopus 로고
    • Recombinant human cytochrome P450 1A2 and N-terminal-truncated form: Construction, purification, aggregation properties, and interactions with flavodoxin, ferredoxin, and NADPH-cytochrome P450 reductase
    • Dong, M.-S., Yamazaki, H., Guo, Z., and Guengerich, F. P. (1996) Recombinant human cytochrome P450 1A2 and N-terminal-truncated form: Construction, purification, aggregation properties, and interactions with flavodoxin, ferredoxin, and NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. 327, 11-19.
    • (1996) Arch. Biochem. Biophys. , vol.327 , pp. 11-19
    • Dong, M.-S.1    Yamazaki, H.2    Guo, Z.3    Guengerich, F.P.4
  • 26
    • 0019405311 scopus 로고
    • Immunological comparison of rat, rabbit, and human liver NADPH-cytochrome P-450 reductase
    • Guengerich, F. P., Wang, P., and Mason, P. S. (1981) Immunological comparison of rat, rabbit, and human liver NADPH-cytochrome P-450 reductase. Biochemistry 20, 2379-2385.
    • (1981) Biochemistry , vol.20 , pp. 2379-2385
    • Guengerich, F.P.1    Wang, P.2    Mason, P.S.3
  • 29
    • 0002254766 scopus 로고
    • Analysis and characterization of enzymes
    • Hayes, A. W., Ed., Raven Press, New York
    • Guengerich, F. P. (1994) Analysis and characterization of enzymes in "Principles and Methods of Toxicology" (Hayes, A. W., Ed.), pp. 1259-1313, Raven Press, New York.
    • (1994) Principles and Methods of Toxicology , pp. 1259-1313
    • Guengerich, F.P.1
  • 30
    • 0032734466 scopus 로고    scopus 로고
    • Prediction of human microsomal oxidations of 7-ethoxycoumarin and chlorzoxazone using kinetic parameters of recombinant cytochrome P450 enzymes
    • Shimada, T., Tsumura, F., and Yamazaki, H. (1999) Prediction of human microsomal oxidations of 7-ethoxycoumarin and chlorzoxazone using kinetic parameters of recombinant cytochrome P450 enzymes. Drug Metab. Dispos. 27, 1274-1280.
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 1274-1280
    • Shimada, T.1    Tsumura, F.2    Yamazaki, H.3
  • 31
    • 0028237729 scopus 로고
    • Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: Studies with liver microsomes of 30 Japanese and 30 Caucasians
    • Shimada, T., Yamazaki, H., Mimura, M., Inui, Y., and Guengerich, F. P. (1994) Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: Studies with liver microsomes of 30 Japanese and 30 Caucasians. J. Pharmacol. Exp. Ther. 270, 414-423.
    • (1994) J. Pharmacol. Exp. Ther. , vol.270 , pp. 414-423
    • Shimada, T.1    Yamazaki, H.2    Mimura, M.3    Inui, Y.4    Guengerich, F.P.5
  • 32
    • 0031003669 scopus 로고    scopus 로고
    • Relationship between CYP2C9 and 2C19 genotypes and tolbutamide methyl hydroxylation and S-mephenytoin 4′-hydroxylation activities in livers of Japanese and Caucasian populations
    • Inoue, K., Yamazaki, H., Imiya, K., Akasaka, S., Guengerich, F. P., and Shimada, T. (1997) Relationship between CYP2C9 and 2C19 genotypes and tolbutamide methyl hydroxylation and S-mephenytoin 4′-hydroxylation activities in livers of Japanese and Caucasian populations. Pharmacogenetics 7, 103-113.
    • (1997) Pharmacogenetics , vol.7 , pp. 103-113
    • Inoue, K.1    Yamazaki, H.2    Imiya, K.3    Akasaka, S.4    Guengerich, F.P.5    Shimada, T.6
  • 33
    • 0032931833 scopus 로고    scopus 로고
    • Roles of CYP2A6 and CYP2B6 in nicotine C-oxidation by human liver microsomes
    • Yamazaki, H., Inoue, K., Hashimato, M., and Shimada, T. (1999) Roles of CYP2A6 and CYP2B6 in nicotine C-oxidation by human liver microsomes. Arch. Toxicol. 73, 65-70.
    • (1999) Arch. Toxicol. , vol.73 , pp. 65-70
    • Yamazaki, H.1    Inoue, K.2    Hashimato, M.3    Shimada, T.4
  • 34
    • 0032725398 scopus 로고    scopus 로고
    • Oxidation of troglitazone to a quinone-type metabolite catalyzed by cytochrome P450 2C8 and P450 3A4 in human liver microsomes
    • Yamazaki, H., Shibata, A., Suzuki, M., Nakajima, M., Shimada, N., Guengerich, F. P., and Yokoi, T. (1999) Oxidation of troglitazone to a quinone-type metabolite catalyzed by cytochrome P450 2C8 and P450 3A4 in human liver microsomes. Drug Metab. Dispos. 27, 1260-1266.
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 1260-1266
    • Yamazaki, H.1    Shibata, A.2    Suzuki, M.3    Nakajima, M.4    Shimada, N.5    Guengerich, F.P.6    Yokoi, T.7
  • 35
    • 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
  • 37
    • 0020028678 scopus 로고
    • Estimation of isozymes of microsomal cytochrome P-450 in rats, rabbits, and humans using immunochemical staining coupled with sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Guengerich, F. P., Wang, P., and Davidson, N. K. (1982) Estimation of isozymes of microsomal cytochrome P-450 in rats, rabbits, and humans using immunochemical staining coupled with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochemistry 21, 1698-1706.
    • (1982) Biochemistry , vol.21 , pp. 1698-1706
    • Guengerich, F.P.1    Wang, P.2    Davidson, N.K.3
  • 39
    • 0033105118 scopus 로고    scopus 로고
    • Integrated cytochrome P450 reaction phenotyping. Attempting to bridge the gap between cDNA-expressed cytochromes P450 and native human liver microsomes
    • Rodrigues, A. D. (1999) Integrated cytochrome P450 reaction phenotyping. Attempting to bridge the gap between cDNA-expressed cytochromes P450 and native human liver microsomes. Biochem. Pharmacol. 57, 465-480.
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 465-480
    • Rodrigues, A.D.1
  • 40
    • 0028987970 scopus 로고
    • 5, NADPH- P450 reductase, and lipid on the rate of 6β-hydroxylation of testosterone as catalyzed by a human P450 3A4 fusion protein
    • 5, NADPH- P450 reductase, and lipid on the rate of 6b-hydroxylation of testosterone as catalyzed by a human P450 3A4 fusion protein. Arch. Biochem. Biophys. 318, 314-321.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 314-321
    • Shet, M.S.1    Faulkner, K.M.2    Holmans, P.L.3    Fisher, C.W.4    Estabrook, R.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.