메뉴 건너뛰기




Volumn 52, Issue 2, 1996, Pages 301-309

Requirements for cytochrome b5 in the oxidation of 7-ethoxycoumarin, chlorzoxazone, aniline, and N-nitrosodimethylamine by recombinant cytochrome P450 2E1 and by human liver microsomes

Author keywords

7 ethoxycoumarin; aniline; chlorzoxazone; cytochrome b5; elec tron transfer; N nitrosodimethylamine; P450 2E1; reconstitution

Indexed keywords

7 ETHOXYCOUMARIN DEETHYLASE; ANILINE; CHLORZOXAZONE; CYTOCHROME B5; CYTOCHROME B5 REDUCTASE; CYTOCHROME P450 ISOENZYME; CYTOCHROME P450 REDUCTASE; DIMETHYLNITROSAMINE; ENZYME ANTIBODY; IMMUNOGLOBULIN G; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; 7 ETHOXYCOUMARIN; 7-ETHOXYCOUMARIN; ANILINE DERIVATIVE; COUMARIN DERIVATIVE; CYTOCHROME P450; CYTOCHROME P450 1A2; CYTOCHROME P450 2E1; N DEMETHYLASE; OXIDOREDUCTASE; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

EID: 0030602654     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/0006-2952(96)00208-0     Document Type: Article
Times cited : (69)

References (43)
  • 1
    • 0026750647 scopus 로고
    • The human hepatic cytochromes P450 involved in drug metabolism
    • 1. Wrighton SA and Stevens JC, The human hepatic cytochromes P450 involved in drug metabolism. Crit Rev Toxicol 22: 1-21, 1992.
    • (1992) Crit Rev Toxicol , vol.22 , pp. 1-21
    • Wrighton, S.A.1    Stevens, J.C.2
  • 2
    • 0025992864 scopus 로고
    • Oxidation of toxic and carcinogenic chemicals by human cytochrome P-450 enzymes
    • 2. Guengerich FP and Shimada T, Oxidation of toxic and carcinogenic chemicals by human cytochrome P-450 enzymes. Chem Res Toxicol 4: 391-407, 1991.
    • (1991) Chem Res Toxicol , vol.4 , pp. 391-407
    • Guengerich, F.P.1    Shimada, T.2
  • 4
    • 0022499774 scopus 로고
    • Evidence that isoniazid and ethanol induce the same microsomal cytochrome P-450 in rat liver, an isozyme homologous to rabbit liver cytochrome P-450 isozyme 3a
    • 4. Ryan DE, Koop DR, Thomas PE, Coon MJ and Levin W, Evidence that isoniazid and ethanol induce the same microsomal cytochrome P-450 in rat liver, an isozyme homologous to rabbit liver cytochrome P-450 isozyme 3a. Arch Biochem Biophys 246: 633-644, 1986.
    • (1986) Arch Biochem Biophys , vol.246 , pp. 633-644
    • Ryan, D.E.1    Koop, D.R.2    Thomas, P.E.3    Coon, M.J.4    Levin, W.5
  • 5
    • 0023180336 scopus 로고
    • Regulation of cytochrome P-450j, a high-affinity N-nitrosodimethylamine demethylase, in rat hepatic microsomes
    • 5. Thomas PE, Bandiera S, Maines SL, Ryan DE and Levin W, Regulation of cytochrome P-450j, a high-affinity N-nitrosodimethylamine demethylase, in rat hepatic microsomes. Biochemistry 26: 2280-2289, 1987.
    • (1987) Biochemistry , vol.26 , pp. 2280-2289
    • Thomas, P.E.1    Bandiera, S.2    Maines, S.L.3    Ryan, D.E.4    Levin, W.5
  • 6
    • 0023900010 scopus 로고
    • Ethanol-, fasting-, and acetone-inducible cytochromes P-450 in rat liver: Regulation and characteristics of enzymes belonging to the IIB and IIE gene subfamilies
    • 6. Johansson I, Ekstrom G, Scholte B, Puzycki D, Jornvall H and Ingelman-Sundberg M, Ethanol-, fasting-, and acetone-inducible cytochromes P-450 in rat liver: Regulation and characteristics of enzymes belonging to the IIB and IIE gene subfamilies. Biochemistry 27: 1925-1934, 1988.
    • (1988) Biochemistry , vol.27 , pp. 1925-1934
    • Johansson, I.1    Ekstrom, G.2    Scholte, B.3    Puzycki, D.4    Jornvall, H.5    Ingelman-Sundberg, M.6
  • 8
    • 0023920685 scopus 로고
    • Purification and characterization of diabetes-inducible cytochrome P-450
    • 8. Funae Y, Imaoka S and Shimojo N, Purification and characterization of diabetes-inducible cytochrome P-450. Biochem Int 16: 503-509, 1988.
    • (1988) Biochem Int , vol.16 , pp. 503-509
    • Funae, Y.1    Imaoka, S.2    Shimojo, N.3
  • 9
    • 0026035519 scopus 로고
    • Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects
    • 9. Guengerich FP, Kim DH and Iwasaki M, Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects. Chem Res Toxicol 4: 168-179, 1991.
    • (1991) Chem Res Toxicol , vol.4 , pp. 168-179
    • Guengerich, F.P.1    Kim, D.H.2    Iwasaki, M.3
  • 10
    • 0023200612 scopus 로고
    • Purification and characterization of ethanol-inducible human hepatic cytochrome P-450HLj
    • 10. Wrighton SA, Thomas PE, Ryan DE and Levin W, Purification and characterization of ethanol-inducible human hepatic cytochrome P-450HLj. Arch Biochem Biophys 258: 292-297, 1987.
    • (1987) Arch Biochem Biophys , vol.258 , pp. 292-297
    • Wrighton, S.A.1    Thomas, P.E.2    Ryan, D.E.3    Levin, W.4
  • 11
    • 0025601454 scopus 로고
    • Lidocaine metabolism by human cytochrome P-450s purified from hepatic microsomes: Comparison of those with rat hepatic cytochrome P-450s
    • 11. Imaoka S, Enomoto K, Oda Y, Asada A, Fujimori M, Shimada T, Fujita S, Guengerich FP and Funae Y, Lidocaine metabolism by human cytochrome P-450s purified from hepatic microsomes: Comparison of those with rat hepatic cytochrome P-450s. J Pharmacol Exp Ther 255: 1385-1391, 1990.
    • (1990) J Pharmacol Exp Ther , vol.255 , pp. 1385-1391
    • Imaoka, S.1    Enomoto, K.2    Oda, Y.3    Asada, A.4    Fujimori, M.5    Shimada, T.6    Fujita, S.7    Guengerich, F.P.8    Funae, Y.9
  • 12
    • 0026654417 scopus 로고
    • Role of phospholipids in reconstituted cytochrome P450 3A form and mechanism of their activation of catalytic activity
    • 12. Imaoka S, Imai Y, Shimada T and Funae Y, Role of phospholipids in reconstituted cytochrome P450 3A form and mechanism of their activation of catalytic activity. Biochemistry 31: 6063-6069, 1992.
    • (1992) Biochemistry , vol.31 , pp. 6063-6069
    • Imaoka, S.1    Imai, Y.2    Shimada, T.3    Funae, Y.4
  • 13
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme
    • 13. Gillam E, Baba T, Kim BR, Ohmori S and Guengerich FP, Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch Biochem Biophys 305: 123-131, 1993.
    • (1993) Arch Biochem Biophys , vol.305 , pp. 123-131
    • Gillam, E.1    Baba, T.2    Kim, B.R.3    Ohmori, S.4    Guengerich, F.P.5
  • 14
    • 0028912205 scopus 로고
    • Expression of cytochrome P450 3A5 in Escherichia coli: Effects of 5′ modification, purification, spectral characterization, reconstitution conditions, and catalytic activities
    • 14. Gillam EMJ, Guo Z, Ueng Y-F, Yamazaki H, Cock I, Reilly PEB, Hopper WD and Guengerich FP, Expression of cytochrome P450 3A5 in Escherichia coli: Effects of 5′ modification, purification, spectral characterization, reconstitution conditions, and catalytic activities. Arch Biochem Biophys 317: 374-384, 1995.
    • (1995) Arch Biochem Biophys , vol.317 , pp. 374-384
    • Gillam, E.M.J.1    Guo, Z.2    Ueng, Y.-F.3    Yamazaki, H.4    Cock, I.5    Reilly, P.E.B.6    Hopper, W.D.7    Guengerich, F.P.8
  • 16
    • 0029047732 scopus 로고
    • Roles of divalent metal ions in oxidations catalyzed by recombinant cytochrome P450 3A4 and replacement of NADPH-cytochrome P450 reductase with other flavoproteins, ferredoxin, and oxygen surrogates
    • 16. Yamazaki H, Ueng Y-F, Shimada T and Guengerich FP, Roles of divalent metal ions in oxidations catalyzed by recombinant cytochrome P450 3A4 and replacement of NADPH-cytochrome P450 reductase with other flavoproteins, ferredoxin, and oxygen surrogates. Biochemistry 34: 8380-8389, 1995.
    • (1995) Biochemistry , vol.34 , pp. 8380-8389
    • Yamazaki, H.1    Ueng, Y.-F.2    Shimada, T.3    Guengerich, F.P.4
  • 18
    • 0027524747 scopus 로고
    • 5, microsomal epoxide hydrolase, and glutathione transferases: Evidence for an important role of microsomal epoxide hydrolase in the formation of hydroquinone
    • 5, microsomal epoxide hydrolase, and glutathione transferases: Evidence for an important role of microsomal epoxide hydrolase in the formation of hydroquinone. Toxicol Appl Pharmocol 122: 172-181, 1993.
    • (1993) Toxicol Appl Pharmocol , vol.122 , pp. 172-181
    • Snyder, R.1    Chepiga, T.2    Yang, C.S.3    Thomas, H.4    Platt, K.5    Oesch, F.6
  • 19
    • 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
    • 19. Shimada T, Yamazaki H, Mimura M, Inui Y and Guengerich FP, 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.
    • (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
  • 20
    • 0002254766 scopus 로고
    • Analysis and characterization of enzymes
    • (Ed. Hayes AW), 3rd Edn, Raven Press, New York
    • 20. Guengerich FP, Analysis and characterization of enzymes. In: Principles and Methods of Toxicology (Ed. Hayes AW), 3rd Edn, pp. 1259-1313. Raven Press, New York, 1994.
    • (1994) Principles and Methods of Toxicology , pp. 1259-1313
    • Guengerich, F.P.1
  • 21
    • 0028023169 scopus 로고
    • Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties
    • 21. Gillam EMJ, Guo Z and Guengerich FP, Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties. Arch Biochem Biophys 312: 59-66, 1994.
    • (1994) Arch Biochem Biophys , vol.312 , pp. 59-66
    • Gillam, E.M.J.1    Guo, Z.2    Guengerich, F.P.3
  • 22
    • 0028071497 scopus 로고
    • Expression of modified human cytochrome P450 1A1 in Escherichia coli: Effects of 5′ substitution, stabilization, purification, spectral characterization, and catalytic properties
    • 22. Guo Z, Gillam EMJ, Ohmori S, Tukey RH and Guengerich FP, Expression of modified human cytochrome P450 1A1 in Escherichia coli: Effects of 5′ substitution, stabilization, purification, spectral characterization, and catalytic properties. Arch Biochem Biophys 312: 436-446, 1994.
    • (1994) Arch Biochem Biophys , vol.312 , pp. 436-446
    • Guo, Z.1    Gillam, E.M.J.2    Ohmori, S.3    Tukey, R.H.4    Guengerich, F.P.5
  • 23
    • 0028358220 scopus 로고
    • Expression of modified human cytochrome P450 1A2 in Escherichia coli. Stabilization, purification, spectral characterization, and catalytic activities of the enzymes
    • 23. Sandhu P, Guo Z, Baba T, Martin MV, Tukey RH and Guengerich FP, Expression of modified human cytochrome P450 1A2 in Escherichia coli. Stabilization, purification, spectral characterization, and catalytic activities of the enzymes. Arch Biochem Biophys 309: 168-177, 1994-
    • (1994) Arch Biochem Biophys , vol.309 , pp. 168-177
    • Sandhu, P.1    Guo, Z.2    Baba, T.3    Martin, M.V.4    Tukey, R.H.5    Guengerich, F.P.6
  • 24
    • 0023276802 scopus 로고
    • Cytochrome P-450-mediated activation of procarcinogens and promutagens to DNA-damaging products by measuring expression of umu gene in Salmonella typhimurium TA1535/pSK1002
    • 24. Shimada T and Nakamura S, Cytochrome P-450-mediated activation of procarcinogens and promutagens to DNA-damaging products by measuring expression of umu gene in Salmonella typhimurium TA1535/pSK1002. Biochem Pharmacol 36: 1979-1987, 1987.
    • (1987) Biochem Pharmacol , vol.36 , pp. 1979-1987
    • Shimada, T.1    Nakamura, S.2
  • 25
    • 0016618618 scopus 로고
    • 5 reductase from rabbit liver microsomes
    • 5 reductase from rabbit liver microsomes. J Biochem (Tokyo) 78: 1057-1073, 1975.
    • (1975) J Biochem (Tokyo) , vol.78 , pp. 1057-1073
    • Mihara, K.1    Sato, R.2
  • 26
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • 26. Yasukochi Y and Masters B, Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography. J Biol Chem 251: 5337-5344, 1976.
    • (1976) J Biol Chem , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.2
  • 27
    • 0022574425 scopus 로고
    • Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxidative drug metabolism. Purification and characterization of two similar forms involved in the reaction
    • 27. Shimada T, Misono KS and Guengerich FP, Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxidative drug metabolism. Purification and characterization of two similar forms involved in the reaction. J Biol Chem 261: 909-921, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 909-921
    • Shimada, T.1    Misono, K.S.2    Guengerich, F.P.3
  • 28
    • 0019741894 scopus 로고
    • Production and application of antibodies to rat liver cytochrome P-450
    • 28. Kaminsky LS, Fasco MJ and Guengerich FP, Production and application of antibodies to rat liver cytochrome P-450. Methods Enzymol 74: 262-272, 1981.
    • (1981) Methods Enzymol , vol.74 , pp. 262-272
    • Kaminsky, L.S.1    Fasco, M.J.2    Guengerich, F.P.3
  • 29
    • 0017874892 scopus 로고
    • Immunochemical study on the electron pathway from NADH to cytochrome P-450 of liver microsomes
    • 29. Noshiro M and Omura T, Immunochemical study on the electron pathway from NADH to cytochrome P-450 of liver microsomes. J Biochem (Tokyo) 83: 61-77, 1978.
    • (1978) J Biochem (Tokyo) , vol.83 , pp. 61-77
    • Noshiro, M.1    Omura, T.2
  • 30
    • 0030064194 scopus 로고    scopus 로고
    • 7-Ethoxycoumarin O-deethylation catalyzed by cytochromes P450 1A2 and 2E1 in human liver microsomes
    • 30. Yamazaki H, Inoue K, Mimura M, Oda Y, Guengerich FP and Shimada T, 7-Ethoxycoumarin O-deethylation catalyzed by cytochromes P450 1A2 and 2E1 in human liver microsomes. Biochem Pharmacol 51: 313-319, 1996.
    • (1996) Biochem Pharmacol , vol.51 , pp. 313-319
    • Yamazaki, H.1    Inoue, K.2    Mimura, M.3    Oda, Y.4    Guengerich, F.P.5    Shimada, T.6
  • 32
    • 0028918999 scopus 로고
    • Selectivity of cytochrome P450 2E1 in chlorzoxazone 6-hydroxylation
    • 32. Yamazaki H, Guo Z and Guengerich FP, Selectivity of cytochrome P450 2E1 in chlorzoxazone 6-hydroxylation. Drug Metab Dispos 23: 438-440, 1995.
    • (1995) Drug Metab Dispos , vol.23 , pp. 438-440
    • Yamazaki, H.1    Guo, Z.2    Guengerich, F.P.3
  • 33
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • 33. Nash T, The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochem J 55: 416-421, 1953.
    • (1953) Biochem J , vol.55 , pp. 416-421
    • Nash, T.1
  • 34
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • 34. Omura T and Sato R, The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J Biol Chem 239: 2370-2378, 1964.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 36
    • 0020465448 scopus 로고
    • Catalytic activity of cytochrome P-450 isozyme 3a isolated from liver microsomes of ethanol-treated rabbits
    • 36. Morgan ET, Koop DR and Coon MJ, Catalytic activity of cytochrome P-450 isozyme 3a isolated from liver microsomes of ethanol-treated rabbits. J Biol Chem 257: 13951-13957, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 13951-13957
    • Morgan, E.T.1    Koop, D.R.2    Coon, M.J.3
  • 37
    • 0022523166 scopus 로고
    • Monoclonal antibodies to ethanol induced cytochrome P-450 that inhibit aniline and nitrosamine metabolism
    • 37. Park SS, Ko I-Y, Patten C, Yang CS and Geiboin HV, Monoclonal antibodies to ethanol induced cytochrome P-450 that inhibit aniline and nitrosamine metabolism. Biochem Pharmacol 35: 2855-2858, 1986.
    • (1986) Biochem Pharmacol , vol.35 , pp. 2855-2858
    • Park, S.S.1    Ko, I.-Y.2    Patten, C.3    Yang, C.S.4    Geiboin, H.V.5
  • 38
    • 0017660027 scopus 로고
    • The organization and interaction of monooxygenase enzymes in the microsomal membrane
    • 38. Young CS, The organization and interaction of monooxygenase enzymes in the microsomal membrane. Life Sci 21: 1047-1058, 1977.
    • (1977) Life Sci , vol.21 , pp. 1047-1058
    • Young, C.S.1
  • 39
    • 0028948688 scopus 로고
    • 5 on the stoichiometry of P450 2E1-catalyzed reactions
    • 5 on the stoichiometry of P450 2E1-catalyzed reactions. Arch Biochem Biophys 317: 504-513, 1995.
    • (1995) Arch Biochem Biophys , vol.317 , pp. 504-513
    • Patten, C.J.1    Koch, P.2
  • 41
    • 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 6β-hydroxylation of testosterone as catalyzed by a human P450 3A4 fusion protein. Arch Biochem Biophys 318: 314-321, 1995.
    • (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
  • 42
    • 0028172287 scopus 로고
    • Influence of ionic strength on the P450 monooxygenase reaction and role of cytochrome b5 in the process
    • 42. Schenkman JB, Voznesensky AI and Jansson I, Influence of ionic strength on the P450 monooxygenase reaction and role of cytochrome b5 in the process. Arch Biochem Biophys 314: 234-241, 1994.
    • (1994) Arch Biochem Biophys , vol.314 , pp. 234-241
    • Schenkman, J.B.1    Voznesensky, A.I.2    Jansson, I.3
  • 43
    • 0022395582 scopus 로고
    • Evidence for a predominantly NADH-dependent O-dealkylating system in rat hepatic microsomes
    • 43. Kuwahara S and Mannering GJ, Evidence for a predominantly NADH-dependent O-dealkylating system in rat hepatic microsomes. Biochem Pharmacol 34: 4215-4228, 1985.
    • (1985) Biochem Pharmacol , vol.34 , pp. 4215-4228
    • Kuwahara, S.1    Mannering, G.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.