메뉴 건너뛰기




Volumn 57, Issue 2, 2008, Pages 188-200

Heterologous expression and characterization of wild-type human cytochrome P450 1A2 without conventional N-terminal modification in Escherichia coli

Author keywords

Catalytic function; Heterologous expression; Human cytochrome P450 1A2; N terminal membrane anchor domain; N terminal modification; Spin equilibrium

Indexed keywords

CYTOCHROME P450 1A2; DEUTERIUM; ENZYME INHIBITOR; HYDROGEN PEROXIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 37349017983     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.10.010     Document Type: Article
Times cited : (29)

References (45)
  • 2
    • 0026750647 scopus 로고
    • The human hepatic cytochromes P450 involved in drug metabolism
    • Wrighton S.A., and Stevens J.C. The human hepatic cytochromes P450 involved in drug metabolism. Crit. Rev. Toxicol. 22 (1992) 1-21
    • (1992) Crit. Rev. Toxicol. , vol.22 , pp. 1-21
    • Wrighton, S.A.1    Stevens, J.C.2
  • 3
    • 33646494635 scopus 로고    scopus 로고
    • Functional expression of human cytochrome P450 enzymes in Escherichia coli
    • Yun C.H., Yim S.K., Kim D.H., and Ahn T. Functional expression of human cytochrome P450 enzymes in Escherichia coli. Curr. Drug. Metab. 7 (2006) 411-429
    • (2006) Curr. Drug. Metab. , vol.7 , pp. 411-429
    • Yun, C.H.1    Yim, S.K.2    Kim, D.H.3    Ahn, T.4
  • 4
    • 0036223831 scopus 로고    scopus 로고
    • Summary of information on human CYP enzymes: human P450 metabolism data
    • Rendic S. Summary of information on human CYP enzymes: human P450 metabolism data. Drug. Metab. Rev. 34 (2002) 83-448
    • (2002) Drug. Metab. Rev. , vol.34 , pp. 83-448
    • Rendic, S.1
  • 5
    • 0024326433 scopus 로고
    • Roles of individual human cytochrome P-450 enzymes in the bioactivation of benzo(a)pyrene, 7,8-dihydroxy-7,8-dihydrobenzo(a)pyrene, and other dihydrodiol derivatives of polycyclic aromatic hydrocarbons
    • Shimada T., Martin M.V., Pruess-Schwartz D., Marnett L.J., and Guengerich F.P. Roles of individual human cytochrome P-450 enzymes in the bioactivation of benzo(a)pyrene, 7,8-dihydroxy-7,8-dihydrobenzo(a)pyrene, and other dihydrodiol derivatives of polycyclic aromatic hydrocarbons. Cancer Res. 49 (1989) 6304-6312
    • (1989) Cancer Res. , vol.49 , pp. 6304-6312
    • Shimada, T.1    Martin, M.V.2    Pruess-Schwartz, D.3    Marnett, L.J.4    Guengerich, F.P.5
  • 6
    • 0024343858 scopus 로고
    • Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines
    • Butler M.A., Iwasaki M., Guengerich F.P., and Kadlubar F.F. Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines. Proc. Natl. Acad. Sci. USA 86 (1989) 7696-7700
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7696-7700
    • Butler, M.A.1    Iwasaki, M.2    Guengerich, F.P.3    Kadlubar, F.F.4
  • 8
    • 34347235844 scopus 로고    scopus 로고
    • Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2
    • Sansen S., Yano J.K., Reynald R.L., Schoch G.A., Griffin K.J., Stout C.D., and Johnson E.F. Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. J. Biol. Chem. 282 (2007) 14348-14355
    • (2007) J. Biol. Chem. , vol.282 , pp. 14348-14355
    • Sansen, S.1    Yano, J.K.2    Reynald, R.L.3    Schoch, G.A.4    Griffin, K.J.5    Stout, C.D.6    Johnson, E.F.7
  • 10
    • 0028358220 scopus 로고
    • Expression of modified human cytochrome P450 1A2 in Escherichia coli: stabilization, purification, spectral characterization, and catalytic activities of the enzyme
    • Sandhu P., Guo Z., Baba T., Martin M.V., Tukey R.H., and Guengerich F.P. Expression of modified human cytochrome P450 1A2 in Escherichia coli: stabilization, purification, spectral characterization, and catalytic activities of the enzyme. Arch. Biochem. Biophys. 309 (1994) 168-177
    • (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
  • 11
    • 0029852566 scopus 로고    scopus 로고
    • New applications of bacterial systems to problems in toxicology
    • Guengerich F.P., Gillam E.M., and Shimada T. New applications of bacterial systems to problems in toxicology. Crit. Rev. Toxicol. 26 (1996) 551-583
    • (1996) Crit. Rev. Toxicol. , vol.26 , pp. 551-583
    • Guengerich, F.P.1    Gillam, E.M.2    Shimada, T.3
  • 12
    • 0034687092 scopus 로고    scopus 로고
    • Rate-determining steps in phenacetin oxidations by human cytochrome P450 1A2 and selected mutants
    • Yun C.H., Miller G.P., and Guengerich F.P. Rate-determining steps in phenacetin oxidations by human cytochrome P450 1A2 and selected mutants. Biochemistry 39 (2000) 11319-11329
    • (2000) Biochemistry , vol.39 , pp. 11319-11329
    • Yun, C.H.1    Miller, G.P.2    Guengerich, F.P.3
  • 13
    • 0035836465 scopus 로고    scopus 로고
    • Oxidations of p-alkoxyacylanilides catalyzed by human cytochrome P450 1A2: structure-activity relationships and simulation of rate constants of individual steps in catalysis
    • Yun C.H., Miller G.P., and Guengerich F.P. Oxidations of p-alkoxyacylanilides catalyzed by human cytochrome P450 1A2: structure-activity relationships and simulation of rate constants of individual steps in catalysis. Biochemistry 40 (2001) 4521-4530
    • (2001) Biochemistry , vol.40 , pp. 4521-4530
    • Yun, C.H.1    Miller, G.P.2    Guengerich, F.P.3
  • 14
    • 21744439829 scopus 로고    scopus 로고
    • Involvement of nonlamellar-prone lipids in the stability increase of human cytochrome P450 1A2 in reconstituted membranes
    • Ahn T., Yun C.H., and Oh D.B. Involvement of nonlamellar-prone lipids in the stability increase of human cytochrome P450 1A2 in reconstituted membranes. Biochemistry 44 (2005) 9188-9196
    • (2005) Biochemistry , vol.44 , pp. 9188-9196
    • Ahn, T.1    Yun, C.H.2    Oh, D.B.3
  • 15
    • 16844371090 scopus 로고    scopus 로고
    • Kinetic analysis of oxidation of coumarins by human cytochrome P450 2A6
    • Yun C.H., Kim K.H., Calcutt M.W., and Guengerich F.P. Kinetic analysis of oxidation of coumarins by human cytochrome P450 2A6. J. Biol. Chem. 280 (2005) 12279-12291
    • (2005) J. Biol. Chem. , vol.280 , pp. 12279-12291
    • Yun, C.H.1    Kim, K.H.2    Calcutt, M.W.3    Guengerich, F.P.4
  • 16
    • 33646267951 scopus 로고    scopus 로고
    • Kinetic deuterium isotope effects for 7-alkoxycoumarin O-dealkylation reactions catalyzed by human cytochromes P450 and in liver microsomes. Rate-limiting C-H bond breaking in cytochrome P450 1A2 substrate oxidation
    • Kim K.H., Isin E.M., Yun C.H., Kim D.H., and Guengerich F.P. Kinetic deuterium isotope effects for 7-alkoxycoumarin O-dealkylation reactions catalyzed by human cytochromes P450 and in liver microsomes. Rate-limiting C-H bond breaking in cytochrome P450 1A2 substrate oxidation. FEBS J. 273 (2006) 2223-2231
    • (2006) FEBS J. , vol.273 , pp. 2223-2231
    • Kim, K.H.1    Isin, E.M.2    Yun, C.H.3    Kim, D.H.4    Guengerich, F.P.5
  • 17
    • 0031822496 scopus 로고    scopus 로고
    • Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities
    • Hanna I.H., Teiber J.F., Kokones K.L., and Hollenberg P.F. Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities. Arch. Biochem. Biophys. 350 (1998) 324-332
    • (1998) Arch. Biochem. Biophys. , vol.350 , pp. 324-332
    • Hanna, I.H.1    Teiber, J.F.2    Kokones, K.L.3    Hollenberg, P.F.4
  • 18
    • 0024518203 scopus 로고
    • Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis
    • Shen A.L., Porter T.D., Wilson T.E., and Kasper C.B. Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis. J. Biol. Chem. 264 (1989) 7584-7589
    • (1989) J. Biol. Chem. , vol.264 , pp. 7584-7589
    • Shen, A.L.1    Porter, T.D.2    Wilson, T.E.3    Kasper, C.B.4
  • 19
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T., and Sato R. The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239 (1964) 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 20
    • 0021096850 scopus 로고
    • Oxidation-reduction properties of rat liver cytochromes P-450 and NADPH-cytochrome p-450 reductase related to catalysis in reconstituted systems
    • Guengerich F.P. Oxidation-reduction properties of rat liver cytochromes P-450 and NADPH-cytochrome p-450 reductase related to catalysis in reconstituted systems. Biochemistry 22 (1983) 2811-2820
    • (1983) Biochemistry , vol.22 , pp. 2811-2820
    • Guengerich, F.P.1
  • 21
    • 0027636460 scopus 로고
    • Experimental method to correct fluorescence intensities for the inner filter effect
    • Subbarao N.K., and MacDonald R.C. Experimental method to correct fluorescence intensities for the inner filter effect. Analyst 118 (1993) 913-916
    • (1993) Analyst , vol.118 , pp. 913-916
    • Subbarao, N.K.1    MacDonald, R.C.2
  • 22
    • 0034705191 scopus 로고    scopus 로고
    • Elucidation of distinct ligand binding sites for cytochrome P450 3A4
    • Hosea N.A., Miller G.P., and Guengerich F.P. Elucidation of distinct ligand binding sites for cytochrome P450 3A4. Biochemistry 39 (2000) 5929-5939
    • (2000) Biochemistry , vol.39 , pp. 5929-5939
    • Hosea, N.A.1    Miller, G.P.2    Guengerich, F.P.3
  • 23
    • 33646942269 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of ligand binding by cytochrome P450 3A4
    • Isin E.M., and Guengerich F.P. Kinetics and thermodynamics of ligand binding by cytochrome P450 3A4. J. Biol. Chem. 281 (2006) 9127-9136
    • (2006) J. Biol. Chem. , vol.281 , pp. 9127-9136
    • Isin, E.M.1    Guengerich, F.P.2
  • 24
    • 0020601426 scopus 로고
    • Differential effects of phenobarbitone and 3-methylcholanthrene induction on the hepatic microsomal metabolism and cytochrome P-450-binding of phenoxazone and a homologous series of its n-alkyl ethers (alkoxyresorufins)
    • Burke M.D., and Mayer R.T. Differential effects of phenobarbitone and 3-methylcholanthrene induction on the hepatic microsomal metabolism and cytochrome P-450-binding of phenoxazone and a homologous series of its n-alkyl ethers (alkoxyresorufins). Chem. Biol. Interact. 45 (1983) 243-258
    • (1983) Chem. Biol. Interact. , vol.45 , pp. 243-258
    • Burke, M.D.1    Mayer, R.T.2
  • 25
    • 1542328873 scopus 로고    scopus 로고
    • The effect of reciprocal active site mutations in human cytochromes P450 1A1 and 1A2 on alkoxyresorufin metabolism
    • Liu J., Ericksen S.S., Sivaneri M., Besspiata D., Fisher C.W., and Szklarz G.D. The effect of reciprocal active site mutations in human cytochromes P450 1A1 and 1A2 on alkoxyresorufin metabolism. Arch. Biochem. Biophys. 424 (2004) 33-43
    • (2004) Arch. Biochem. Biophys. , vol.424 , pp. 33-43
    • Liu, J.1    Ericksen, S.S.2    Sivaneri, M.3    Besspiata, D.4    Fisher, C.W.5    Szklarz, G.D.6
  • 27
    • 0016832598 scopus 로고
    • Steady-state analysis of kinetic isotope effects in enzymic reactions
    • Northrop D.B. Steady-state analysis of kinetic isotope effects in enzymic reactions. Biochemistry 14 (1975) 2644-2651
    • (1975) Biochemistry , vol.14 , pp. 2644-2651
    • Northrop, D.B.1
  • 28
    • 0020345922 scopus 로고
    • Deuterium and tritium kinetic isotope effects on initial rates
    • Northrop D.B. Deuterium and tritium kinetic isotope effects on initial rates. Methods Enzymol. 87 (1982) 607-625
    • (1982) Methods Enzymol. , vol.87 , pp. 607-625
    • Northrop, D.B.1
  • 29
    • 0023953283 scopus 로고
    • Direct protein microsequencing from Immobilon-P Transfer Membrane
    • LeGendre N., and Matsudaira P. Direct protein microsequencing from Immobilon-P Transfer Membrane. Biotechniques 6 (1988) 154-159
    • (1988) Biotechniques , vol.6 , pp. 154-159
    • LeGendre, N.1    Matsudaira, P.2
  • 30
    • 0029763107 scopus 로고    scopus 로고
    • Identification of retained N-formylmethionine in bacterial recombinant mammalian cytochrome P450 proteins with the N-terminal sequence MALLLAVFL.: roles of residues 3-5 in retention and membrane topology
    • Dong M.S., Bell L.C., Guo Z., Phillips D.R., Blair I.A., and Guengerich F.P. Identification of retained N-formylmethionine in bacterial recombinant mammalian cytochrome P450 proteins with the N-terminal sequence MALLLAVFL.: roles of residues 3-5 in retention and membrane topology. Biochemistry 35 (1996) 10031-10040
    • (1996) Biochemistry , vol.35 , pp. 10031-10040
    • Dong, M.S.1    Bell, L.C.2    Guo, Z.3    Phillips, D.R.4    Blair, I.A.5    Guengerich, F.P.6
  • 31
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli
    • Barnes H.J., Arlotto M.P., and Waterman M.R. Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli. Proc. Natl. Acad. Sci. USA 88 (1991) 5597-5601
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 32
    • 0020480282 scopus 로고
    • Characterization of translational initiation sites in E. coli
    • Stormo G.D., Schneider T.D., and Gold L.M. Characterization of translational initiation sites in E. coli. Nucleic Acids Res. 10 (1982) 2971-2996
    • (1982) Nucleic Acids Res. , vol.10 , pp. 2971-2996
    • Stormo, G.D.1    Schneider, T.D.2    Gold, L.M.3
  • 33
    • 0014059179 scopus 로고
    • Spectral studies of drug interaction with hepatic microsomal cytochrome
    • Schenkman J.B., Remmer H., and Estabrook R.W. Spectral studies of drug interaction with hepatic microsomal cytochrome. Mol. Pharmacol. 3 (1967) 113-123
    • (1967) Mol. Pharmacol. , vol.3 , pp. 113-123
    • Schenkman, J.B.1    Remmer, H.2    Estabrook, R.W.3
  • 34
    • 3042644563 scopus 로고    scopus 로고
    • High-level expression of human cytochrome P450 1A2 by co-expression with human molecular chaperone HDJ-1 (Hsp40)
    • Ahn T., Yang S., and Yun C.H. High-level expression of human cytochrome P450 1A2 by co-expression with human molecular chaperone HDJ-1 (Hsp40). Protein Expr. Purif. 36 (2004) 48-52
    • (2004) Protein Expr. Purif. , vol.36 , pp. 48-52
    • Ahn, T.1    Yang, S.2    Yun, C.H.3
  • 35
    • 7044231916 scopus 로고    scopus 로고
    • High-level expression of human cytochrome P450 3A4 by co-expression with human molecular chaperone HDJ-1 (Hsp40)
    • Ahn T., and Yun C.H. High-level expression of human cytochrome P450 3A4 by co-expression with human molecular chaperone HDJ-1 (Hsp40). Arch. Pharm. Res. 27 (2004) 319-323
    • (2004) Arch. Pharm. Res. , vol.27 , pp. 319-323
    • Ahn, T.1    Yun, C.H.2
  • 36
    • 0025361553 scopus 로고
    • Predicting optimal and suboptimal secondary structure for RNA
    • Jaeger J.A., Turner D.H., and Zuker M. Predicting optimal and suboptimal secondary structure for RNA. Methods Enzymol. 183 (1990) 281-306
    • (1990) Methods Enzymol. , vol.183 , pp. 281-306
    • Jaeger, J.A.1    Turner, D.H.2    Zuker, M.3
  • 37
  • 39
    • 29244442685 scopus 로고    scopus 로고
    • Heterologous expression, purification, and properties of human cytochrome P450 27C1
    • Wu Z.L., Bartleson C.J., Ham A.J., and Guengerich F.P. Heterologous expression, purification, and properties of human cytochrome P450 27C1. Arch. Biochem. Biophys. 445 (2006) 138-146
    • (2006) Arch. Biochem. Biophys. , vol.445 , pp. 138-146
    • Wu, Z.L.1    Bartleson, C.J.2    Ham, A.J.3    Guengerich, F.P.4
  • 40
    • 0020434524 scopus 로고
    • Purification and characterization of liver microsomal cytochromes p-450: electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or beta-naphthoflavone
    • Guengerich F.P., Dannan G.A., Wright S.T., Martin M.V., and Kaminsky L.S. Purification and characterization of liver microsomal cytochromes p-450: electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or beta-naphthoflavone. Biochemistry 21 (1982) 6019-6030
    • (1982) Biochemistry , vol.21 , pp. 6019-6030
    • Guengerich, F.P.1    Dannan, G.A.2    Wright, S.T.3    Martin, M.V.4    Kaminsky, L.S.5
  • 41
    • 0032530954 scopus 로고    scopus 로고
    • Membrane insertion of cytochrome P450 1A2 promoted by anionic phospholipids
    • Ahn T., Guengerich F.P., and Yun C.H. Membrane insertion of cytochrome P450 1A2 promoted by anionic phospholipids. Biochemistry 37 (1998) 12860-12866
    • (1998) Biochemistry , vol.37 , pp. 12860-12866
    • Ahn, T.1    Guengerich, F.P.2    Yun, C.H.3
  • 42
    • 0026569583 scopus 로고
    • Membrane topology of the mammalian P450 cytochromes
    • Black S.D. Membrane topology of the mammalian P450 cytochromes. FASEB J. 6 (1992) 680-685
    • (1992) FASEB J. , vol.6 , pp. 680-685
    • Black, S.D.1
  • 43
    • 0029856855 scopus 로고    scopus 로고
    • Conformational change of cytochrome P450 1A2 induced by sodium chloride
    • Yun C.H., Song M., Ahn T., and Kim H. Conformational change of cytochrome P450 1A2 induced by sodium chloride. J. Biol. Chem. 271 (1996) 31312-31316
    • (1996) J. Biol. Chem. , vol.271 , pp. 31312-31316
    • Yun, C.H.1    Song, M.2    Ahn, T.3    Kim, H.4
  • 44
    • 0030857439 scopus 로고    scopus 로고
    • Conformational change of cytochrome P450 1A2 induced by phospholipids and detergents
    • Yun C.H., Song M., and Kim H. Conformational change of cytochrome P450 1A2 induced by phospholipids and detergents. J. Biol. Chem. 272 (1997) 19725-19730
    • (1997) J. Biol. Chem. , vol.272 , pp. 19725-19730
    • Yun, C.H.1    Song, M.2    Kim, H.3
  • 45
    • 0021138883 scopus 로고
    • On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450. Products of oxygen reduction
    • Gorsky L.D., Koop D.R., and Coon M.J. On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450. Products of oxygen reduction. J. Biol. Chem. 259 (1984) 6812-6817
    • (1984) J. Biol. Chem. , vol.259 , pp. 6812-6817
    • Gorsky, L.D.1    Koop, D.R.2    Coon, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.