메뉴 건너뛰기




Volumn 42, Issue 51, 2003, Pages 15068-15077

Direct Interaction between Substrates and Endogenous Steroids in the Active Site May Change the Activity of Cytochrome P450 3A4

Author keywords

[No Author keywords available]

Indexed keywords

BENZENE; HYDROXYLATION; MATHEMATICAL MODELS; METABOLISM; SUBSTRATES;

EID: 0346963231     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034409n     Document Type: Article
Times cited : (45)

References (46)
  • 1
    • 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
  • 2
    • 0025184340 scopus 로고
    • Mechanism-based inactivation of human liver microsomal cytochrome P-450 IIIA4 by gestodene
    • Guengerich, F. P. (1990) Mechanism-based inactivation of human liver microsomal cytochrome P-450 IIIA4 by gestodene, Chem. Res. Toxicol. 3, 363-371.
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 363-371
    • Guengerich, F.P.1
  • 4
    • 0027763629 scopus 로고
    • Cortisol metabolism in vitro-III. Inhibition of microsomal 6 beta-hydroxylase and cytosolic 4-ene-reductase
    • Abel, S. M., and Back, D. J. (1993) Cortisol metabolism in vitro-III. Inhibition of microsomal 6 beta-hydroxylase and cytosolic 4-ene-reductase, J. Steroid Biochem. Mol. Biol. 46, 827-832.
    • (1993) J. Steroid Biochem. Mol. Biol. , vol.46 , pp. 827-832
    • Abel, S.M.1    Back, D.J.2
  • 5
    • 0023929834 scopus 로고
    • Human liver microsomal steroid metabolism: Identification of the major microsomal steroid hormone 6 beta-hydroxylase cytochrome P-450 enzyme
    • Waxman, D. J., Attisano, C., Guengerich, F. P., and Lapenson, D. P. (1988) Human liver microsomal steroid metabolism: identification of the major microsomal steroid hormone 6 beta-hydroxylase cytochrome P-450 enzyme, Arch. Biochem. Biophys. 263, 424-436.
    • (1988) Arch. Biochem. Biophys. , vol.263 , pp. 424-436
    • Waxman, D.J.1    Attisano, C.2    Guengerich, F.P.3    Lapenson, D.P.4
  • 6
    • 0026451998 scopus 로고
    • Nature of cytochromes P450 involved in the 2-/4-hydroxylations of estradiol in human liver microsomes
    • Kerlan, V., Dreano, Y., Bercovici, J. P., Beaune, P. H., Floch, H. H., and Berthou, F. (1992) Nature of cytochromes P450 involved in the 2-/4-hydroxylations of estradiol in human liver microsomes, Biochem. Pharmacol. 3, 1745-1756.
    • (1992) Biochem. Pharmacol. , vol.3 , pp. 1745-1756
    • Kerlan, V.1    Dreano, Y.2    Bercovici, J.P.3    Beaune, P.H.4    Floch, H.H.5    Berthou, F.6
  • 7
    • 0031260323 scopus 로고    scopus 로고
    • Progesterone and testosterone hydroxylation by cytochromes P450 2C19, 2C9, and 3A4 in human liver microsomes
    • Yamazaki, H., and Shimada, T. (1997) Progesterone and testosterone hydroxylation by cytochromes P450 2C19, 2C9, and 3A4 in human liver microsomes, Arch. Biochem. Biophys. 346, 161-169.
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 161-169
    • Yamazaki, H.1    Shimada, T.2
  • 9
    • 0021800943 scopus 로고
    • Identification of the cytochrome P-450 induced by macrolide antibiotics in rat liver as the glucocorticoid responsive cytochrome P-450
    • Wrighton, S. A., Maurel, P, Schuetz, E. G., Watkins, P. B., Young, B., and Guzelian, P. S. (1985) Identification of the cytochrome P-450 induced by macrolide antibiotics in rat liver as the glucocorticoid responsive cytochrome P-450, Biochemistry 24, 2171-2178.
    • (1985) Biochemistry , vol.24 , pp. 2171-2178
    • Wrighton, S.A.1    Maurel, P.2    Schuetz, E.G.3    Watkins, P.B.4    Young, B.5    Guzelian, P.S.6
  • 10
    • 0023949862 scopus 로고
    • Modulation of rabbit and human hepatic cytochrome P-450-catalyzed steroid hydroxylations by alpha-naphthoflavone
    • Schwab, G. E., Raucy, J. L., and Johnson, E. F. (1988) Modulation of rabbit and human hepatic cytochrome P-450-catalyzed steroid hydroxylations by alpha-naphthoflavone, Mol. Pharmacol. 33, 493-499.
    • (1988) Mol. Pharmacol. , vol.33 , pp. 493-499
    • Schwab, G.E.1    Raucy, J.L.2    Johnson, E.F.3
  • 11
    • 0024269576 scopus 로고
    • Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c
    • Johnson, E. F., Schwab, G. E., and Vickery, L. E. (1988) Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c, J. Biol. Chem. 263, 17672-17677.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17672-17677
    • Johnson, E.F.1    Schwab, G.E.2    Vickery, L.E.3
  • 12
    • 0031028518 scopus 로고    scopus 로고
    • Cooperativity in oxidations catalyzed by cytochrome P450 3A4
    • Ueng, Y. F., Kuwabara, T., Chun, Y. J., and Guengerich, F. P. (1997) Cooperativity in oxidations catalyzed by cytochrome P450 3A4, Biochemistry 36, 370-381.
    • (1997) Biochemistry , vol.36 , pp. 370-381
    • Ueng, Y.F.1    Kuwabara, T.2    Chun, Y.J.3    Guengerich, F.P.4
  • 13
    • 0000227103 scopus 로고    scopus 로고
    • Identification of three key residues in substrate recognition site 5 of human cytochrome P450 3A4 by cassette and site-directed mutagenesis
    • He, Y. A., He, Y. Q., Szklarz, G. D., and Halpert, J. R. (1997) Identification of three key residues in substrate recognition site 5 of human cytochrome P450 3A4 by cassette and site-directed mutagenesis, Biochemistry 36, 8831-8839.
    • (1997) Biochemistry , vol.36 , pp. 8831-8839
    • He, Y.A.1    He, Y.Q.2    Szklarz, G.D.3    Halpert, J.R.4
  • 14
    • 0031041652 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of a putative substrate recognition site in human cytochrome P450 3A4. Role of residues 210 and 211 in flavonoid activation and substrate specificity
    • Harlow, G. R., and Halpert, J. R. (1997) Alanine-scanning mutagenesis of a putative substrate recognition site in human cytochrome P450 3A4. Role of residues 210 and 211 in flavonoid activation and substrate specificity, J. Biol. Chem. 272, 5396-5402.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5396-5402
    • Harlow, G.R.1    Halpert, J.R.2
  • 15
    • 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., Parise, 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    Parise, R.A.5    Rettie, A.E.6    Gonzalez, F.J.7    Tracy, T.S.8
  • 16
    • 0033045179 scopus 로고    scopus 로고
    • Activation of human cytochrome P450 3A4 catalyzed meloxicam 5′-methylhydroxylation by quinidine and hydro-quinidine in vitro
    • Ludwig, E., Schmid, J., Beschke, K., and Ebner, T. (1999) Activation of human cytochrome P450 3A4 catalyzed meloxicam 5′-methylhydroxylation by quinidine and hydro-quinidine in vitro, J. Pharmacol. Exp. Ther. 290, 1-8.
    • (1999) J. Pharmacol. Exp. Ther. , vol.290 , pp. 1-8
    • Ludwig, E.1    Schmid, J.2    Beschke, K.3    Ebner, T.4
  • 17
    • 0034105896 scopus 로고    scopus 로고
    • In vitro-in vivo scaling of CYP kinetic data not consistent with the classical Michaelis-Menten model
    • Houston, J. B., and Kenworthy, K. E. (2000) In vitro-in vivo scaling of CYP kinetic data not consistent with the classical Michaelis-Menten model, Drug Metab. Dispos. 28, 246-254.
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 246-254
    • Houston, J.B.1    Kenworthy, K.E.2
  • 18
    • 0035910579 scopus 로고    scopus 로고
    • A kinetic model for the metabolic interaction of two substrates at the active site of cytochrome P450 3A4
    • Shou, M., Dai, R., Cui, D., Korzekwa, K. R., Baillie, T. A., and Rushmore, T. H. (2001) A kinetic model for the metabolic interaction of two substrates at the active site of cytochrome P450 3A4, J. Biol. Chem. 276, 2256-2262.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2256-2262
    • Shou, M.1    Dai, R.2    Cui, D.3    Korzekwa, K.R.4    Baillie, T.A.5    Rushmore, T.H.6
  • 19
    • 0035193493 scopus 로고    scopus 로고
    • Multisite kinetic models for CYP3A4: Simultaneous activation and inhibition of diazepam and testosterone metabolism
    • Kenworthy, K. E., Clarke, S. E., Andrews, J., and Houston, J. B. (2001) Multisite kinetic models for CYP3A4: simultaneous activation and inhibition of diazepam and testosterone metabolism, Drug Metab. Dispos. 29, 1644-1651.
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 1644-1651
    • Kenworthy, K.E.1    Clarke, S.E.2    Andrews, J.3    Houston, J.B.4
  • 20
    • 0032499691 scopus 로고    scopus 로고
    • Analysis of human cytochrome P450 3A4 cooperativity: Construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics
    • Harlow, G. R., and Halpert, J. R. (1998) Analysis of human cytochrome P450 3A4 cooperativity: construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics, Proc. Natl. Acad. Sci. U.S.A. 95, 6636-6641.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6636-6641
    • Harlow, G.R.1    Halpert, J.R.2
  • 21
  • 22
    • 0031031676 scopus 로고    scopus 로고
    • Structure of cytochrome P450eryF: Substrate, inhibitors, and model compounds bound in the active site
    • Cupp-Vickery, J. R., and Poulos, T. L. (1997) Structure of cytochrome P450eryF: Substrate, inhibitors, and model compounds bound in the active site, Steroids 62, 112-116.
    • (1997) Steroids , vol.62 , pp. 112-116
    • Cupp-Vickery, J.R.1    Poulos, T.L.2
  • 23
    • 0034724310 scopus 로고    scopus 로고
    • Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity
    • Cupp-Vickery, J., Anderson, R., and Hatziris, Z. (2000) Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity, Proc. Natl. Acad. Sci. U.S.A. 97, 3050-3055.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3050-3055
    • Cupp-Vickery, J.1    Anderson, R.2    Hatziris, Z.3
  • 24
    • 0031005752 scopus 로고    scopus 로고
    • Human cytochrome P450 3A4-catalyzed testosterone 6 beta-hydroxylation and erythromycin N-demethylation
    • Wang, R. W., Newton, D. J., Scheri, T. D., and Lu, A. Y. (1997) Human cytochrome P450 3A4-catalyzed testosterone 6 beta-hydroxylation and erythromycin N-demethylation, Drug Metab. Dispos. 25, 502-507.
    • (1997) Drug Metab. Dispos. , vol.25 , pp. 502-507
    • Wang, R.W.1    Newton, D.J.2    Scheri, T.D.3    Lu, A.Y.4
  • 25
    • 0028307539 scopus 로고
    • Activation of CYP3A4: Evidence for the simultaneous binding of two substrates in a cytochrome P450 active site
    • Shou, M., Grogan, J., Mancewicz, J. A., Krausz, K. W., Gonzalez, F. J., Gelboin, H. V., and Korzekwa, K. R. (1994) Activation of CYP3A4: evidence for the simultaneous binding of two substrates in a cytochrome P450 active site, Biochemistry 33, 6450-6455.
    • (1994) Biochemistry , vol.33 , pp. 6450-6455
    • Shou, M.1    Grogan, J.2    Mancewicz, J.A.3    Krausz, K.W.4    Gonzalez, F.J.5    Gelboin, H.V.6    Korzekwa, K.R.7
  • 26
    • 0032496311 scopus 로고    scopus 로고
    • Differential catalytic properties in metabolism of endogenous and exogenous substrates among CYP3A enzymes expressed in COS-7 cells
    • Ohmori, S., Nakasa, H., Asanome, K., Kurose, Y., Ishii, I., Hosokawa, M., and Kitada, M. (1998) Differential catalytic properties in metabolism of endogenous and exogenous substrates among CYP3A enzymes expressed in COS-7 cells, Biochim. Biophys. Acta 1380, 297-304.
    • (1998) Biochim. Biophys. Acta , vol.1380 , pp. 297-304
    • Ohmori, S.1    Nakasa, H.2    Asanome, K.3    Kurose, Y.4    Ishii, I.5    Hosokawa, M.6    Kitada, M.7
  • 28
    • 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, 2370-2385.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2385
    • Omura, T.1    Sato, R.2
  • 29
    • 73849173955 scopus 로고
    • Hepatic triphosphopyridine nucleotide-cytochrome c reductase
    • Phillips, A. H., and Langdon, R. J. (1962) Hepatic triphosphopyridine nucleotide-cytochrome c reductase, J. Biol. Chem. 237, 2652-2790.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2652-2790
    • Phillips, A.H.1    Langdon, R.J.2
  • 30
  • 31
    • 0032701771 scopus 로고    scopus 로고
    • Biotransformation of nevirapine, a nonnucleoside HIV-1 reverse transcriptase inhibitor, in mice, rats, rabbits, dogs, monkeys, and chimpanzees
    • Riska, P. S., Joseph, D. P., Dinallo, R. M., Davidson, W. C., Keirns, J. J., and Hattox, S. E. (1999) Biotransformation of nevirapine, a nonnucleoside HIV-1 reverse transcriptase inhibitor, in mice, rats, rabbits, dogs, monkeys, and chimpanzees, Drug Metab. Dispos. 27, 1434-1447.
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 1434-1447
    • Riska, P.S.1    Joseph, D.P.2    Dinallo, R.M.3    Davidson, W.C.4    Keirns, J.J.5    Hattox, S.E.6
  • 32
    • 0034108229 scopus 로고    scopus 로고
    • Dual role of human cytochrome P450 3A4 residue Phe-304 in substrate specificity and cooperativity
    • Domanski, T. L., He, Y. A., Harlow, G. R., and Halpert, J. R. (2000) Dual role of human cytochrome P450 3A4 residue Phe-304 in substrate specificity and cooperativity, J. Pharmacol. Exp. Ther. 293, 585-591.
    • (2000) J. Pharmacol. Exp. Ther. , vol.293 , pp. 585-591
    • Domanski, T.L.1    He, Y.A.2    Harlow, G.R.3    Halpert, J.R.4
  • 33
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of nonlinear parameters
    • Marquardt, D. W. (1963) An algorithm for least-squares estimation of nonlinear parameters, J. Soc. Ind. Appl. 11, 431-441.
    • (1963) J. Soc. Ind. Appl. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 34
    • 0004016501 scopus 로고
    • Composition of simple potential functions for simulating liquid water
    • Jorgensen, W. L., Chandrasekhar, J., and Madura, J. D. (1983) Composition of simple potential functions for simulating liquid water, J. Chem. Phys. 79, 926-935.
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3
  • 37
    • 84988053694 scopus 로고
    • An all-atom force field for simulations of proteins and nuclei acid
    • Weiner, S. J., Kollman, P. A., Nguyen, D. T., and Case, D. A. (1986) An all-atom force field for simulations of proteins and nuclei acid, J. Comput. Chem. 7, 230-252.
    • (1986) J. Comput. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 39
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke, A. D. (1993) Density-functional thermochemistry. III. The role of exact exchange, J. Chem. Phys. 98, 5648-5652.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 40
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • Lee, C., Yang, W., and Parr, R. G. (1988) Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density, Phys. Rev. B37, 785-789.
    • (1988) Phys. Rev. , vol.B37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 41
    • 0037045235 scopus 로고    scopus 로고
    • Origin of attraction and directionality of the π/π interaction: Model chemistry calculations of benzene dimer interaction
    • Tsuzuki, S., Honda, K., Uchimaru, T., Mikami, M., and Tanabe, K. (2002) Origin of attraction and directionality of the π/π interaction: model chemistry calculations of benzene dimer interaction, J. Am. Chem. Soc. 124, 104-112.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 104-112
    • Tsuzuki, S.1    Honda, K.2    Uchimaru, T.3    Mikami, M.4    Tanabe, K.5
  • 42
    • 0242276321 scopus 로고    scopus 로고
    • CYP3A4 and CYP3A7-Mediated Carbamazepine 10,11-Epoxidation Are Activated by Differential Endogenous Steroids
    • Nakamura, H., Torimoto, N., Ishii, I., Ariyoshi, N., Nakasa, H., Ohmori, S., and Kitada, M. (2003) CYP3A4 and CYP3A7-Mediated Carbamazepine 10,11-Epoxidation Are Activated by Differential Endogenous Steroids, Drug Metab. Dispos. 31, 432-438.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 432-438
    • Nakamura, H.1    Torimoto, N.2    Ishii, I.3    Ariyoshi, N.4    Nakasa, H.5    Ohmori, S.6    Kitada, M.7
  • 43
    • 0037229515 scopus 로고    scopus 로고
    • Analysis of homotropic and heterotropic cooperativity of diazepam oxidation by CYP3A4 using site-directed mutagenesis and kinetic modeling
    • He, Y. A., Roussel, F., and Halpert, J. R. (2003) Analysis of homotropic and heterotropic cooperativity of diazepam oxidation by CYP3A4 using site-directed mutagenesis and kinetic modeling, Arch. Biochem. Biophys. 409, 92-101.
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 92-101
    • He, Y.A.1    Roussel, F.2    Halpert, J.R.3
  • 44
    • 0036178095 scopus 로고    scopus 로고
    • Midazolam Oxidation by cytochrome P450 3A4 and active-site mutations: And evaluation of multiple binding sites and of the metabolic pathway that leads to enzyme
    • Khan, K. K., He, Y. A., Domanski, T. L., and Halpert, J. R. (2002) Midazolam Oxidation by cytochrome P450 3A4 and active-site mutations: and evaluation of multiple binding sites and of the metabolic pathway that leads to enzyme, Mol. Pharmacol. 61, 495-506.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 495-506
    • Khan, K.K.1    He, Y.A.2    Domanski, T.L.3    Halpert, J.R.4
  • 45
    • 0037048522 scopus 로고    scopus 로고
    • Pyrene-Pyrene complexes at the active site of cytochrome P450 3A4: Evidence for a multiple substrate binding site
    • Dabrowski, M. J., Schrag, M. L., Wienkers, L. C., and Atkins, W. M. (2002) Pyrene-Pyrene complexes at the active site of cytochrome P450 3A4: Evidence for a multiple substrate binding site, J. Am. Chem. Soc. 124, 11866-11867.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11866-11867
    • Dabrowski, M.J.1    Schrag, M.L.2    Wienkers, L.C.3    Atkins, W.M.4
  • 46
    • 0042265520 scopus 로고    scopus 로고
    • Crystal structure of human cytochrome P450 2C9 with bound warfarin
    • Williams, P. A., Cosme, J., Ward, A., Angove, H., C., Vinkovic, D. M., and Jhoti, H. (2003) Crystal structure of human cytochrome P450 2C9 with bound warfarin, Nature 424, 464-466.
    • (2003) Nature , vol.424 , pp. 464-466
    • Williams, P.A.1    Cosme, J.2    Ward, A.3    Angove, H.4    Vinkovic, D.M.5    Jhoti, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.