메뉴 건너뛰기




Volumn 46, Issue 35, 2007, Pages 10192-10201

Global analysis of protein-protein interactions reveals multiple CYP2E1-reductase complexes

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; COMPLEXATION; CONCENTRATION (PROCESS); DIMERS; TITRATION;

EID: 34548528384     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7003476     Document Type: Article
Times cited : (28)

References (40)
  • 1
    • 33644907149 scopus 로고    scopus 로고
    • A generalized matrix formalism for steady state enzyme kinetics: Application to 17beta-HSD
    • Kuzmic, P. (2006) A generalized matrix formalism for steady state enzyme kinetics: Application to 17beta-HSD, Mol. Cell. Endocrinol. 248, 172-181.
    • (2006) Mol. Cell. Endocrinol , vol.248 , pp. 172-181
    • Kuzmic, P.1
  • 2
    • 0025784027 scopus 로고
    • Cytochrome P-450: Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms
    • Porter, T. D., and Coon, M. J. (1991) Cytochrome P-450: multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms, J. Biol. Chem. 266, 13469-13472.
    • (1991) J. Biol. Chem , vol.266 , pp. 13469-13472
    • Porter, T.D.1    Coon, M.J.2
  • 3
    • 12444335982 scopus 로고    scopus 로고
    • Functional interaction of cytochrome P450 with its redox partners: A critical assessment and update of the topology of predicted contact regions
    • Hlavica, P., Schulze, J., and Lewis, D. F. (2003) Functional interaction of cytochrome P450 with its redox partners: a critical assessment and update of the topology of predicted contact regions, Inorg. Biochem. 96, 279-297.
    • (2003) Inorg. Biochem , vol.96 , pp. 279-297
    • Hlavica, P.1    Schulze, J.2    Lewis, D.F.3
  • 4
    • 0015011537 scopus 로고
    • Biochemical and genetic factors influencing drug metabolism. Influence of hepatic microsomal mixed function oxidation reactions on cellular metabolic control
    • Estabrook, R., Franklin, M. R., Cohen, B., Shigamatzu, A., and Hildebrandt, A. G. (1971) Biochemical and genetic factors influencing drug metabolism. Influence of hepatic microsomal mixed function oxidation reactions on cellular metabolic control, Metabolism 20, 187-199.
    • (1971) Metabolism , vol.20 , pp. 187-199
    • Estabrook, R.1    Franklin, M.R.2    Cohen, B.3    Shigamatzu, A.4    Hildebrandt, A.G.5
  • 5
    • 0027463971 scopus 로고
    • Densities of NADPH-ferrihemoprotein reductase and cytochrome P-450 molecules in the endoplasmic reticulum membrane of rat hepatocytes
    • Watanabe, J., Asaka, Y., Fujimoto, S., and Kanamura, S. (1993) Densities of NADPH-ferrihemoprotein reductase and cytochrome P-450 molecules in the endoplasmic reticulum membrane of rat hepatocytes, J. Histochem. Cytochem. 42, 43-49.
    • (1993) J. Histochem. Cytochem , vol.42 , pp. 43-49
    • Watanabe, J.1    Asaka, Y.2    Fujimoto, S.3    Kanamura, S.4
  • 6
    • 0021112338 scopus 로고
    • Rotation of cytochrome P-450: Complex formation of cytochrome P-450 with NADPH-cytochrome P-450 reductase in liposomes demonstrated by combining protein rotation with antibody-induced cross-linking
    • Gut, J., Richter, C., Cherry, R. J., Winterhalter, K. H., and Kawato, S. (1983) Rotation of cytochrome P-450: complex formation of cytochrome P-450 with NADPH-cytochrome P-450 reductase in liposomes demonstrated by combining protein rotation with antibody-induced cross-linking, J. Biol. Chem. 258, 8588-8594.
    • (1983) J. Biol. Chem , vol.258 , pp. 8588-8594
    • Gut, J.1    Richter, C.2    Cherry, R.J.3    Winterhalter, K.H.4    Kawato, S.5
  • 7
    • 0020147516 scopus 로고
    • Rotational diffusion of cytochrome P-450 in the microsomal membrane-evidence for a clusterlike organization from saturation transfer electron paramagnetic resonance spectroscopy
    • Schwarz, D., Pirrwitz, J., and Ruckpaul, K. (1982) Rotational diffusion of cytochrome P-450 in the microsomal membrane-evidence for a clusterlike organization from saturation transfer electron paramagnetic resonance spectroscopy, Arch. Biochem. Biophys. 216, 322-328.
    • (1982) Arch. Biochem. Biophys , vol.216 , pp. 322-328
    • Schwarz, D.1    Pirrwitz, J.2    Ruckpaul, K.3
  • 9
    • 0023821815 scopus 로고
    • 5, cytochrome c, and cytochrome P-450 interactions with NADPH-cytochrome P-450 reductase in phospholipid vesicles
    • 5, cytochrome c, and cytochrome P-450 interactions with NADPH-cytochrome P-450 reductase in phospholipid vesicles, Biochemistry 27, 5869-5876.
    • (1988) Biochemistry , vol.27 , pp. 5869-5876
    • Nisimoto, Y.1    Otsuka-Murakami, H.2
  • 10
    • 0016752947 scopus 로고
    • Interactions between solubilized cytochrome P-450 and hepatic microsomes
    • Yang, C. S., and Strickhart, F. S. (1975) Interactions between solubilized cytochrome P-450 and hepatic microsomes, J. Biol. Chem. 250, 7968-7972.
    • (1975) J. Biol. Chem , vol.250 , pp. 7968-7972
    • Yang, C.S.1    Strickhart, F.S.2
  • 11
    • 0017875640 scopus 로고
    • Interaction between NADPH-cytochrome P-450 reductase and hepatic microsomes
    • Yang, C. S., Strickhart, F. S., and Kicha, L. P. (1978) Interaction between NADPH-cytochrome P-450 reductase and hepatic microsomes, Biochim. Biophys. Acta 509, 326-337.
    • (1978) Biochim. Biophys. Acta , vol.509 , pp. 326-337
    • Yang, C.S.1    Strickhart, F.S.2    Kicha, L.P.3
  • 12
    • 0018786901 scopus 로고
    • Studies on the association of cytochrome P-450 and NADPH-cytochrome c reductase during catalysis in a reconstituted hydroxylating system
    • Miwa, G. T., West, S. B., Huang, M. T., and Lu, A. Y. (1979) Studies on the association of cytochrome P-450 and NADPH-cytochrome c reductase during catalysis in a reconstituted hydroxylating system, J. Biol. Chem. 254, 5695-5700.
    • (1979) J. Biol. Chem , vol.254 , pp. 5695-5700
    • Miwa, G.T.1    West, S.B.2    Huang, M.T.3    Lu, A.Y.4
  • 13
    • 0026035519 scopus 로고
    • Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects
    • Guengerich, F. P., Kim, D. H., and Iwasaki, M. (1991) Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects, Chem. Res. Toxicol. 4, 168-79.
    • (1991) Chem. Res. Toxicol , vol.4 , pp. 168-179
    • Guengerich, F.P.1    Kim, D.H.2    Iwasaki, M.3
  • 15
    • 0030602654 scopus 로고    scopus 로고
    • 5 in the oxidation of 7-ethoxycoumarin, chlorzoxazone, aniline, and N-nitrosodimethylamine by recombinant cytochrome P450 2E1 and by human liver microsomes
    • 5 in the oxidation of 7-ethoxycoumarin, chlorzoxazone, aniline, and N-nitrosodimethylamine by recombinant cytochrome P450 2E1 and by human liver microsomes, Biochem. Pharmacol. 52, 301-309.
    • (1996) Biochem. Pharmacol , vol.52 , pp. 301-309
    • Yamazaki, H.1    Nakano, M.2    Gillam, E.M.J.3    Guengerich, F.P.4    Shimada, T.5
  • 16
    • 0031588947 scopus 로고    scopus 로고
    • Molecular modelling of CYP2E1 enzymes from rat, mouse and man: An explanation for species differences in butadiene metabolism and potential carcinogenicity, and rationalization of CYP2E substrate specificity
    • Lewis, D. F., Bird, M. G., and Parke, D. V. (1997) Molecular modelling of CYP2E1 enzymes from rat, mouse and man: an explanation for species differences in butadiene metabolism and potential carcinogenicity, and rationalization of CYP2E substrate specificity, Toxicology 118, 93-113.
    • (1997) Toxicology , vol.118 , pp. 93-113
    • Lewis, D.F.1    Bird, M.G.2    Parke, D.V.3
  • 17
    • 17444368995 scopus 로고    scopus 로고
    • Engineering of proteolytically stable NADPH-cytochrome P450 reductase
    • Bonina, T. A., Gilep, A. A., Estabrook, R. W., and Usanov, S. A. (2005) Engineering of proteolytically stable NADPH-cytochrome P450 reductase, Biochemistry (Moscow) 70, 357-365.
    • (2005) Biochemistry (Moscow) , vol.70 , pp. 357-365
    • Bonina, T.A.1    Gilep, A.A.2    Estabrook, R.W.3    Usanov, S.A.4
  • 18
    • 33847096845 scopus 로고    scopus 로고
    • CYP2E1 active site residues in substrate recognition sequence 5 identified by photoaffinity labeling and homology modeling
    • Collom, S. L., Jamakhandi, A. P., Tackett, A. J., Radominska-Pandya, A., and Miller, G. P. (2007) CYP2E1 active site residues in substrate recognition sequence 5 identified by photoaffinity labeling and homology modeling, Arch. Biochem. Biophys. 459, 59-69.
    • (2007) Arch. Biochem. Biophys , vol.459 , pp. 59-69
    • Collom, S.L.1    Jamakhandi, A.P.2    Tackett, A.J.3    Radominska-Pandya, A.4    Miller, G.P.5
  • 19
    • 0032530282 scopus 로고    scopus 로고
    • Interactions among P450 enzymes when combined in reconstituted systems: Formation of a 2B4-1A2 complex with a high affinity for NADPH-cytochrome P450 reductase
    • Backes, W. L., Batie, C. J., and Cawley, G. F. (1998) Interactions among P450 enzymes when combined in reconstituted systems: formation of a 2B4-1A2 complex with a high affinity for NADPH-cytochrome P450 reductase, Biochemistry 37, 12852-12859.
    • (1998) Biochemistry , vol.37 , pp. 12852-12859
    • Backes, W.L.1    Batie, C.J.2    Cawley, G.F.3
  • 20
    • 25844503055 scopus 로고    scopus 로고
    • Association of cytochrome P450 enzymes is a determining factor in their catalytic activity
    • Hazai, E., Bikadi, Z., Simonyi, M., and Kupfer, D. (2005) Association of cytochrome P450 enzymes is a determining factor in their catalytic activity, J. Comput.-Aided Mol. Des. 19, 271-85.
    • (2005) J. Comput.-Aided Mol. Des , vol.19 , pp. 271-285
    • Hazai, E.1    Bikadi, Z.2    Simonyi, M.3    Kupfer, D.4
  • 21
    • 0348226986 scopus 로고    scopus 로고
    • High-level expression of recombinant rabbit cytochrome P450 2E1 in Escherichia coli C41 and its purification
    • Cheng, D., Kelley, R. W., Cawley, G. F., and Backes, W. L. (2004) High-level expression of recombinant rabbit cytochrome P450 2E1 in Escherichia coli C41 and its purification, Protein Expression Purif. 33, 66-71.
    • (2004) Protein Expression Purif , vol.33 , pp. 66-71
    • Cheng, D.1    Kelley, R.W.2    Cawley, G.F.3    Backes, W.L.4
  • 23
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase, Anal. Biochem. 237, 260-273.
    • (1996) Anal. Biochem , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 24
    • 33947088324 scopus 로고    scopus 로고
    • I, T.-P., and Nancollas, G. H. (1972) EQUIL - A general computational method for the calculation of solution equilibria, Anal. Chem. 44, 1940-1950.
    • I, T.-P., and Nancollas, G. H. (1972) EQUIL - A general computational method for the calculation of solution equilibria, Anal. Chem. 44, 1940-1950.
  • 27
    • 0001511660 scopus 로고
    • Recherches sur la formation de complexes mineraux en solution, et sur leur stabilité
    • Job, P. (1928) Recherches sur la formation de complexes mineraux en solution, et sur leur stabilité, Ann. Chim. (Paris) 9, 113-203.
    • (1928) Ann. Chim. (Paris) , vol.9 , pp. 113-203
    • Job, P.1
  • 31
    • 14044278205 scopus 로고    scopus 로고
    • Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2
    • Kelley, R. W., Reed, J. R., and Backes, W. L. (2005) Effects of ionic strength on the functional interactions between CYP2B4 and CYP1A2, Biochemistry 44, 2632-2641.
    • (2005) Biochemistry , vol.44 , pp. 2632-2641
    • Kelley, R.W.1    Reed, J.R.2    Backes, W.L.3
  • 32
    • 0020440236 scopus 로고
    • Determination of binding stoichiometry by the continuous variation method: The Job plot
    • Huang, C. Y. (1982) Determination of binding stoichiometry by the continuous variation method: the Job plot, Methods Enzymol. 87, 509-525.
    • (1982) Methods Enzymol , vol.87 , pp. 509-525
    • Huang, C.Y.1
  • 33
    • 0019818431 scopus 로고
    • Studies on the stimulation of cytochrome P-450-dependent monooxygenase activity by dilauroylphosphatidylcholine
    • Miwa, G. T., and Lu, A. Y. H. (1981) Studies on the stimulation of cytochrome P-450-dependent monooxygenase activity by dilauroylphosphatidylcholine, Arch. Biochem. Biophys. 211, 454-458.
    • (1981) Arch. Biochem. Biophys , vol.211 , pp. 454-458
    • Miwa, G.T.1    Lu, A.Y.H.2
  • 34
    • 0021707118 scopus 로고
    • The association of cytochrome P-450 and NADPH-cytochrome P-450 reductase in phospholipid membranes
    • Miwa, G. T., and Lu, A. Y. H. (1984) The association of cytochrome P-450 and NADPH-cytochrome P-450 reductase in phospholipid membranes, Arch. Biochem. Biophys. 234, 161-166.
    • (1984) Arch. Biochem. Biophys , vol.234 , pp. 161-166
    • Miwa, G.T.1    Lu, A.Y.H.2
  • 36
    • 0020491479 scopus 로고
    • Relationship between state of aggregation and catalytic activity for cytochrome P-450LM2 and NADPH-cytochrome P-450 reductase
    • Dean, W. L., and Gray, R. D. (1982) Relationship between state of aggregation and catalytic activity for cytochrome P-450LM2 and NADPH-cytochrome P-450 reductase, J. Biol. Chem. 257, 14679-14685.
    • (1982) J. Biol. Chem , vol.257 , pp. 14679-14685
    • Dean, W.L.1    Gray, R.D.2
  • 37
    • 0037408258 scopus 로고    scopus 로고
    • Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes
    • Backes, W. L., and Kelley, R. W. (2003) Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes, Pharmacol. Ther. 98, 221-233.
    • (2003) Pharmacol. Ther , vol.98 , pp. 221-233
    • Backes, W.L.1    Kelley, R.W.2
  • 38
    • 11144328243 scopus 로고    scopus 로고
    • Interactions between Cyp2C9 and Cyp2C19 in reconstituted binary systems influence their catalytic activity: Possible rationale for the inability of Cyp2C19 to catalyze methoxychlor demethylation in human liver microsomes
    • Hazai, E., and Kupfer, D. (2005) Interactions between Cyp2C9 and Cyp2C19 in reconstituted binary systems influence their catalytic activity: Possible rationale for the inability of Cyp2C19 to catalyze methoxychlor demethylation in human liver microsomes, Drug Metab. Dispos. 33, 157-164.
    • (2005) Drug Metab. Dispos , vol.33 , pp. 157-164
    • Hazai, E.1    Kupfer, D.2
  • 39
    • 0035699972 scopus 로고    scopus 로고
    • Association of cytochromes P450 1A2 and 2B4: Are the interactions between different P450 species involved in the control of the monooxygenase activity and coupling?
    • Davydov, D. R., Petushkova, N. A., Bobrovnikova, E. V., Knyushko, T. V., and Dansette, P. (2001) Association of cytochromes P450 1A2 and 2B4: are the interactions between different P450 species involved in the control of the monooxygenase activity and coupling?, Adv. Exp. Med. Biol. 500, 335-338.
    • (2001) Adv. Exp. Med. Biol , vol.500 , pp. 335-338
    • Davydov, D.R.1    Petushkova, N.A.2    Bobrovnikova, E.V.3    Knyushko, T.V.4    Dansette, P.5
  • 40
    • 0026719686 scopus 로고
    • Global analysis of biochemical and biophysical data
    • Beechem, J. M. (1992) Global analysis of biochemical and biophysical data, Methods Enzymol. 210, 37-54.
    • (1992) Methods Enzymol , vol.210 , pp. 37-54
    • Beechem, J.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.