메뉴 건너뛰기




Volumn 2, Issue 2, 1998, Pages 263-268

Cytochrome P450 monooxygenases

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS);

EID: 0032039678     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(98)80068-9     Document Type: Article
Times cited : (78)

References (44)
  • 2
    • 0001733185 scopus 로고    scopus 로고
    • Plant cytochrome P450 monooxygenases
    • A timely, comprehensive and critical review of the chemistry and biology of plant P450 enzymes
    • Schular MA: Plant cytochrome P450 monooxygenases. Crit Rev Plant Sci 1996, 15:235-284. A timely, comprehensive and critical review of the chemistry and biology of plant P450 enzymes.
    • (1996) Crit Rev Plant Sci , vol.15 , pp. 235-284
    • Ma, S.1
  • 5
    • 0000462317 scopus 로고    scopus 로고
    • Direct measurement of the reduction potential of catalytically active cytochrome c peroxidase Compound I: Voltametric detection of a reversible, cooperative two-electron transfer reaction
    • Madhu S, Fuller H, Armstrong FA: Direct measurement of the reduction potential of catalytically active cytochrome c peroxidase Compound I: Voltametric detection of a reversible, cooperative two-electron transfer reaction. J Am Chem Soc 1996, 118:263-264.
    • (1996) J Am Chem Soc , vol.118 , pp. 263-264
    • Madhu, S.1    Fuller, H.2    Armstrong, F.A.3
  • 6
    • 0029140873 scopus 로고
    • An incredibly fast apparent oxygen rebound rate constant for hydrocarbon activation by cytochrome P450 enzymes
    • Newcomb M, Le Tadic M-H, Putt D, Hollenberg PF: An incredibly fast apparent oxygen rebound rate constant for hydrocarbon activation by cytochrome P450 enzymes. J Am Chem Soc 1995, 117:3312-3313.
    • (1995) J Am Chem Soc , vol.117 , pp. 3312-3313
    • Newcomb, M.1    Le Tadic, M.-H.2    Putt, D.3    Hollenberg, P.F.4
  • 7
    • 8944253773 scopus 로고    scopus 로고
    • Regiochemical variations in reactions of methylcubane with tert-butoxyl radical, cytochrome P450 enzymes, and a methane monooxygenase system
    • Choi S-Y, Eaton PE, Hollenberg PF, Liu KE, Lippard SJ, Newcomb M, Putt DA, Upadhyaya SP, Xiong Y: Regiochemical variations in reactions of methylcubane with tert-butoxyl radical, cytochrome P450 enzymes, and a methane monooxygenase system. J Am Chem Soc 1996, 118:6547-6555. A detailed investigation into the kinetics of CÆH bond activation in which the reactivities of a tert-butoxyl radical and two monooxygenase enzymes are compared to generate new and important insights into the elementary step of C-H activation by biological systems.
    • (1996) J Am Chem Soc , vol.118 , pp. 6547-6555
    • Choi, S.-Y.1    Eaton, P.E.2    Hollenberg, P.F.3    Liu, K.E.4    Lippard, S.J.5    Newcomb, M.6    Putt, D.A.7    Upadhyaya, S.P.8    Xiong, Y.9
  • 8
    • 0026485793 scopus 로고
    • High-level expression in Escherichia coli of enzymatically active fusion proteins containing the domains of mammalian cytochromes P450 and NADPH-P450 reductase flavoprotein
    • Fisher CW, Shet MS, Caudle DL, Martin-Wixtrom CA, Estabrook RW: High-level expression in Escherichia coli of enzymatically active fusion proteins containing the domains of mammalian cytochromes P450 and NADPH-P450 reductase flavoprotein. Proc Natl Acad Sci USA 1992, 89:10817-10821.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10817-10821
    • Fisher, C.W.1    Shet, M.S.2    Caudle, D.L.3    Martin-Wixtrom, C.A.4    Estabrook, R.W.5
  • 9
    • 0031106383 scopus 로고    scopus 로고
    • The function of recombinant cytochrome P450s in intact Escherichia coli cells: The 17 α-hydroxylation of progesterone and pregnenolone by P450c17
    • Shet MS, Fisher CW, Estabrook RW: The function of recombinant cytochrome P450s in intact Escherichia coli cells: the 17 α-hydroxylation of progesterone and pregnenolone by P450c17. Arch Biochem Biophys 1997, 339:218-225. This paper describes the functional expression of a fusion protein and the in vivo oxidation of steroids as an example of biotransformation using P450 enzymes for the synthesis of biologically active compounds.
    • (1997) Arch Biochem Biophys , vol.339 , pp. 218-225
    • Shet, M.S.1    Fisher, C.W.2    Estabrook, R.W.3
  • 10
    • 0029124814 scopus 로고
    • In vitro metabolism of terfenadine by a purified recombinant fusion protein containing cytochrome P4503A4 and NADPH-P450 reductase. Comparison to human liver microsomes and precision-cut liver tissue slices
    • Rodrigues AD, Mulford DJ, Lee RD, Surber BW, Kukulka MJ, Ferrero JL, Thomas SB, Shet MS, Estabrook RW: In vitro metabolism of terfenadine by a purified recombinant fusion protein containing cytochrome P4503A4 and NADPH-P450 reductase. Comparison to human liver microsomes and precision-cut liver tissue slices. Drug Metab Dispos 1995, 23:765-775.
    • (1995) Drug Metab Dispos , vol.23 , pp. 765-775
    • Rodrigues, A.D.1    Mulford, D.J.2    Lee, R.D.3    Surber, B.W.4    Kukulka, M.J.5    Ferrero, J.L.6    Thomas, S.B.7    Shet, M.S.8    Estabrook, R.W.9
  • 11
    • 0030843652 scopus 로고    scopus 로고
    • Drug metabolism by Escherichia coli expressing human cytochromes P450
    • Parikh A, Gillman EMJ, Guengerich FP: Drug metabolism by Escherichia coli expressing human cytochromes P450. Nat Biotechnol 1997, 15:784-788. This excellent paper summarizes the methodologies of functional expression of human P450 enzymes which metabolize drugs and other xenobiotics. The recombinant P450 enzymes expressed as fusions with NADPH P450 reductases are incorporated into membranes and the whole cell oxidation of a number of drugs and xenobiotics is described.
    • (1997) Nat Biotechnol , vol.15 , pp. 784-788
    • Parikh, A.1    Gillman, E.M.J.2    Guengerich, F.P.3
  • 12
    • 0030021980 scopus 로고    scopus 로고
    • Mutagenesis study of Asp-290 in cytochrome P450 2B11 using a fusion protein with rat NADPH-cytochrome P450 reductase
    • Harlow GR, Halpert JR: Mutagenesis study of Asp-290 in cytochrome P450 2B11 using a fusion protein with rat NADPH-cytochrome P450 reductase. Arch Biochem Biophys 1996, 326:85-92.
    • (1996) Arch Biochem Biophys , vol.326 , pp. 85-92
    • Harlow, G.R.1    Halpert, J.R.2
  • 16
    • 0029739962 scopus 로고    scopus 로고
    • Application of electrochemistry for P450-catalysed reactions
    • Estabrook RW, Faulkner KM, Shet MS, Fisher CW: Application of electrochemistry for P450-catalysed reactions. Methods Enzymol 1996, 272:44-51. A very interesting review of electrochemically driven substrate turnover by a number of mammalian P450 enzymes.
    • (1996) Methods Enzymol , vol.272 , pp. 44-51
    • Estabrook, R.W.1    Faulkner, K.M.2    Shet, M.S.3    Fisher, C.W.4
  • 17
    • 0030474192 scopus 로고    scopus 로고
    • The use of electrochemistry for the synthesis of 17 alpha-hydroxyprogesterone by a fusion protein containing P450c17
    • Estabrook RW, Shet MS, Faulkner K, Fisher CW: The use of electrochemistry for the synthesis of 17 alpha-hydroxyprogesterone by a fusion protein containing P450c17. Endocr Res 1996, 22:665-671. An outstanding example of the electrochemical synthesis of a biologically active compound using P450 enzymes.
    • (1996) Endocr Res , vol.22 , pp. 665-671
    • Estabrook, R.W.1    Shet, M.S.2    Faulkner, K.3    Fisher, C.W.4
  • 18
    • 33847168352 scopus 로고
    • Biodegradation of polycyclic aromatic hydrocarbons
    • Cerniglia CE: Biodegradation of polycyclic aromatic hydrocarbons. Biodegradation 1992, 3:351-368.
    • (1992) Biodegradation , vol.3 , pp. 351-368
    • Cerniglia, C.E.1
  • 19
    • 0031008420 scopus 로고    scopus 로고
    • Polycyclic aromatic hydrocarbon bioremediation design
    • Harayama S: Polycyclic aromatic hydrocarbon bioremediation design. Curr Opin Biotechnol 1997, 8:268-273.
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 268-273
    • Harayama, S.1
  • 20
    • 0028100163 scopus 로고
    • Bacterial dehalogenases: Biochemistry, genetics, and biotechnological applications
    • Fetzner S, Lingens F: Bacterial dehalogenases: Biochemistry, genetics, and biotechnological applications. Microbiol Rev 1994, 58:641-685.
    • (1994) Microbiol Rev , vol.58 , pp. 641-685
    • Fetzner, S.1    Lingens, F.2
  • 21
    • 0030043560 scopus 로고    scopus 로고
    • Evidence for cytochrome P450-mediated benzo[a]pyrene hydroxylation in the white rot fungus Phanerochaete chrysosporium
    • Masaphy S, Levanon D, Henis Y, Venkateswarlu K, Kelly SL: Evidence for cytochrome P450-mediated benzo[a]pyrene hydroxylation in the white rot fungus Phanerochaete chrysosporium. FEMS Microbiol Lett 1996, 135:51-55.
    • (1996) FEMS Microbiol Lett , vol.135 , pp. 51-55
    • Masaphy, S.1    Levanon, D.2    Henis, Y.3    Venkateswarlu, K.4    Kelly, S.L.5
  • 25
    • 0029144146 scopus 로고
    • Recruitment of co-metabolic enzymes for environmental detoxification of organohalides
    • Wackett LP: Recruitment of co-metabolic enzymes for environmental detoxification of organohalides. Environ Health Perspect 1995, 103:45-48.
    • (1995) Environ Health Perspect , vol.103 , pp. 45-48
    • Wackett, L.P.1
  • 27
    • 0028909926 scopus 로고
    • Functional expression of fused enzymes between human cytochrome P4501A1 and human NADPH-cytochrome P450 oxidoreductase in Saccharomyces cerevisiae
    • Wittekindt NE, Würgler FE, Sengstag C: Functional expression of fused enzymes between human cytochrome P4501A1 and human NADPH-cytochrome P450 oxidoreductase in Saccharomyces cerevisiae. DNA Cell Biol 1995, 14:273-283.
    • (1995) DNA Cell Biol , vol.14 , pp. 273-283
    • Wittekindt, N.E.1    Würgler, F.E.2    Sengstag, C.3
  • 28
    • 0025949445 scopus 로고
    • Structural function of residue-209 in coumarin 7-hydroxylase (P450coh)
    • Juvonen RO, Iwasaki M, Negishi M: Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). J Biol Chem 1991, 266:16431-16435.
    • (1991) J Biol Chem , vol.266 , pp. 16431-16435
    • Juvonen, R.O.1    Iwasaki, M.2    Negishi, M.3
  • 29
    • 0028968913 scopus 로고
    • Altering the regiospecificity of androstenedione hydroxylase activity in P450s 2a-4/5 by a mutation of the residue at position 481
    • Iwasaki M, Darden TA, Pedersen LG, Negishi M: Altering the regiospecificity of androstenedione hydroxylase activity in P450s 2a-4/5 by a mutation of the residue at position 481. Biochemistry 1995, 34:5054-5059.
    • (1995) Biochemistry , vol.34 , pp. 5054-5059
    • Iwasaki, M.1    Darden, T.A.2    Pedersen, L.G.3    Negishi, M.4
  • 30
    • 0027447333 scopus 로고
    • A single amino acid substitution confers progesterone 6β-hydroxylase activity to rabbit cytochrome P450 2C3
    • Hsu M-H, Griffin KJ, Wang Y, Kemper B, Johnson EF: A single amino acid substitution confers progesterone 6β-hydroxylase activity to rabbit cytochrome P450 2C3. J Biol Chem 1993, 268:6939-6944.
    • (1993) J Biol Chem , vol.268 , pp. 6939-6944
    • Hsu, M.-H.1    Griffin, K.J.2    Wang, Y.3    Kemper, B.4    Johnson, E.F.5
  • 31
    • 0031021585 scopus 로고    scopus 로고
    • An active site substitution, F87V, converts cytochrome P450BM-3 into a regio- And stereoselective (14S,15R)-arachidonic acid epoxygenase
    • Graham-Lorence S, Truan G, Peterson JA, Falck JR, Wei S, Helvig C, Capdevila JH: An active site substitution, F87V, converts cytochrome P450BM-3 into a regio- and stereoselective (14S,15R)-arachidonic acid epoxygenase. J Biol Chem 1997, 272:1127-1135. An example of how a subtle change in the active site characteristics can give rise to totally altered stereoselectivity of substrate oxidation, leading to the synthesis of a useful intermediate.
    • (1997) J Biol Chem , vol.272 , pp. 1127-1135
    • Graham-Lorence, S.1    Truan, G.2    Peterson, J.A.3    Falck, J.R.4    Wei, S.5    Helvig, C.6    Capdevila, J.H.7
  • 34
    • 0024208742 scopus 로고
    • cam as revealed by site-directed mutagenesis
    • cam as revealed by site-directed mutagenesis. J Biol Chem 1988, 263:18842-18849.
    • (1988) J Biol Chem , vol.263 , pp. 18842-18849
    • Atkins, W.M.1    Sligar, S.G.2
  • 36
    • 0027375275 scopus 로고
    • Molecular recognition in cytochrome P450: Mechanism for the control of uncoupling reactions
    • Loida PJ, Sugar SG: Molecular recognition in cytochrome P450: Mechanism for the control of uncoupling reactions. Biochemistry 1993, 32:11530-11538.
    • (1993) Biochemistry , vol.32 , pp. 11530-11538
    • Loida, P.J.1    Sugar, S.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.