메뉴 건너뛰기




Volumn 438, Issue 2, 2013, Pages 289-294

High-level heterologous expression of fungal cytochrome P450s in Escherichia coli

Author keywords

Escherichia coli; Eukaryotic cytochrome P450; Heterologous expression; High level expression; Large scale screening; Wood rotting basidiomycetes

Indexed keywords

CYTOCHROME P450; FUNGAL PROTEIN;

EID: 84882720783     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.07.057     Document Type: Article
Times cited : (27)

References (33)
  • 2
    • 73249132581 scopus 로고    scopus 로고
    • The cytochrome p450 homepage
    • Nelson D.R. The cytochrome p450 homepage. Hum. Genomics. 2009, 4:59-65.
    • (2009) Hum. Genomics. , vol.4 , pp. 59-65
    • Nelson, D.R.1
  • 4
    • 84880141746 scopus 로고    scopus 로고
    • Microbial cytochromes P450: biodiversity and biotechnology. Where do cytochromes P450 come from, what do they do and what can they do for us?
    • Kelly S.L., Kelly D.E. Microbial cytochromes P450: biodiversity and biotechnology. Where do cytochromes P450 come from, what do they do and what can they do for us?. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2013, 368:20120476.
    • (2013) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.368 , pp. 20120476
    • Kelly, S.L.1    Kelly, D.E.2
  • 6
    • 84861905310 scopus 로고    scopus 로고
    • Molecular identification and functional characterization of cytochrome P450 monooxygenases from the brown-rot basidiomycete Postia placenta
    • Ide M., Ichinose H., Wariishi H. Molecular identification and functional characterization of cytochrome P450 monooxygenases from the brown-rot basidiomycete Postia placenta. Arch. Microbiol. 2012, 194:243-253.
    • (2012) Arch. Microbiol. , vol.194 , pp. 243-253
    • Ide, M.1    Ichinose, H.2    Wariishi, H.3
  • 7
    • 77952097008 scopus 로고    scopus 로고
    • Molecular characterization and isolation of cytochrome P450 genes from the filamentous fungus Aspergillus oryzae
    • Nazir K.H.M.N.H., Ichinose H., Wariishi H. Molecular characterization and isolation of cytochrome P450 genes from the filamentous fungus Aspergillus oryzae. Arch. Microbiol. 2010, 192:395-408.
    • (2010) Arch. Microbiol. , vol.192 , pp. 395-408
    • Nazir, K.H.M.N.H.1    Ichinose, H.2    Wariishi, H.3
  • 8
    • 79955593960 scopus 로고    scopus 로고
    • Construction and application of a functional library of cytochrome P450 monooxygenases from the filamentous fungus Aspergillus oryzae
    • Nazir K.H.M.N.H., Ichinose H., Wariishi H. Construction and application of a functional library of cytochrome P450 monooxygenases from the filamentous fungus Aspergillus oryzae. Appl. Environ. Microbiol. 2011, 77:3147-3150.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 3147-3150
    • Nazir, K.H.M.N.H.1    Ichinose, H.2    Wariishi, H.3
  • 9
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli
    • Barnes H.J., Arlotto M.P., Waterman M.R. Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli. Proc. Natl. Acad. Sci. USA 1991, 88:5597-5601.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 10
    • 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., Backes W.L. High-level expression of recombinant rabbit cytochrome P450 2E1 in Escherichia coli C41 and its purification. Protein Expr. Purif. 2004, 33:66-71.
    • (2004) Protein Expr. Purif. , vol.33 , pp. 66-71
    • Cheng, D.1    Kelley, R.W.2    Cawley, G.F.3    Backes, W.L.4
  • 11
    • 33646494635 scopus 로고    scopus 로고
    • Functional expression of human cytochrome P450 enzymes in Escherichia coli
    • Yun C.H., Yim S.K., Kim D.H., Ahn T. Functional expression of human cytochrome P450 enzymes in Escherichia coli. Curr. Drug. Metab. 2006, 7:411-429.
    • (2006) Curr. Drug. Metab. , vol.7 , pp. 411-429
    • Yun, C.H.1    Yim, S.K.2    Kim, D.H.3    Ahn, T.4
  • 12
    • 84856096694 scopus 로고    scopus 로고
    • Heterologous expression and mechanistic investigation of a fungal cytochrome P450 (CYP5150A2): involvement of alternative redox partners
    • Ichinose H., Wariishi H. Heterologous expression and mechanistic investigation of a fungal cytochrome P450 (CYP5150A2): involvement of alternative redox partners. Arch. Biochem. Biophys. 2012, 518:8-15.
    • (2012) Arch. Biochem. Biophys. , vol.518 , pp. 8-15
    • Ichinose, H.1    Wariishi, H.2
  • 13
    • 57149146568 scopus 로고    scopus 로고
    • Expression and characterization of CYP51, the ancient sterol 14-demethylase activity for cytochromes P450 (CYP), in the white-rot fungus Phanerochaete chrysosporium
    • Warrilow A., Ugochukwu C., Lamb D., Kelly D., Kelly S. Expression and characterization of CYP51, the ancient sterol 14-demethylase activity for cytochromes P450 (CYP), in the white-rot fungus Phanerochaete chrysosporium. Lipids 2008, 43:1143-1153.
    • (2008) Lipids , vol.43 , pp. 1143-1153
    • Warrilow, A.1    Ugochukwu, C.2    Lamb, D.3    Kelly, D.4    Kelly, S.5
  • 14
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: classification and secondary structure prediction system for membrane proteins
    • Hirokawa T., Boon-Chieng S., Mitaku S. SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics 1998, 14:378-379.
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 15
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes, II. Solubilization, purification, and properties
    • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes, II. Solubilization, purification, and properties. J. Biol. Chem. 1964, 239:2379-2385.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 16
    • 0034043337 scopus 로고    scopus 로고
    • High-level expression in Escherichia coli and purification of the membrane-bound form of cytochrome b(5)
    • Mulrooney S.B., Waskell L. High-level expression in Escherichia coli and purification of the membrane-bound form of cytochrome b(5). Protein Expr. Purif. 2000, 19:173-178.
    • (2000) Protein Expr. Purif. , vol.19 , pp. 173-178
    • Mulrooney, S.B.1    Waskell, L.2
  • 17
    • 0027497950 scopus 로고
    • Expression of truncated forms of liver microsomal P450 cytochromes 2B4 and 2E1 in Escherichia coli: influence of NH2-terminal region on localization in cytosol and membranes
    • Pernecky S.J., Larson J.R., Philpot R.M., Coon M.J. Expression of truncated forms of liver microsomal P450 cytochromes 2B4 and 2E1 in Escherichia coli: influence of NH2-terminal region on localization in cytosol and membranes. Proc. Natl. Acad. Sci. USA 1993, 90:2651-2655.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2651-2655
    • Pernecky, S.J.1    Larson, J.R.2    Philpot, R.M.3    Coon, M.J.4
  • 18
    • 70349577507 scopus 로고    scopus 로고
    • Membrane integration of recombinant human P450 forms
    • Shukla A., Huang W., Depaz I.M., Gillam E.M. Membrane integration of recombinant human P450 forms. Xenobiotica 2009, 39:495-507.
    • (2009) Xenobiotica , vol.39 , pp. 495-507
    • Shukla, A.1    Huang, W.2    Depaz, I.M.3    Gillam, E.M.4
  • 19
    • 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., Yun C.H. High-level expression of human cytochrome P450 1A2 by co-expression with human molecular chaperone HDJ-1(Hsp40). Protein Expr. Purif. 2004, 36:48-52.
    • (2004) Protein Expr. Purif. , vol.36 , pp. 48-52
    • Ahn, T.1    Yang, S.2    Yun, C.H.3
  • 20
    • 0031106366 scopus 로고    scopus 로고
    • Microsomal P450 2C3 is expressed as a soluble dimer in Escherichia coli following modification of its N-terminus
    • von Wachenfeldt C., Richardson T.H., Cosme J., Johnson E.F. Microsomal P450 2C3 is expressed as a soluble dimer in Escherichia coli following modification of its N-terminus. Arch. Biochem. Biophys. 1997, 339:107-114.
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 107-114
    • von Wachenfeldt, C.1    Richardson, T.H.2    Cosme, J.3    Johnson, E.F.4
  • 21
    • 0032522904 scopus 로고    scopus 로고
    • High catalytic activity of human cytochrome P450 co-expressed with human NADPH-cytochrome P450 reductase in Escherichia coli
    • Iwata H., Fujita K., Kushida H., Suzuki A., Konno Y., Nakamura K., Fujino A., Kamataki T. High catalytic activity of human cytochrome P450 co-expressed with human NADPH-cytochrome P450 reductase in Escherichia coli. Biochem. Pharmacol. 1998, 55:1315-1325.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1315-1325
    • Iwata, H.1    Fujita, K.2    Kushida, H.3    Suzuki, A.4    Konno, Y.5    Nakamura, K.6    Fujino, A.7    Kamataki, T.8
  • 22
    • 0030954347 scopus 로고    scopus 로고
    • Cytochrome P450 2C11: Escherichia coli expression, purification, functional characterization, and mechanism-based inactivation of the enzyme
    • Licad-Coles E., He K., Yin H., Correia M.A. Cytochrome P450 2C11: Escherichia coli expression, purification, functional characterization, and mechanism-based inactivation of the enzyme. Arch. Biochem. Biophys. 1997, 338:35-42.
    • (1997) Arch. Biochem. Biophys. , vol.338 , pp. 35-42
    • Licad-Coles, E.1    He, K.2    Yin, H.3    Correia, M.A.4
  • 23
    • 0034671918 scopus 로고    scopus 로고
    • Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3
    • Kitazume T., Takaya N., Nakayama N., Shoun H. Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3. J. Biol. Chem. 2000, 275:39734-39740.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39734-39740
    • Kitazume, T.1    Takaya, N.2    Nakayama, N.3    Shoun, H.4
  • 24
    • 0029892430 scopus 로고    scopus 로고
    • Cytochrome P450foxy, a catalytically self-sufficient fatty acid hydroxylase of the Fusarium oxysporum
    • Nakayama N., Takemae A., Shoun H. Cytochrome P450foxy, a catalytically self-sufficient fatty acid hydroxylase of the Fusarium oxysporum. J. Biochem. 1996, 119:435-440.
    • (1996) J. Biochem. , vol.119 , pp. 435-440
    • Nakayama, N.1    Takemae, A.2    Shoun, H.3
  • 25
    • 0036236942 scopus 로고    scopus 로고
    • Kinetic analysis of hydroxylation of saturated fatty acids by recombinant P450foxy produced by an Escherichia coli expression system
    • Kitazume T., Tanaka A., Takaya N., Nakamura A., Matsuyama S., Suzuki T., Shoun H. Kinetic analysis of hydroxylation of saturated fatty acids by recombinant P450foxy produced by an Escherichia coli expression system. Eur. J. Biochem. 2002, 269:2075-2082.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2075-2082
    • Kitazume, T.1    Tanaka, A.2    Takaya, N.3    Nakamura, A.4    Matsuyama, S.5    Suzuki, T.6    Shoun, H.7
  • 26
    • 0028071497 scopus 로고
    • Expression of modified human cytochrome P450 1A1 in Escherichia coli: effects of 5' substitution, stabilization, purification, spectral characterization, and catalytic properties
    • Guo Z., Gillam E.M., Ohmori S., Tukey R.H., Guengerich F.P. Expression of modified human cytochrome P450 1A1 in Escherichia coli: effects of 5' substitution, stabilization, purification, spectral characterization, and catalytic properties. Arch. Biochem. Biophys. 1994, 312:436-446.
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 436-446
    • Guo, Z.1    Gillam, E.M.2    Ohmori, S.3    Tukey, R.H.4    Guengerich, F.P.5
  • 27
    • 0035110289 scopus 로고    scopus 로고
    • Microsomal p450s use specific proline-rich sequences for efficient folding, but not for maintenance of the folded structure
    • Kusano K., Sakaguchi M., Kagawa N., Waterman M.R., Omura T. Microsomal p450s use specific proline-rich sequences for efficient folding, but not for maintenance of the folded structure. J. Biochem. 2001, 129:259-269.
    • (2001) J. Biochem. , vol.129 , pp. 259-269
    • Kusano, K.1    Sakaguchi, M.2    Kagawa, N.3    Waterman, M.R.4    Omura, T.5
  • 28
    • 0035113534 scopus 로고    scopus 로고
    • Importance of a proline-rich sequence in the amino-terminal region for correct folding of mitochondrial and soluble microbial p450s
    • Kusano K., Kagawa N., Sakaguchi M., Omura T., Waterman M.R. Importance of a proline-rich sequence in the amino-terminal region for correct folding of mitochondrial and soluble microbial p450s. J. Biochem. 2001, 129:271-277.
    • (2001) J. Biochem. , vol.129 , pp. 271-277
    • Kusano, K.1    Kagawa, N.2    Sakaguchi, M.3    Omura, T.4    Waterman, M.R.5
  • 29
    • 4444378844 scopus 로고    scopus 로고
    • Structural basis for the role in protein folding of conserved proline-rich regions in cytochromes P450
    • Kemper B. Structural basis for the role in protein folding of conserved proline-rich regions in cytochromes P450. Toxicol. Appl. Pharmacol. 2004, 199:305-315.
    • (2004) Toxicol. Appl. Pharmacol. , vol.199 , pp. 305-315
    • Kemper, B.1
  • 30
    • 0027217892 scopus 로고
    • Deletion of a conserved tetrapeptide, PPGP, in P450 2C2 results in loss of enzymatic activity without a change in its cellular location
    • Szczesna-Skorupa E., Straub P., Kemper B. Deletion of a conserved tetrapeptide, PPGP, in P450 2C2 results in loss of enzymatic activity without a change in its cellular location. Arch. Biochem. Biophys. 1993, 304:170-175.
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 170-175
    • Szczesna-Skorupa, E.1    Straub, P.2    Kemper, B.3
  • 31
    • 0029960709 scopus 로고    scopus 로고
    • Different structural requirements at specific proline residue positions in the conserved proline-rich region of cytochrome P450 2C2
    • Chen C.D., Kemper B. Different structural requirements at specific proline residue positions in the conserved proline-rich region of cytochrome P450 2C2. J. Biol. Chem. 1996, 271:28607-28611.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28607-28611
    • Chen, C.D.1    Kemper, B.2
  • 32
    • 0031847967 scopus 로고    scopus 로고
    • A conserved proline-rich sequence between the N-terminal signal-anchor and catalytic domains is required for assembly of functional cytochrome P450 2C2
    • Chen C.D., Doray B., Kemper B. A conserved proline-rich sequence between the N-terminal signal-anchor and catalytic domains is required for assembly of functional cytochrome P450 2C2. Arch. Biochem. Biophys. 1998, 350:233-238.
    • (1998) Arch. Biochem. Biophys. , vol.350 , pp. 233-238
    • Chen, C.D.1    Doray, B.2    Kemper, B.3
  • 33
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme
    • Gillam E.M., Baba T., Kim B.R., Ohmori S., Guengerich F.P. Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch. Biochem. Biophys. 1993, 305:123-131.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 123-131
    • Gillam, E.M.1    Baba, T.2    Kim, B.R.3    Ohmori, S.4    Guengerich, F.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.