메뉴 건너뛰기




Volumn 68, Issue 1, 2009, Pages 18-21

Functional expression of N-terminally tagged membrane bound cytochrome P450

Author keywords

CYP79A1; Cytochrome P450; N terminal tagging; StrepII tag

Indexed keywords

ALA TRP ARG HIS PRO GLN PHE GLY GLY; ALA-TRP-ARG-HIS-PRO-GLN-PHE-GLY-GLY; CYTOCHROME P450; CYTOCHROME P450TYR; OLIGOPEPTIDE; RECOMBINANT PROTEIN; TYROSINE; VEGETABLE PROTEIN;

EID: 68349152778     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.06.005     Document Type: Article
Times cited : (4)

References (31)
  • 1
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems
    • Terpe K. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 60 (2003) 523-533
    • (2003) Appl. Microbiol. Biotechnol. , vol.60 , pp. 523-533
    • Terpe, K.1
  • 2
    • 0035979713 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins: determinants and dynamics
    • Goder V., and Spiess M. Topogenesis of membrane proteins: determinants and dynamics. FEBS Lett. 504 (2001) 87-93
    • (2001) FEBS Lett. , vol.504 , pp. 87-93
    • Goder, V.1    Spiess, M.2
  • 3
    • 28744449655 scopus 로고    scopus 로고
    • A new epitope of CYP2D6 recognized by liver kidney microsomal autoantibody from Japanese patients with autoimmune hepatitis
    • Imaoka S., Obata N., Hiroi T., Osada-Oka M., Hara R., Nishiguchi S., and Funae Y. A new epitope of CYP2D6 recognized by liver kidney microsomal autoantibody from Japanese patients with autoimmune hepatitis. Biol. Pharm. Bull. 28 (2005) 2240-2243
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 2240-2243
    • Imaoka, S.1    Obata, N.2    Hiroi, T.3    Osada-Oka, M.4    Hara, R.5    Nishiguchi, S.6    Funae, Y.7
  • 4
    • 0035450155 scopus 로고    scopus 로고
    • N-terminal deletions and His-tag fusions dramatically affect expression of cytochrome P4502C2 in bacteria
    • Doray B., Chen C.D., and Kemper B. N-terminal deletions and His-tag fusions dramatically affect expression of cytochrome P4502C2 in bacteria. Arch. Biochem. Biophys. 393 (2001) 143-153
    • (2001) Arch. Biochem. Biophys. , vol.393 , pp. 143-153
    • Doray, B.1    Chen, C.D.2    Kemper, B.3
  • 5
    • 4444369799 scopus 로고    scopus 로고
    • Immunodetection and quantification of cytochromes P450 using epitope tagging: immunological, spectroscopic, and kinetic analysis of cinnamate 4-hydroxylase
    • Humphreys J.M., and Chapple C. Immunodetection and quantification of cytochromes P450 using epitope tagging: immunological, spectroscopic, and kinetic analysis of cinnamate 4-hydroxylase. J. Immunol. Methods 292 (2004) 97-107
    • (2004) J. Immunol. Methods , vol.292 , pp. 97-107
    • Humphreys, J.M.1    Chapple, C.2
  • 7
    • 3042683304 scopus 로고    scopus 로고
    • Expression of human cytochrome P450 46A1 in Escherichia coli: effects of N- and C-terminal modifications
    • Mast N., Andersson U., Nakayama K., Bjorkhem I., and Pikuleva I.A. Expression of human cytochrome P450 46A1 in Escherichia coli: effects of N- and C-terminal modifications. Arch. Biochem. Biophys. 428 (2004) 99-108
    • (2004) Arch. Biochem. Biophys. , vol.428 , pp. 99-108
    • Mast, N.1    Andersson, U.2    Nakayama, K.3    Bjorkhem, I.4    Pikuleva, I.A.5
  • 8
    • 0029128324 scopus 로고
    • Truncated human P450 2D6 - expression in Escherichia coli, Ni2+-chelate affinity purification, and characterization of solubility and aggregation
    • Kempf A.C., Zanger U.M., and Meyer U.A. Truncated human P450 2D6 - expression in Escherichia coli, Ni2+-chelate affinity purification, and characterization of solubility and aggregation. Arch. Biochem. Biophys. 321 (1995) 277-288
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 277-288
    • Kempf, A.C.1    Zanger, U.M.2    Meyer, U.A.3
  • 9
    • 0642369727 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression in E. coli of cytochrome P45017 alpha comparison of structural and functional properties of substrate-specific cytochromes P450 from different species
    • Gilep A.A., Estabrook R.W., and Usanov S.A. Molecular cloning and heterologous expression in E. coli of cytochrome P45017 alpha comparison of structural and functional properties of substrate-specific cytochromes P450 from different species. Biochemistry-Moscow 68 (2003) 86-98
    • (2003) Biochemistry-Moscow , vol.68 , pp. 86-98
    • Gilep, A.A.1    Estabrook, R.W.2    Usanov, S.A.3
  • 10
    • 0032211208 scopus 로고    scopus 로고
    • Isolation of partially purified P450 2D18 and characterization of activity toward the tricyclic antidepressants imipramine and desipramine
    • Thompson C.M., Kawashima H., and Strobel H.W. Isolation of partially purified P450 2D18 and characterization of activity toward the tricyclic antidepressants imipramine and desipramine. Arch. Biochem. Biophys. 359 (1998) 115-121
    • (1998) Arch. Biochem. Biophys. , vol.359 , pp. 115-121
    • Thompson, C.M.1    Kawashima, H.2    Strobel, H.W.3
  • 11
    • 0012697772 scopus 로고    scopus 로고
    • Human CYP1A1 allelic variants: baculovirus expression and purification, hydrodynamic, spectral, and catalytical properties and their potency in the formation of all-trans-retinoic acid
    • Chernogolov A., Behlke J., Schunck W.H., Roots I., and Schwar D. Human CYP1A1 allelic variants: baculovirus expression and purification, hydrodynamic, spectral, and catalytical properties and their potency in the formation of all-trans-retinoic acid. Protein Expr. Purif. 28 (2003) 259-269
    • (2003) Protein Expr. Purif. , vol.28 , pp. 259-269
    • Chernogolov, A.1    Behlke, J.2    Schunck, W.H.3    Roots, I.4    Schwar, D.5
  • 12
    • 12044256272 scopus 로고
    • Involvement of cytochrome-P-450 in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench
    • Halkier B.A., and Møller B.L. Involvement of cytochrome-P-450 in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench. Plant Physiol. 96 (1991) 10-17
    • (1991) Plant Physiol. , vol.96 , pp. 10-17
    • Halkier, B.A.1    Møller, B.L.2
  • 13
    • 0028985451 scopus 로고
    • Cytochrome P-450(Tyr) is a multifunctional heme-thiolate enzyme catalyzing the conversion of l-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
    • Sibbesen O., Koch B., Halkier B.A., and Møller B.L. Cytochrome P-450(Tyr) is a multifunctional heme-thiolate enzyme catalyzing the conversion of l-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. J. Biol. Chem. 270 (1995) 3506-3511
    • (1995) J. Biol. Chem. , vol.270 , pp. 3506-3511
    • Sibbesen, O.1    Koch, B.2    Halkier, B.A.3    Møller, B.L.4
  • 14
    • 0031397803 scopus 로고    scopus 로고
    • Isolation and reconstitution of cytochrome P450ox and in vitro reconstitution of the entire biosynthetic pathway of the cyanogenic glucoside dhurrin from Sorghum
    • Kahn R.A., Bak S., Svendsen I., Halkier B.A., and Møller B.L. Isolation and reconstitution of cytochrome P450ox and in vitro reconstitution of the entire biosynthetic pathway of the cyanogenic glucoside dhurrin from Sorghum. Plant Physiol. 115 (1997) 1661-1670
    • (1997) Plant Physiol. , vol.115 , pp. 1661-1670
    • Kahn, R.A.1    Bak, S.2    Svendsen, I.3    Halkier, B.A.4    Møller, B.L.5
  • 15
    • 0032005917 scopus 로고    scopus 로고
    • Cloning of three A-type cytochromes p450, CYP71E1, CYP98, and CYP99 from Sorghum bicolor (L.) Moench by a PCR approach and identification by expression in Escherichia coli of CYP71E1 as a multifunctional cytochrome p450 in the biosynthesis of the cyanogenic glucoside dhurrin
    • Bak S., Kahn R.A., Nielsen H.L., Møller B.L., and Halkier B.A. Cloning of three A-type cytochromes p450, CYP71E1, CYP98, and CYP99 from Sorghum bicolor (L.) Moench by a PCR approach and identification by expression in Escherichia coli of CYP71E1 as a multifunctional cytochrome p450 in the biosynthesis of the cyanogenic glucoside dhurrin. Plant Mol. Biol. 36 (1998) 393-405
    • (1998) Plant Mol. Biol. , vol.36 , pp. 393-405
    • Bak, S.1    Kahn, R.A.2    Nielsen, H.L.3    Møller, B.L.4    Halkier, B.A.5
  • 16
    • 0033544872 scopus 로고    scopus 로고
    • The UDP-glucose: p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor - isolation, cloning, heterologous expression, and substrate specificity
    • Jones P.R., Møller B.L., and Høj P.B. The UDP-glucose: p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor - isolation, cloning, heterologous expression, and substrate specificity. J. Biol. Chem. 274 (1999) 35483-35491
    • (1999) J. Biol. Chem. , vol.274 , pp. 35483-35491
    • Jones, P.R.1    Møller, B.L.2    Høj, P.B.3
  • 17
    • 0033102583 scopus 로고    scopus 로고
    • Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
    • Kahn R.A., Fahrendorf T., Halkier B.A., and Møller B.L. Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. Arch. Biochem. Biophys. 363 (1999) 9-18
    • (1999) Arch. Biochem. Biophys. , vol.363 , pp. 9-18
    • Kahn, R.A.1    Fahrendorf, T.2    Halkier, B.A.3    Møller, B.L.4
  • 18
    • 0040106748 scopus 로고
    • The biosynthesis of cyanogenic glucosides in higher-plants - channeling of intermediates in dhurrin biosynthesis by a microsomal system from Sorghum bicolor (Linn) Moench
    • Møller B.L., and Conn E.E. The biosynthesis of cyanogenic glucosides in higher-plants - channeling of intermediates in dhurrin biosynthesis by a microsomal system from Sorghum bicolor (Linn) Moench. J. Biol. Chem. 255 (1980) 3049-3056
    • (1980) J. Biol. Chem. , vol.255 , pp. 3049-3056
    • Møller, B.L.1    Conn, E.E.2
  • 20
    • 13444249488 scopus 로고    scopus 로고
    • Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome
    • Kristensen C., Morant M., Olsen C.E., Ekstrom C.T., Galbraith D.W., Møller B.L., and Bak S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779-1784
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1779-1784
    • Kristensen, C.1    Morant, M.2    Olsen, C.E.3    Ekstrom, C.T.4    Galbraith, D.W.5    Møller, B.L.6    Bak, S.7
  • 22
    • 0026562884 scopus 로고
    • Improved method for high-efficiency transformation of intact yeast-cells
    • Gietz D., Stjean A., Woods R.A., and Schiestl R.H. Improved method for high-efficiency transformation of intact yeast-cells. Nucleic Acids Res. 20 (1992) 1425
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    Stjean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 23
    • 34848836038 scopus 로고    scopus 로고
    • Improved cloning and expression of cytochrome P450s and cytochrome P450 reductase in yeast
    • Hamann T., and Møller B.L. Improved cloning and expression of cytochrome P450s and cytochrome P450 reductase in yeast. Protein Expr. Purif. 56 (2007) 121-127
    • (2007) Protein Expr. Purif. , vol.56 , pp. 121-127
    • Hamann, T.1    Møller, B.L.2
  • 24
    • 33750975084 scopus 로고    scopus 로고
    • Advancing uracil-excision based cloning towards an ideal technique for cloning PCR fragments
    • 10.1093/nar/gkl635
    • Nour-Eldin H.H., Hansen B.G., Nørholm M.H.H., Jensen J.K., and Halkier B.A. Advancing uracil-excision based cloning towards an ideal technique for cloning PCR fragments. Nucleic Acids Res. 34 (2006) e122 10.1093/nar/gkl635
    • (2006) Nucleic Acids Res. , vol.34
    • Nour-Eldin, H.H.1    Hansen, B.G.2    Nørholm, M.H.H.3    Jensen, J.K.4    Halkier, B.A.5
  • 25
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • Hartmann E., Rapoport T.A., and Lodish H.F. Predicting the orientation of eukaryotic membrane-spanning proteins. Proc. Natl. Acad. Sci. USA 86 (1989) 5786-5790
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 26
    • 0023955730 scopus 로고
    • Positive charges at the Nh2 terminus convert the membrane-anchor signal peptide of cytochrome-P-450 to a secretory signal peptide
    • Szczesna-Skorupa E., Browne N., Mead D., and Kemper B. Positive charges at the Nh2 terminus convert the membrane-anchor signal peptide of cytochrome-P-450 to a secretory signal peptide. Proc. Natl. Acad. Sci. USA 85 (1988) 738-742
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 738-742
    • Szczesna-Skorupa, E.1    Browne, N.2    Mead, D.3    Kemper, B.4
  • 27
    • 0024478250 scopus 로고
    • Nh2-terminal substitutions of basic amino-acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome-P450Iic2
    • Szczesna-Skorupa E., and Kemper B. Nh2-terminal substitutions of basic amino-acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome-P450Iic2. J. Cell Biol. 108 (1989) 1237-1243
    • (1989) J. Cell Biol. , vol.108 , pp. 1237-1243
    • Szczesna-Skorupa, E.1    Kemper, B.2
  • 28
    • 33645673185 scopus 로고    scopus 로고
    • Identification of membrane-contacting loops of the catalytic domain of cytochrome P4502C2 by tryptophan fluorescence scanning
    • Ozalp C., Szczesna-Skorupa E., and Kemper B. Identification of membrane-contacting loops of the catalytic domain of cytochrome P4502C2 by tryptophan fluorescence scanning. Biochemistry 45 (2006) 4629-4637
    • (2006) Biochemistry , vol.45 , pp. 4629-4637
    • Ozalp, C.1    Szczesna-Skorupa, E.2    Kemper, B.3
  • 29
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity
    • Williams P.A., Cosme J., Sridhar V., Johnson E.F., and Mcree D.E. Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol. Cell 5 (2000) 121-131
    • (2000) Mol. Cell , vol.5 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    Mcree, D.E.5
  • 30
    • 62349122684 scopus 로고    scopus 로고
    • Substrate specificity of plant UDP-dependent glycosyltransferases predicted from crystal structures and homology modeling
    • Osmani S.A., Bak S., and Møller B.L. Substrate specificity of plant UDP-dependent glycosyltransferases predicted from crystal structures and homology modeling. Phytochemistry 70 (2009) 325-347
    • (2009) Phytochemistry , vol.70 , pp. 325-347
    • Osmani, S.A.1    Bak, S.2    Møller, B.L.3
  • 31
    • 31144445569 scopus 로고    scopus 로고
    • Determination of catalytic key amino acids and UDP sugar donor specificity of the cyanohydrin glycosyltransferase UGT85B1 from Sorghum bicolor. Molecular modeling substantiated by site-specific mutagenesis and biochemical analyses
    • Thorsøe K.S., Bak S., Olsen C.E., Imberty A., Breton C., and Møller B.L. Determination of catalytic key amino acids and UDP sugar donor specificity of the cyanohydrin glycosyltransferase UGT85B1 from Sorghum bicolor. Molecular modeling substantiated by site-specific mutagenesis and biochemical analyses. Plant Physiol. 139 (2005) 664-673
    • (2005) Plant Physiol. , vol.139 , pp. 664-673
    • Thorsøe, K.S.1    Bak, S.2    Olsen, C.E.3    Imberty, A.4    Breton, C.5    Møller, B.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.