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Volumn 11, Issue 2, 1997, Pages 191-201

Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) moench, a cytochrome p450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; HYBRID PROTEIN; LANOSTEROL 14 ALPHA-DEMETHYLASE; OXIDOREDUCTASE; STEROL 14ALPHA DEMETHYLASE;

EID: 0031079568     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1997.11020191.x     Document Type: Article
Times cited : (83)

References (33)
  • 1
    • 0026072189 scopus 로고
    • Different substrate specificities of lanosterol 14-alpha-demethylase (P450-14DM) of Saccharomyces cerevisiae and rat liver for 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol
    • Aoyama, Y. and Yoshida, Y. (1991) Different substrate specificities of lanosterol 14-alpha-demethylase (P450-14DM) of Saccharomyces cerevisiae and rat liver for 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol. Biochem. Biophys. Res. Commun. 178, 1064-1071.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 1064-1071
    • Aoyama, Y.1    Yoshida, Y.2
  • 2
    • 0026735841 scopus 로고
    • 14DM) of yeast: Differences between the substrate recognition by yeast and plant sterol 14α-demethylases
    • 14DM) of yeast: differences between the substrate recognition by yeast and plant sterol 14α-demethylases. Biochem. Biophys. Res. Commun. 183, 1266-1272.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 1266-1272
    • Aoyama, Y.1    Yoshida, Y.2
  • 5
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17α-hydroxylase in Escherichia coli
    • Barnes, H.J., Arlotto, M.P. and Waterman, M.R. (1991) Expression and enzymatic activity of recombinant cytochrome P450 17α-hydroxylase in Escherichia coli. Proc. Natl Acad. Sci. USA, 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
  • 7
    • 0028302301 scopus 로고
    • Rapid detection and identification of Candida albicans and Torulopsis (Candida) glabrata in clinical specimens by species-specific nested PCR amplification of a cytochrome P-450 lanosterol-alpha-demethylase (L1A1) gene fragment
    • Burgener-Kairuz, P., Zuber, J.P., Buchman, T.G. and Rossier, M. (1994) Rapid detection and identification of Candida albicans and Torulopsis (Candida) glabrata in clinical specimens by species-specific nested PCR amplification of a cytochrome P-450 lanosterol-alpha-demethylase (L1A1) gene fragment. J. Clin. Microbiol. 32, 1902-1907.
    • (1994) J. Clin. Microbiol. , vol.32 , pp. 1902-1907
    • Burgener-Kairuz, P.1    Zuber, J.P.2    Buchman, T.G.3    Rossier, M.4
  • 8
    • 0028837082 scopus 로고
    • Biochemistry and molecular biology of the isoprenoid biosynthetic pathway in plants
    • Chappell, J. (1995) Biochemistry and molecular biology of the isoprenoid biosynthetic pathway in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 46, 521-547.
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 521-547
    • Chappell, J.1
  • 9
    • 0024114790 scopus 로고
    • Primary structure of the cytochrome P450 lanosterol 14α-demethylase gene from Candida tropicalis
    • Chen, C., Kalb, V.F., Turi, T.G. and Loper, J.C. (1988) Primary structure of the cytochrome P450 lanosterol 14α-demethylase gene from Candida tropicalis. DNA, 7, 617-626.
    • (1988) DNA , vol.7 , pp. 617-626
    • Chen, C.1    Kalb, V.F.2    Turi, T.G.3    Loper, J.C.4
  • 10
    • 0029621245 scopus 로고
    • Diversity and evolution of plant P450 and P450-reductases
    • Durst, F. and Nelson D.R. (1995) Diversity and evolution of plant P450 and P450-reductases. Drug Metabol. Drug Interact. 12, 189-206.
    • (1995) Drug Metabol. Drug Interact. , vol.12 , pp. 189-206
    • Durst, F.1    Nelson, D.R.2
  • 11
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • Gotoh, O. (1992) Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem. 267, 83-90.
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 12
    • 0029294552 scopus 로고
    • Functional expression of Saccharomyces cerevisiae CYP51A1 encoding lanosterol-14-demethylase in tobacco results in bypass of endogenous sterol biosynthetic pathway and resistance to an obtusifoliol-14-demethylase herbicide inhibitor
    • Grausem, B., Chaubet, N., Gigot, C., Loper, J.C. and Benveniste, P. (1995) Functional expression of Saccharomyces cerevisiae CYP51A1 encoding lanosterol-14-demethylase in tobacco results in bypass of endogenous sterol biosynthetic pathway and resistance to an obtusifoliol-14-demethylase herbicide inhibitor. Plant J. 7, 761-770.
    • (1995) Plant J. , vol.7 , pp. 761-770
    • Grausem, B.1    Chaubet, N.2    Gigot, C.3    Loper, J.C.4    Benveniste, P.5
  • 14
    • 0029643786 scopus 로고
    • Structure and function of cytochrome P450: A comparative analysis of three crystal structures
    • Hasemann, C.A., Kurumbail, R.G., Boddupallili, S.S., Peterson, J.A. and Deisenhofer, J. (1995) Structure and function of cytochrome P450: a comparative analysis of three crystal structures. Structure, 3, 41-62.
    • (1995) Structure , vol.3 , pp. 41-62
    • Hasemann, C.A.1    Kurumbail, R.G.2    Boddupallili, S.S.3    Peterson, J.A.4    Deisenhofer, J.5
  • 15
    • 0014101794 scopus 로고
    • Conversion of P-450 to P-420 by neutral salts and some other reagents
    • Imai, Y. and Sato, R. (1967) Conversion of P-450 to P-420 by neutral salts and some other reagents. Eur. J. Biochem. 1, 419-426.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 419-426
    • Imai, Y.1    Sato, R.2
  • 16
    • 0017794351 scopus 로고
    • Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy
    • Jefcoate, C.R. (1978) Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy. Methods Enzymol. 27, 258-279.
    • (1978) Methods Enzymol. , vol.27 , pp. 258-279
    • Jefcoate, C.R.1
  • 17
    • 12644251864 scopus 로고    scopus 로고
    • Isolation and characterization of the heme-thilate protein obtusifoliol 14α-demethylase from Sorghum bicolor (L.). Moench
    • Kahn, R.A., Bak, S., Olsen, C.E., Svendsen, I. and Møller, B.L. (1996) Isolation and characterization of the heme-thilate protein obtusifoliol 14α-demethylase from Sorghum bicolor (L.). Moench. J. Biol. Chem. 271, 32944-32950.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32944-32950
    • Kahn, R.A.1    Bak, S.2    Olsen, C.E.3    Svendsen, I.4    Møller, B.L.5
  • 18
    • 0022981279 scopus 로고
    • Isolation of a cytochrome P-450 structural gene from Saccharomyces cerevisiae
    • Kalb, V.F., Loper, J.C., Dey, C.R., Woods, C.W. and Sutter, T.R. (1986) Isolation of a cytochrome P-450 structural gene from Saccharomyces cerevisiae. Gene, 45, 237-245.
    • (1986) Gene , vol.45 , pp. 237-245
    • Kalb, V.F.1    Loper, J.C.2    Dey, C.R.3    Woods, C.W.4    Sutter, T.R.5
  • 19
    • 0024595561 scopus 로고
    • Nucleotide sequence of cytochrome P450 L1A1 (lanosterol 14α- Demethylase) from Candida albicans
    • Lai, M.H. and Kirsch, D.R. (1989) Nucleotide sequence of cytochrome P450 L1A1 (lanosterol 14α- demethylase) from Candida albicans. Nucl Res. 17, 804.
    • (1989) Nucl Res. , vol.17 , pp. 804
    • Lai, M.H.1    Kirsch, D.R.2
  • 20
    • 9044254525 scopus 로고    scopus 로고
    • P450 superfamily: Update on new sequences, gene mapping, accession numbers and nomenclature
    • Nelson, D.R., Koymans, L., Kamataki, T. et al. (1996) P450 superfamily: update on new sequences, gene mapping, accession numbers and nomenclature. Pharmacogenetics, 6, 1-42.
    • (1996) Pharmacogenetics , vol.6 , pp. 1-42
    • Nelson, D.R.1    Koymans, L.2    Kamataki, T.3
  • 21
    • 0016210017 scopus 로고
    • Role of sterols in membranes
    • Nes, W.R. (1973) Role of sterols in membranes. Lipids, 9, 596-612.
    • (1973) Lipids , vol.9 , pp. 596-612
    • Nes, W.R.1
  • 22
    • 85051483390 scopus 로고
    • Regulation of phytosterol biosynthesis
    • Moore, T.S., ed.. Boca Raton, FL: CRC Press
    • Nes, W.D., Parker, S.R., Crumley, F.G. and Ross, S.A. (1993) Regulation of phytosterol biosynthesis. In Lipid Metabolism in Plants (Moore, T.S., ed.). Boca Raton, FL: CRC Press, pp. 389-426.
    • (1993) Lipid Metabolism in Plants , pp. 389-426
    • Nes, W.D.1    Parker, S.R.2    Crumley, F.G.3    Ross, S.A.4
  • 23
    • 0024244368 scopus 로고
    • The T7 phage gene 10 leader RNA, a ribosome-binding site that dramatically enhances the expression of foreign genes in Escherichia coli
    • Olins, P.O., Devine, C.S., Rangwals, S.H. and Kavka, K.S. (1988) The T7 phage gene 10 leader RNA, a ribosome-binding site that dramatically enhances the expression of foreign genes in Escherichia coli. Gene, 73, 227-235.
    • (1988) Gene , vol.73 , pp. 227-235
    • Olins, P.O.1    Devine, C.S.2    Rangwals, S.H.3    Kavka, K.S.4
  • 24
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes
    • Omura, T. and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. J. Biol. Chem. 239, 2370-2378.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 26
    • 0023010745 scopus 로고
    • The 14α-demethylation of obtusifoliol by a cytochrome P-450 monooxygenase from higher plant microsomes
    • Rahier, A. and Taton, M. (1986) The 14α-demethylation of obtusifoliol by a cytochrome P-450 monooxygenase from higher plant microsomes. Biochem. Biophys. Res. Commun. 140, 1064-1072.
    • (1986) Biochem. Biophys. Res. Commun. , vol.140 , pp. 1064-1072
    • Rahier, A.1    Taton, M.2
  • 27
    • 0021259115 scopus 로고
    • Distribution of hopanoid triterpenes in prokaryotes
    • Rohmer, M., Bouvier-Nave, P. and Ourisson, G. (1984) Distribution of hopanoid triterpenes in prokaryotes. J. Gen. Microbiol. 130, 1137-1150.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 1137-1150
    • Rohmer, M.1    Bouvier-Nave, P.2    Ourisson, G.3
  • 29
    • 0029094658 scopus 로고
    • Cloning and functional expression of the cDNA encoding rat lanosterol 14α-demethylase
    • Sloane, D.L., So, O.Y., Leung, R., Scarafia, L.E., Saldou, N., Jarnagin, K. and Swinney, D.C. (1995) Cloning and functional expression of the cDNA encoding rat lanosterol 14α-demethylase. Gene, 161, 243-248.
    • (1995) Gene , vol.161 , pp. 243-248
    • Sloane, D.L.1    So, O.Y.2    Leung, R.3    Scarafia, L.E.4    Saldou, N.5    Jarnagin, K.6    Swinney, D.C.7
  • 30
    • 0029974620 scopus 로고    scopus 로고
    • The ubiquitously expressed human CYP51 encodes lanosterol 14α-demethylase, a cytochrome P450 whose expression is regulated by oxysterols
    • Strömstedt, M., Rozman, D. and Waterman, M. (1996) The ubiquitously expressed human CYP51 encodes lanosterol 14α-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. Arch. Biochem. Biophys. 329, 73-81.
    • (1996) Arch. Biochem. Biophys. , vol.329 , pp. 73-81
    • Strömstedt, M.1    Rozman, D.2    Waterman, M.3
  • 31
    • 0025816145 scopus 로고
    • Properties and structural requirements for substrate specificity of cytochrome P 450-dependent obtusifoliol 14α-demethylase from maize (Zea mays) seedlings
    • Taton, M. and Rahier, A. (1991) Properties and structural requirements for substrate specificity of cytochrome P 450-dependent obtusifoliol 14α-demethylase from maize (Zea mays) seedlings. Biochem. J. 277, 483-492.
    • (1991) Biochem. J. , vol.277 , pp. 483-492
    • Taton, M.1    Rahier, A.2
  • 32
    • 0029882092 scopus 로고    scopus 로고
    • Isolation and molecular characterisation of the gene encoding eburicol 14α-demethylase (CYP51) from Penicillium italicum
    • Van Nistelrooy, J.G.M., Van den Brink, J.M., Van Kan, J.A.L., Van Gorcom, R.F.M. and De Ward, M.A. (1996) Isolation and molecular characterisation of the gene encoding eburicol 14α-demethylase (CYP51) from Penicillium italicum. Mol. Gen. Genet. 250, 725-733.
    • (1996) Mol. Gen. Genet. , vol.250 , pp. 725-733
    • Van Nistelrooy, J.G.M.1    Van den Brink, J.M.2    Van Kan, J.A.L.3    Van Gorcom, R.F.M.4    De Ward, M.A.5
  • 33
    • 0001684253 scopus 로고
    • Sterol biosynthesis
    • Omura, T., Ishimura, Y Fujii-Kuriyama, Y., eds. Tokyo: Kodansha and Weinheim: VCH
    • Yoshida, Y. (1993) Sterol biosynthesis. In Cytochrome P-450, 2nd edn (Omura, T., Ishimura, Y. and Fujii-Kuriyama, Y., eds). Tokyo: Kodansha and Weinheim: VCH, pp. 93-101.
    • (1993) Cytochrome P-450, 2nd Edn , pp. 93-101
    • Yoshida, Y.1


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