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Volumn 126, Issue 5, 1999, Pages 927-933

Purification and characterization of rat sterol 14-demethylase P450 (CYP51) expressed in Escherichia coli

Author keywords

Characterization; CYP51; Expressed enzyme; P450; Sterol 14 demethylase

Indexed keywords

COMPLEMENTARY DNA; CYTOCHROME P450 REDUCTASE; DIHYDROLANOSTEROL; FLUCONAZOLE; ITRACONAZOLE; KETOCONAZOLE; LANOSTEROL; METHYLTRANSFERASE;

EID: 0032722882     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022536     Document Type: Article
Times cited : (12)

References (25)
  • 2
    • 0021717363 scopus 로고
    • Cytochrome P-450-dependent oxidation of lanosterol in cholesterol biosynthesis. Microsomal electron transport and C-32 demethylation
    • Trzaskos, J.M., Brown, W.D., Shafiee, A., Fischer, R.T., and Gaylor, J.L. (1984) Cytochrome P-450-dependent oxidation of lanosterol in cholesterol biosynthesis. Microsomal electron transport and C-32 demethylation. J. Biol. Chem. 259, 13402-13412
    • (1984) J. Biol. Chem. , vol.259 , pp. 13402-13412
    • Trzaskos, J.M.1    Brown, W.D.2    Shafiee, A.3    Fischer, R.T.4    Gaylor, J.L.5
  • 3
    • 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
  • 4
    • 0002974935 scopus 로고
    • The P450 superfamily: A group of versatile hemoproteins contributing to the oxidation of various small molecules
    • (Fujita, H., ed.) AlphaMed Press, Dayton
    • Yoshida, Y. and Aoyama, Y. (1994) The P450 superfamily: A group of versatile hemoproteins contributing to the oxidation of various small molecules in Regulation of Heme Protein Synthesis (Fujita, H., ed.) pp. 75-88, AlphaMed Press, Dayton
    • (1994) Regulation of Heme Protein Synthesis , pp. 75-88
    • Yoshida, Y.1    Aoyama, Y.2
  • 5
    • 0031446299 scopus 로고    scopus 로고
    • Structural and evolutionary studies on sterol 14-demethylase P450 (CYP51), the most conserved P450 monooxygenase: II. Evolutionary analysis of protein and gene structures
    • Yoshida, Y., Noshiro, M., Aoyama, Y., Kawamoto, T., Horiuchi, T., and Gotoh, O. (1997) Structural and evolutionary studies on sterol 14-demethylase P450 (CYP51), the most conserved P450 monooxygenase: II. Evolutionary analysis of protein and gene structures. J. Biochem. 122, 1122-1128
    • (1997) J. Biochem. , vol.122 , pp. 1122-1128
    • Yoshida, Y.1    Noshiro, M.2    Aoyama, Y.3    Kawamoto, T.4    Horiuchi, T.5    Gotoh, O.6
  • 6
    • 0021330643 scopus 로고
    • Yeast cytochrome P-450 catalyzing lanosterol 14α-demethylation. I. Purification and spectral properties
    • Yoshida, Y. and Aoyama, Y. (1984) Yeast cytochrome P-450 catalyzing lanosterol 14α-demethylation. I. Purification and spectral properties. J. Biol. Chem. 259, 1655-1660
    • (1984) J. Biol. Chem. , vol.259 , pp. 1655-1660
    • Yoshida, Y.1    Aoyama, Y.2
  • 8
    • 0023656331 scopus 로고
    • Isolation and characterization of an altered cytochrome P-450 from a yeast mutant defective in lanosterol 14-demethylation
    • Aoyama, Y., Yoshida, Y., Nishino, T., Katsuki, H., Maitra, U.S., Mohan, V.P., and Sprinson, D.B. (1987) Isolation and characterization of an altered cytochrome P-450 from a yeast mutant defective in lanosterol 14-demethylation. J. Biol. Chem. 262, 14260-14264
    • (1987) J. Biol. Chem. , vol.262 , pp. 14260-14264
    • Aoyama, Y.1    Yoshida, Y.2    Nishino, T.3    Katsuki, H.4    Maitra, U.S.5    Mohan, V.P.6    Sprinson, D.B.7
  • 9
    • 0024441201 scopus 로고
    • 14DM (lanosterol 14-demethylase) from yeast. Evidence confirming the intermediate step of lanosterol 14-demethylation
    • 14DM (lanosterol 14-demethylase) from yeast. Evidence confirming the intermediate step of lanosterol 14-demethylation. J. Biol. Chem. 264, 18502-18505
    • (1989) J. Biol. Chem. , vol.264 , pp. 18502-18505
    • Aoyama, Y.1    Yoshida, Y.2    Sonoda, Y.3    Sato, Y.4
  • 10
    • 0006324683 scopus 로고
    • P450 Monooxygenase system of microorganisms
    • (Omura, T., Ishimura, Y., and Fujii-Kuriyama, Y., eds.) Kodansha, Tokyo
    • Yoshida, Y. (1993) P450 Monooxygenase system of microorganisms in Cytochrome P-450; Second Edition (Omura, T., Ishimura, Y., and Fujii-Kuriyama, Y., eds.) pp. 171-186, Kodansha, Tokyo
    • (1993) Cytochrome P-450; Second Edition , pp. 171-186
    • Yoshida, Y.1
  • 11
    • 0022829026 scopus 로고
    • Microsomal enzymes of cholesterol biosynthesis. Purification of lanosterol 14α-methyl demethylase cytochrome P450 from hepatic microsomes
    • Trzaskos, J.M., Kawata, S., and Gaylor, J.L. (1986) Microsomal enzymes of cholesterol biosynthesis. Purification of lanosterol 14α-methyl demethylase cytochrome P450 from hepatic microsomes. J. Biol. Chem. 261, 14651-14657
    • (1986) J. Biol. Chem. , vol.261 , pp. 14651-14657
    • Trzaskos, J.M.1    Kawata, S.2    Gaylor, J.L.3
  • 12
    • 0025772836 scopus 로고
    • 14DM (lanosterol 14α-demethylase) from pig liver microsomes
    • 14DM (lanosterol 14α-demethylase) from pig liver microsomes. Biochim. Biophys. Acta 1078, 388-394
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 388-394
    • Sono, H.1    Sonoda, Y.2    Sato, Y.3
  • 15
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • Yasukochi, Y. and Masters, B.S.S. (1976) Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography. J. Biol. Chem. 251, 5337-5344
    • (1976) J. Biol. Chem. , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.S.S.2
  • 16
    • 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
  • 17
    • 78651165715 scopus 로고
    • The carbon monooxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature
    • Omura, T. and Sato, R. (1964) The carbon monooxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature. J. Biol. Chem. 239, 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 20
    • 0031767825 scopus 로고    scopus 로고
    • CYP51-like gene of Mycobacterium tuberculosis actually encodes a P450 similar to eukaryotic CYP51
    • Aoyama, Y., Horiuchi, T., Gotoh, O., Noshiro, M., and Yoshida, Y. (1998) CYP51-like gene of Mycobacterium tuberculosis actually encodes a P450 similar to eukaryotic CYP51. J. Biochem. 124, 694-696
    • (1998) J. Biochem. , vol.124 , pp. 694-696
    • Aoyama, Y.1    Horiuchi, T.2    Gotoh, O.3    Noshiro, M.4    Yoshida, Y.5
  • 21
    • 0026072189 scopus 로고
    • 14DM) of Saccharomyces cerevisiae and rat liver for 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol
    • 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
  • 22
    • 0023134858 scopus 로고
    • 14DM purified from Saccharomyces cerevisiae microsomes
    • 14DM purified from Saccharomyces cerevisiae microsomes. Biochem. Pharmacol. 36, 229-235
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 229-235
    • Yoshida, Y.1    Aoyama, Y.2
  • 23
    • 0026470725 scopus 로고
    • Inhibition by a novel azole antifungal agent with a geranyl group on lanosterol 14α-demethylase of yeast
    • Aoyama, Y., Ishida, K., Hori, K., Sakaguchi, A., Kudoh, M., and Yoshida, Y. (1992) Inhibition by a novel azole antifungal agent with a geranyl group on lanosterol 14α-demethylase of yeast. Biochem. Pharmacol. 44, 1701-1705
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 1701-1705
    • Aoyama, Y.1    Ishida, K.2    Hori, K.3    Sakaguchi, A.4    Kudoh, M.5    Yoshida, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.