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Volumn 65, Issue 3, 2009, Pages 260-265

Expression and homology modelling of sterol 14α-demethylase of Magnaporthe grisea and its interaction with azoles

Author keywords

Binding spectrum; CYP51; Expression; Homology modelling; Magnaporthe grisea; Molecular docking

Indexed keywords

AMINO ACID; CYTOCHROME P450; FUNGAL PROTEIN; FUNGICIDE; LANOSTEROL 14 ALPHA-DEMETHYLASE; PYRROLE DERIVATIVE; STEROL 14ALPHA DEMETHYLASE;

EID: 62549145789     PISSN: 1526498X     EISSN: 15264998     Source Type: Journal    
DOI: 10.1002/ps.1680     Document Type: Article
Times cited : (16)

References (28)
  • 2
    • 0034647710 scopus 로고    scopus 로고
    • Sterol 14-demethylase P450 (CYP51) provides a breakthrough for the discussion on the evolution of cytochrome P450 gene superfamily
    • Yoshida Y, Aoyama Y, Noshiro M and Gotoh O, Sterol 14-demethylase P450 (CYP51) provides a breakthrough for the discussion on the evolution of cytochrome P450 gene superfamily. Biochem Biophys Res Commun 273:799-804 (2000).
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 799-804
    • Yoshida, Y.1    Aoyama, Y.2    Noshiro, M.3    Gotoh, O.4
  • 3
    • 27544480885 scopus 로고    scopus 로고
    • Sterol 14α-demethylase, an abundant and essential mixed-function oxidase
    • Waterman MR and Lepesheva GI, Sterol 14α-demethylase, an abundant and essential mixed-function oxidase. Biochem Biophys Res Commun 338:418-422 (2005).
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 418-422
    • Waterman, M.R.1    Lepesheva, G.I.2
  • 4
    • 33846387040 scopus 로고    scopus 로고
    • Sterol 14α-demethylase cytochrome P450 (CYP51), a P450 in all biological kingdoms
    • Lepesheva GIand Waterman MR, Sterol 14α-demethylase cytochrome P450 (CYP51), a P450 in all biological kingdoms. Biochim Biophys Acta 1770:466-477 (2007).
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 466-477
    • Lepesheva1    GIand Waterman, M.R.2
  • 5
    • 27744551165 scopus 로고    scopus 로고
    • Current state of three-dimensional characterisation of antifungal targets and its use for molecular modelling in drug design
    • Ruge E, Korting HC and Borelli C, Current state of three-dimensional characterisation of antifungal targets and its use for molecular modelling in drug design. Internat J Antimicrob Ag 26:427-441 (2005).
    • (2005) Internat J Antimicrob Ag , vol.26 , pp. 427-441
    • Ruge, E.1    Korting, H.C.2    Borelli, C.3
  • 6
    • 0031891490 scopus 로고    scopus 로고
    • Construction of a model of the Candida albicans lanosterol 14α-demethylase active site using the homology modelling technique
    • Holtje H-D and Fattorusso C, Construction of a model of the Candida albicans lanosterol 14α-demethylase active site using the homology modelling technique. Pharm Acta Helv 72:271-277 (1998).
    • (1998) Pharm Acta Helv , vol.72 , pp. 271-277
    • Holtje, H.-D.1    Fattorusso, C.2
  • 7
    • 0028118297 scopus 로고
    • Modeling cytochrome P450 14 alpha demethylase (Candida albicans) from P450cam
    • Boscott PE and Grant GH, Modeling cytochrome P450 14 alpha demethylase (Candida albicans) from P450cam. J Mol Graph 12:185-192 (1994).
    • (1994) J Mol Graph , vol.12 , pp. 185-192
    • Boscott, P.E.1    Grant, G.H.2
  • 10
    • 0034729667 scopus 로고    scopus 로고
    • A three-dimensional model of lanosterol 14α-demethylase of Candida albicans and its interaction with azole antifungals
    • Ji H, Zhang W, Zhou Y, Zhang M, Zhu J, Song Y, et al, A three-dimensional model of lanosterol 14α-demethylase of Candida albicans and its interaction with azole antifungals. J Med Chem 43:2493-2505 (2000).
    • (2000) J Med Chem , vol.43 , pp. 2493-2505
    • Ji, H.1    Zhang, W.2    Zhou, Y.3    Zhang, M.4    Zhu, J.5    Song, Y.6
  • 11
    • 0346784897 scopus 로고    scopus 로고
    • Three-dimensional models of wild-type and mutated forms of cytochrome P450 14α-sterol demethylases from Aspergillus fumigatus and Candida albicans provide insights into posaconazole binding
    • Xiao L, Madison V, Chau AS, Loebenberg D, Palermo RE and McNicholas PM, Three-dimensional models of wild-type and mutated forms of cytochrome P450 14α-sterol demethylases from Aspergillus fumigatus and Candida albicans provide insights into posaconazole binding. Antimicrob Agents Chemother 48:568-574 (2004).
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 568-574
    • Xiao, L.1    Madison, V.2    Chau, A.S.3    Loebenberg, D.4    Palermo, R.E.5    McNicholas, P.M.6
  • 12
    • 2442514053 scopus 로고    scopus 로고
    • Modeling and interactions of Aspergillus fumigatus lanosterol 14-α demethylase 'A' with azole antifungals
    • Gollapudy R, Ajmani S and Kulkarni SA, Modeling and interactions of Aspergillus fumigatus lanosterol 14-α demethylase 'A' with azole antifungals. Bioorgan Med Chem 12:2937-2950 (2004).
    • (2004) Bioorgan Med Chem , vol.12 , pp. 2937-2950
    • Gollapudy, R.1    Ajmani, S.2    Kulkarni, S.A.3
  • 13
    • 22144453224 scopus 로고    scopus 로고
    • Molecular design of two sterol 14α-demethylase homology models and their interactions with the azole antifungals ketoconazole and bifonazole
    • Rupp B, Raub S, Marian C and Holtje H-D, Molecular design of two sterol 14α-demethylase homology models and their interactions with the azole antifungals ketoconazole and bifonazole. J Comput Aid Mol Des 19:149-163 (2005).
    • (2005) J Comput Aid Mol Des , vol.19 , pp. 149-163
    • Rupp, B.1    Raub, S.2    Marian, C.3    Holtje, H.-D.4
  • 14
    • 0027692823 scopus 로고
    • Identification and characterization of MPG1, a gene involved in pathogenicity from the rice blast fungus Magnaporthe grisea
    • Talbot NJ, Ebbole DJ and Hamer JE, Identification and characterization of MPG1, a gene involved in pathogenicity from the rice blast fungus Magnaporthe grisea. Plant Cell 5:1575-1590 (1993).
    • (1993) Plant Cell , vol.5 , pp. 1575-1590
    • Talbot, N.J.1    Ebbole, D.J.2    Hamer, J.E.3
  • 15
    • 0030998617 scopus 로고    scopus 로고
    • Characterization of Saccharomyces cerevisiae CYP51 and a CYP51 fusion protein with NADPH cytochrome P-450 oxidoreductase expressed in Escherichia coli
    • Venkateswarlu K, Kelly DE and Kelly SL, Characterization of Saccharomyces cerevisiae CYP51 and a CYP51 fusion protein with NADPH cytochrome P-450 oxidoreductase expressed in Escherichia coli. Antimicrob Agents Chemother 41:776-780 (1997).
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 776-780
    • Venkateswarlu, K.1    Kelly, D.E.2    Kelly, S.L.3
  • 16
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T and Sato R, The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J Biol Chem 239:2370-2378 (1964).
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 17
    • 0036775336 scopus 로고    scopus 로고
    • Azole antifungals are potent inhibitors of cytochrome P450 mono-oxygenases and bacterial growth in mycobacteria and streptomycetes
    • McLean KJ, Marshall KR, Richmond A, Hunter IS, Fowler K, Kieser T, et al, Azole antifungals are potent inhibitors of cytochrome P450 mono-oxygenases and bacterial growth in mycobacteria and streptomycetes. Microbiology 148:2937-2949 (2002).
    • (2002) Microbiology , vol.148 , pp. 2937-2949
    • McLean, K.J.1    Marshall, K.R.2    Richmond, A.3    Hunter, I.S.4    Fowler, K.5    Kieser, T.6
  • 18
    • 0030028176 scopus 로고    scopus 로고
    • Comparison of D0870, a new triazole antifungal agent, to fluconazole for inhibition of Candida albicans cytochrome P-450 by using in vitro assays
    • Venkateswarlu K, Denning DW, Manning NJ and Kelly SL, Comparison of D0870, a new triazole antifungal agent, to fluconazole for inhibition of Candida albicans cytochrome P-450 by using in vitro assays. Antimicrob Agents Chemother 40:1382-1386 (1996).
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1382-1386
    • Venkateswarlu, K.1    Denning, D.W.2    Manning, N.J.3    Kelly, S.L.4
  • 19
    • 0035967880 scopus 로고    scopus 로고
    • sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • FUGUE
    • Shi J, Blundell TL and Mizuguchi K, FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 310:243-257 (2001).
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 20
    • 33846636934 scopus 로고    scopus 로고
    • Tripos Inc, St Louis, MO
    • SYBYL7.0. Tripos Inc., St Louis, MO (2003).
    • (2003) SYBYL7.0
  • 21
    • 0032738842 scopus 로고    scopus 로고
    • Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking
    • Kramer B, Rarey M and Lengauer T, Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking. Proteins 37:228-241 (1999).
    • (1999) Proteins , vol.37 , pp. 228-241
    • Kramer, B.1    Rarey, M.2    Lengauer, T.3
  • 22
    • 0026088436 scopus 로고
    • The expression of a catalytically active cholesterol 7 alpha-hydroxylase cytochrome P450 in Escherichiacoli
    • Li YC and Chiang JY, The expression of a catalytically active cholesterol 7 alpha-hydroxylase cytochrome P450 in Escherichiacoli. J Biol Chem 266:19186-19191 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 19186-19191
    • Li, Y.C.1    Chiang, J.Y.2
  • 23
    • 37049010497 scopus 로고    scopus 로고
    • Application of binding spectra in DMIs fungicide screening
    • Xiao M, Yang J, Xiao W and Yang S, Application of binding spectra in DMIs fungicide screening. Chin J Biotech 23:165-170 (2007).
    • (2007) Chin J Biotech , vol.23 , pp. 165-170
    • Xiao, M.1    Yang, J.2    Xiao, W.3    Yang, S.4
  • 24
    • 0035853108 scopus 로고    scopus 로고
    • Crystal structure of cytochrome P450 14α-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors
    • Podust LM, Poulos TL and Waterman MR, Crystal structure of cytochrome P450 14α-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors. P Natl Acad Sci USA 98:3068-3073 (2001).
    • (2001) P Natl Acad Sci USA , vol.98 , pp. 3068-3073
    • Podust, L.M.1    Poulos, T.L.2    Waterman, M.R.3
  • 25
  • 26
    • 0030239348 scopus 로고    scopus 로고
    • Catalytic reactivities and structure/function relationships of cytochrome P450 enzymes
    • Halkier BA, Catalytic reactivities and structure/function relationships of cytochrome P450 enzymes. Phytochemistry 43:1-21 (1996).
    • (1996) Phytochemistry , vol.43 , pp. 1-21
    • Halkier, B.A.1
  • 28
    • 0032458367 scopus 로고    scopus 로고
    • Expression, purification, reconstitution and inhibition of Ustilago maydis sterol 14α-demethylase (CYP51;P45014DM)
    • Lamb DC, Kelly DE, Manning NJ, Hollomon DW and Kelly SL, Expression, purification, reconstitution and inhibition of Ustilago maydis sterol 14α-demethylase (CYP51;P45014DM). FEMS Microbiol Lett 169:369-373 (1998).
    • (1998) FEMS Microbiol Lett , vol.169 , pp. 369-373
    • Lamb, D.C.1    Kelly, D.E.2    Manning, N.J.3    Hollomon, D.W.4    Kelly, S.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.