메뉴 건너뛰기




Volumn 81, Issue 10, 2015, Pages 3379-3386

Novel substrate specificity and temperature-sensitive activity of Mycosphaerella graminicola CYP51 supported by the native NADPH cytochrome p450 reductase

Author keywords

[No Author keywords available]

Indexed keywords

AGRICULTURE; ALCOHOLS; CHEMICAL REACTIONS; FUNGICIDES;

EID: 84930013890     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03965-14     Document Type: Article
Times cited : (14)

References (32)
  • 1
    • 0034794248 scopus 로고    scopus 로고
    • Factors affecting diseases of winter wheat in England and Wales, 1989-98
    • Hardwick NV, Jones DR, Slough JE. 2001. Factors affecting diseases of winter wheat in England and Wales, 1989-98 Plant Pathol 50:650-652. http://dx.doi.org/10.1046/j.1365-3059.2001.00641.x.
    • (2001) Plant Pathol , vol.50 , pp. 650-652
    • Hardwick, N.V.1    Jones, D.R.2    Slough, J.E.3
  • 4
    • 0037402336 scopus 로고    scopus 로고
    • The role of sterols in plant growth and development
    • Schaller H. 2003. The role of sterols in plant growth and development Prog Lipid Res 42:163-175. http://dx.doi.org/10.1016/S0163-7827(02)00047-4.
    • (2003) Prog Lipid Res , vol.42 , pp. 163-175
    • Schaller, H.1
  • 5
    • 78650235983 scopus 로고    scopus 로고
    • Multiple mechanisms account for resistance to sterol 14_-demethylation inhibitors in field isolates of Mycosphaerella graminicola
    • Leroux P, Walker AS. 2011. Multiple mechanisms account for resistance to sterol 14_-demethylation inhibitors in field isolates of Mycosphaerella graminicola Pest Manage Sci 67:44-59. http://dx.doi.org/10.1002/ps.2028.
    • (2011) Pest Manage Sci , vol.67 , pp. 44-59
    • Leroux, P.1    Walker, A.S.2
  • 6
    • 84872760127 scopus 로고    scopus 로고
    • Update on mechanisms of azole resistance in Mycosphaerella graminicola and implications for future control
    • Cools HJ, Fraaije BA. 2013. Update on mechanisms of azole resistance in Mycosphaerella graminicola and implications for future control Pest Manage Sc 69:150-155. http://dx.doi.org/10.1002/ps.3348.
    • (2013) Pest Manage Sc , vol.69 , pp. 150-155
    • Cools, H.J.1    Fraaije, B.A.2
  • 7
    • 77749291956 scopus 로고    scopus 로고
    • Screening for amino acid substitutions in the Candida albicans Erg11 protein of azolesusceptible and azole-resistant clinical isolates: new substitutions and a review of the literature
    • Morio F, Loge C, Besse B, Hennequin C, Le Pape P. 2010. Screening for amino acid substitutions in the Candida albicans Erg11 protein of azolesusceptible and azole-resistant clinical isolates: new substitutions and a review of the literature Diagn Microbiol Infect Dis 66:373-384. http://dx .doi.org/10.1016/j.diagmicrobio.2009.11.006.
    • (2010) Diagn Microbiol Infect Dis , vol.66 , pp. 373-384
    • Morio, F.1    Loge, C.2    Besse, B.3    Hennequin, C.4    Le Pape, P.5
  • 8
    • 84864577072 scopus 로고    scopus 로고
    • Fungal cytochrome P450 sterol 14_- demethylase (CYP51) and azole resistance in plant and human pathogens
    • Becher R, Wirsel SG. 2012. Fungal cytochrome P450 sterol 14_- demethylase (CYP51) and azole resistance in plant and human pathogens Appl Microbiol Biotechnol 95:825- 840. http://dx.doi.org/10.1007/s00253-012-4195-9.
    • (2012) Appl Microbiol Biotechnol , vol.95 , pp. 825- 840
    • Becher, R.1    Wirsel, S.G.2
  • 9
    • 1842509253 scopus 로고    scopus 로고
    • Electron transfer by diflavin reductases
    • Murataliev MB, Feyereisen R, Walker FA. 2004. Electron transfer by diflavin reductases Biochim Biophys Acta 1698:1-26. http://dx.doi.org /10.1016/j.bbapap.2003.10.003.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 1-26
    • Murataliev, M.B.1    Feyereisen, R.2    Walker, F.A.3
  • 10
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17_-hydroxylase in Escherichia coli
    • Barnes HJ, Arlotto MP, Waterman MR. 1991. Expression and enzymatic activity of recombinant cytochrome P450 17_-hydroxylase in Escherichia coli Proc Natl Acad Sci U S A 88:5597-5601. http://dx.doi.org/10.1073/pnas.88.13.5597.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 11
    • 33646030623 scopus 로고    scopus 로고
    • Purification and characterization of bovine steroid 21-hydroxylase (P450c21) efficiently expressed in Escherichia coli
    • Arase M, Waterman MR, Kagawa N. 2006. Purification and characterization of bovine steroid 21-hydroxylase (P450c21) efficiently expressed in Escherichia coli Biochem Biophys Res Commun 344:400-405. http://dx.doi.org/10.1016/j.bbrc.2006.03.067.
    • (2006) Biochem Biophys Res Commun , vol.344 , pp. 400-405
    • Arase, M.1    Waterman, M.R.2    Kagawa, N.3
  • 12
    • 0017801794 scopus 로고
    • Purified liver microsomal NADPHcytchrome P450 reductase
    • Vermilion JL, Coon MJ. 1978. Purified liver microsomal NADPHcytchrome P450 reductase J Biol Chem 253:2694-2704.
    • (1978) J Biol Chem , vol.253 , pp. 2694-2704
    • Vermilion, J.L.1    Coon, M.J.2
  • 13
    • 0020490599 scopus 로고
    • Structural features of liver microsomal NADPH-cytochrome P-450 reductase- hydrophobic domain, hydrophilic domain and connecting region
    • Black SD, Coon MJ. 1982. Structural features of liver microsomal NADPH-cytochrome P-450 reductase- hydrophobic domain, hydrophilic domain and connecting region J Biol Chem 257:5929-5938.
    • (1982) J Biol Chem , vol.257 , pp. 5929-5938
    • Black, S.D.1    Coon, M.J.2
  • 20
    • 77952743082 scopus 로고    scopus 로고
    • Candida albicans NADPH-P450 reductase: expression, purification and characterization of recombinant protein
    • Park HG, Lim YR, Eun CY, Han S, Han JS, Cho KS, Chun YJ, Kim D. 2010. Candida albicans NADPH-P450 reductase: expression, purification and characterization of recombinant protein Biochem Biophys Res Commun 396:534-538. http://dx.doi.org/10.1016/j.bbrc.2010.04.138.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 534-538
    • Park, H.G.1    Lim, Y.R.2    Eun, C.Y.3    Han, S.4    Han, J.S.5    Cho, K.S.6    Chun, Y.J.7    Kim, D.8
  • 21
    • 0020479374 scopus 로고
    • Oxidation-reduction states of FMN and FAD in NADPH-cytochrome P-450 reductase during reduction by NADPH
    • Oprian DD, Coon MJ. 1982. Oxidation-reduction states of FMN and FAD in NADPH-cytochrome P-450 reductase during reduction by NADPH J Biol Chem 257:8935-8944.
    • (1982) J Biol Chem , vol.257 , pp. 8935-8944
    • Oprian, D.D.1    Coon, M.J.2
  • 22
    • 0025287247 scopus 로고
    • NADPHcytochrome P-450 reductase: physical properties and redox behavior in the absence of the FAD moiety
    • Kurzban GO, Howarth J, Plamer G, Strobel HW. 1990. NADPHcytochrome P-450 reductase: physical properties and redox behavior in the absence of the FAD moiety J Biol Chem 265:12272-12279.
    • (1990) J Biol Chem , vol.265 , pp. 12272-12279
    • Kurzban, G.O.1    Howarth, J.2    Plamer, G.3    Strobel, H.W.4
  • 23
    • 0036435507 scopus 로고    scopus 로고
    • Phanerochaete chrysosporium NADPH-cytochrome P450 reductase kinetic mechanism
    • Warrilow AGS, Lamb DC, Kelly DE, Kelly SL. 2002. Phanerochaete chrysosporium NADPH-cytochrome P450 reductase kinetic mechanism Biochem Biophys Res Commun 299:189-1915. http://dx.doi.org/10.1016/S0006-291X(02)02600-1.
    • (2002) Biochem Biophys Res Commun , vol.299 , pp. 189-1915
    • Warrilow, A.G.S.1    Lamb, D.C.2    Kelly, D.E.3    Kelly, S.L.4
  • 24
  • 25
    • 42449157733 scopus 로고    scopus 로고
    • Ortiz de Montellano PR (ed), Cytochrome P450: structure, mechanism, and biochemistry, 3rd ed. Kluwer Academic/Plenum Publishers, New York, NY
    • Groves JT. 2005. Models and mechanism of cytochrome P450 action, p 1- 43. In Ortiz de Montellano PR (ed), Cytochrome P450: structure, mechanism, and biochemistry, 3rd ed. Kluwer Academic/Plenum Publishers, New York, NY.
    • (2005) Models and mechanism of cytochrome P450 action , pp. 1- 43
    • Groves, J.T.1
  • 26
    • 0037518367 scopus 로고    scopus 로고
    • Purification and characterization of a soluble form of rat liver NADPHcytochrome P-450 reductase highly expressed in Escherichia coli
    • Hayashi S, Omata Y, Sakamoto H, Hara T, Noguchi M. 2003. Purification and characterization of a soluble form of rat liver NADPHcytochrome P-450 reductase highly expressed in Escherichia coli Protein Expr Purif 29:1-7. http://dx.doi.org/10.1016/S1046-5928(03)00023-8.
    • (2003) Protein Expr Purif , vol.29 , pp. 1-7
    • Hayashi, S.1    Omata, Y.2    Sakamoto, H.3    Hara, T.4    Noguchi, M.5
  • 27
    • 33845967142 scopus 로고    scopus 로고
    • Diminished FADbinding in the Y459H and V492E Antley-Bixler syndrome mutants of human cytochrome P450 reductase
    • Marohnic CC, Panda SP, Martasek P, Masters BS. 2006. Diminished FADbinding in the Y459H and V492E Antley-Bixler syndrome mutants of human cytochrome P450 reductase J Biol Chem 281:35975-35982. http://dx.doi.org/10.1074/jbc.M607095200.
    • (2006) J Biol Chem , vol.281 , pp. 35975-35982
    • Marohnic, C.C.1    Panda, S.P.2    Martasek, P.3    Masters, B.S.4
  • 28
    • 0032571427 scopus 로고    scopus 로고
    • Molecular diversity of sterol 14_- demethylase substrates in plants, fungi and humans
    • Lamb DC, Kelly DE, Kelly SL. 1998. Molecular diversity of sterol 14_- demethylase substrates in plants, fungi and humans FEBS Lett 425:263-265. http://dx.doi.org/10.1016/S0014-5793(98)00247-6.
    • (1998) FEBS Lett , vol.425 , pp. 263-265
    • Lamb, D.C.1    Kelly, D.E.2    Kelly, S.L.3
  • 29
    • 79960975304 scopus 로고    scopus 로고
    • Targeting Trypanosoma cruzi sterol 14_-demethylase (CYP51)
    • Lepesheva GI, Villalta F, Waterman MR. 2011. Targeting Trypanosoma cruzi sterol 14_-demethylase (CYP51) Adv Parasitol 75:65-87. http://dx .doi.org/10.1016/B978-0-12-385863-4.00004-6.
    • (2011) Adv Parasitol , vol.75 , pp. 65-87
    • Lepesheva, G.I.1    Villalta, F.2    Waterman, M.R.3
  • 30
    • 33847411922 scopus 로고    scopus 로고
    • Three-dimensional quantitative structure-activity relationship analysis of human CYP51 inhibitors
    • Ekins S, Mankowski DC, Hoover DJ, Lawton MP, Treadway JL, Harwood HJ. 2007. Three-dimensional quantitative structure-activity relationship analysis of human CYP51 inhibitors Drug Metab Dispos 35:493-500. http://dx.doi.org/10.1124/dmd.106.013888.
    • (2007) Drug Metab Dispos , vol.35 , pp. 493-500
    • Ekins, S.1    Mankowski, D.C.2    Hoover, D.J.3    Lawton, M.P.4    Treadway, J.L.5    Harwood, H.J.6
  • 31
    • 33749667750 scopus 로고    scopus 로고
    • Comparison of lanosterol-14_-demethylase (CYP51) of human and Candida albicans for inhibition by different antifungal azoles
    • Trösken ER, Adamska M, Arand M, Zarn JA, Patten C, Völkel W, Lutz WK. 2006. Comparison of lanosterol-14_-demethylase (CYP51) of human and Candida albicans for inhibition by different antifungal azoles Toxicology 228:24-32. http://dx.doi.org/10.1016/j.tox.2006.08.007.
    • (2006) Toxicology , vol.228 , pp. 24-32
    • Trösken, E.R.1    Adamska, M.2    Arand, M.3    Zarn, J.A.4    Patten, C.5    Völkel, W.6    Lutz, W.K.7
  • 32
    • 65249175098 scopus 로고    scopus 로고
    • The construction and characterization of self-sufficient lanosterol 14-demethylase fusion proteins consisting of yeast CYP51 and its reductase
    • Kitahama Y, Nakamura M, Yoshida Y, Aoyama Y. 2009. The construction and characterization of self-sufficient lanosterol 14-demethylase fusion proteins consisting of yeast CYP51 and its reductase Biol Pharm Bull 32:558-563. http://dx.doi.org/10.1248/bpb.32.558.
    • (2009) Biol Pharm Bull , vol.32 , pp. 558-563
    • Kitahama, Y.1    Nakamura, M.2    Yoshida, Y.3    Aoyama, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.