메뉴 건너뛰기




Volumn 6, Issue 7, 2014, Pages 1620-1634

Fungal cytochrome P450 monooxygenases: Their distribution, structure, functions, family expansion, and evolutionary origin

Author keywords

Characteristic motif; Cytochrome P450; Duplication; Evolution; Fungi

Indexed keywords

CYTOCHROME P450;

EID: 84921915065     PISSN: None     EISSN: 17596653     Source Type: Journal    
DOI: 10.1093/gbe/evu132     Document Type: Article
Times cited : (184)

References (64)
  • 1
    • 0029946638 scopus 로고    scopus 로고
    • Sterol 14-demethylase p450 (p45014dm) is one of the most ancient and conserved p450 species
    • Aoyama Y, et al (1996) Sterol 14-demethylase P450 (P45014DM) is one of the most ancient and conserved P450 species. J Biochem. 119: 926-933.
    • (1996) J Biochem. , vol.119 , pp. 926-933
    • Aoyama, Y.1
  • 2
    • 79957753066 scopus 로고    scopus 로고
    • Double oxidation of the cyclic nonaketide dihydromonacolin l to monacolin j by a single cytochrome p450 monooxygenase, lova
    • Barriuso J, et al (2011) Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA. J Am Chem Soc. 133: 8078-8081.
    • (2011) J Am Chem Soc. , vol.133 , pp. 8078-8081
    • Barriuso, J.1
  • 3
    • 84864577072 scopus 로고    scopus 로고
    • Fungal cytochrome p450 sterol 14 alphademethylase (cyp51) and azole resistance in plant and human pathogens
    • Becher R, Wirsel SG (2012) Fungal cytochrome P450 sterol 14 alphademethylase (CYP51) and azole resistance in plant and human pathogens. Appl Microbiol Biotechnol. 95: 825-840.
    • (2012) Appl Microbiol Biotechnol. , vol.95 , pp. 825-840
    • Becher, R.1    Wirsel, S.G.2
  • 4
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes p450 as versatile biocatalysts
    • Bernhardt R (2006) Cytochromes P450 as versatile biocatalysts. J Biotechnol. 124: 128-145.
    • (2006) J Biotechnol. , vol.124 , pp. 128-145
    • Bernhardt, R.1
  • 5
    • 77952358375 scopus 로고    scopus 로고
    • Structural characterization of cyp51 from trypanosoma cruzi and trypanosoma brucei bound to the antifungal drugs posaconazole and fluconazole
    • Chen CK, et al (2010) Structural characterization of CYP51 from Trypanosoma cruzi and Trypanosoma brucei bound to the antifungal drugs posaconazole and fluconazole. PLoS Negl Trop Dis. 4: e651.
    • (2010) PLoS Negl Trop Dis. , vol.4
    • Chen, C.K.1
  • 7
    • 33947286723 scopus 로고    scopus 로고
    • The evolutionary history of cytochrome p450 genes in four filamentous ascomycetes
    • Deng JX, Carbone I, Dean RA (2007) The evolutionary history of cytochrome P450 genes in four filamentous Ascomycetes. BMC Evol Biol. 7: 30.
    • (2007) BMC Evol Biol. , vol.7 , pp. 30
    • Deng, J.X.1    Carbone, I.2    Dean, R.A.3
  • 8
    • 25444445534 scopus 로고    scopus 로고
    • Genome-wide structural and evolutionary analysis of the p450 monooxygenase genes (p450ome) in the white rot fungus phanerochaete chrysosporium: Evidence for gene duplications and extensive gene clustering
    • Doddapaneni H, Chakraborty R, Yadav JS (2005) Genome-wide structural and evolutionary analysis of the P450 monooxygenase genes (P450ome) in the white rot fungus Phanerochaete chrysosporium: evidence for gene duplications and extensive gene clustering. BMC Genomics 6: 92.
    • (2005) BMC Genomics , vol.6 , pp. 92
    • Doddapaneni, H.1    Chakraborty, R.2    Yadav, J.S.3
  • 9
    • 79961228770 scopus 로고    scopus 로고
    • The plant cell wall-decomposing machinery underlies the functional diversity of forest fungi
    • Eastwood DC, et al (2011) The plant cell wall-decomposing machinery underlies the functional diversity of forest fungi. Science 333: 762-765.
    • (2011) Science , vol.333 , pp. 762-765
    • Eastwood, D.C.1
  • 10
    • 0043206081 scopus 로고    scopus 로고
    • The origin of the metazoa in the light of the proterozoic fossil record
    • Fedonkin MA (2003) The origin of the Metazoa in the light of the Proterozoic fossil record. Paleontol Res. 7: 9-41.
    • (2003) Paleontol Res. , vol.7 , pp. 9-41
    • Fedonkin, M.A.1
  • 11
    • 78649445838 scopus 로고    scopus 로고
    • Arthropod cypomes illustrate the tempo and mode in p450 evolution
    • Feyereisen R (2011) Arthropod CYPomes illustrate the tempo and mode in P450 evolution. Biochim Biophys Acta. 1814: 19-28.
    • (2011) Biochim Biophys Acta. , vol.1814 , pp. 19-28
    • Feyereisen, R.1
  • 12
    • 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
  • 13
    • 0033200309 scopus 로고    scopus 로고
    • How similar are p450s and what can their differences teach us?
    • Graham SE, Peterson JA (1999) How similar are P450s and what can their differences teach us? Arch Biochem Biophys. 369: 24-29.
    • (1999) Arch Biochem Biophys. , vol.369 , pp. 24-29
    • Graham, S.E.1    Peterson, J.A.2
  • 14
    • 36048939609 scopus 로고    scopus 로고
    • Mechanisms of cytochrome p450 substrate oxidation: Minireview
    • Guengerich FP (2007) Mechanisms of cytochrome P450 substrate oxidation: MiniReview. J Biochem Mol Toxicol. 21: 163-168.
    • (2007) J Biochem Mol Toxicol. , vol.21 , pp. 163-168
    • Guengerich, F.P.1
  • 15
    • 84862909219 scopus 로고    scopus 로고
    • Structural complex of sterol 14a-demethylase (cyp51) with 14a-methylenecyclopropyl-7-24, 25-dihydrolanosterol
    • Hargrove TY, et al (2012) Structural complex of sterol 14a-demethylase (CYP51) with 14a-methylenecyclopropyl-7-24, 25-dihydrolanosterol. J Lipid Res. 53: 311-320.
    • (2012) J Lipid Res. , vol.53 , pp. 311-320
    • Hargrove, T.Y.1
  • 16
    • 0031041652 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of a putative substrate recognition site in human cytochrome p450 3a4: Role of residues 210 and 211 in flavonoid activation and substrate specificity
    • Harlow GR, Halpert JR (1997) Alanine-scanning mutagenesis of a putative substrate recognition site in human cytochrome P450 3A4: role of residues 210 and 211 in flavonoid activation and substrate specificity. J Biol Chem. 272: 5396-5402.
    • (1997) J Biol Chem. , vol.272 , pp. 5396-5402
    • Harlow, G.R.1    Halpert, J.R.2
  • 18
    • 0027931515 scopus 로고
    • Site-directed mutagenesis of putative substrate recognition sites in cytochrome p450 2b11: Importance of amino acid residues 114, 290, and 363 for substrate specificity
    • Hasler JA, et al (1994) Site-directed mutagenesis of putative substrate recognition sites in cytochrome P450 2B11: importance of amino acid residues 114, 290, and 363 for substrate specificity. Mol Pharmacol. 46: 338-345.
    • (1994) Mol Pharmacol. , vol.46 , pp. 338-345
    • Hasler, J.A.1
  • 19
    • 33947694781 scopus 로고    scopus 로고
    • Natural products of filamentous fungi: Enzymes, genes, and their regulation
    • Hoffmeister D, Keller NP (2007) Natural products of filamentous fungi: enzymes, genes, and their regulation. Nat Prod Rep. 24: 393-416.
    • (2007) Nat Prod Rep. , vol.24 , pp. 393-416
    • Hoffmeister, D.1    Keller, N.P.2
  • 20
    • 33750329972 scopus 로고    scopus 로고
    • Reconstructing the early evolution of fungi using a six-gene phylogeny
    • James TY, et al (2006) Reconstructing the early evolution of fungi using a six-gene phylogeny. Nature 443: 818-822.
    • (2006) Nature , vol.443 , pp. 818-822
    • James, T.Y.1
  • 21
    • 43149091467 scopus 로고    scopus 로고
    • A fungal cytochrome p450 is expressed during the interaction between the fungal pathogen heterobasidion annosum sensu lato and conifer trees
    • Karlsson M, Elfstrand M, Stenlid J, Olson A (2008) A fungal cytochrome P450 is expressed during the interaction between the fungal pathogen Heterobasidion annosum sensu lato and conifer trees. DNA Seq. 19: 115-120.
    • (2008) DNA Seq. , vol.19 , pp. 115-120
    • Karlsson, M.1    Elfstrand, M.2    Stenlid, J.3    Olson, A.4
  • 22
    • 0031019841 scopus 로고    scopus 로고
    • Aspergillus nidulans stcl encodes a putative cytochrome p450 monooxygenase required for bisfuran desaturation during aflatoxin/ sterigmatocystin biosynthesis
    • Kelkar HS, Skloss TW, Haw JF, Keller NP, Adams TH (1997) Aspergillus nidulans stcL encodes a putative cytochrome P450 monooxygenase required for bisfuran desaturation during aflatoxin/sterigmatocystin biosynthesis. J Biol Chem. 272: 1589-1594.
    • (1997) J Biol Chem. , vol.272 , pp. 1589-1594
    • Kelkar, H.S.1    Skloss, T.W.2    Haw, J.F.3    Keller, N.P.4    Adams, T.H.5
  • 24
    • 84880141746 scopus 로고    scopus 로고
    • Microbial cytochromes p450: Biodiversity and biotechnology. Where do cytochromes p450 come from, what do they do and what can they do for us?
    • Kelly SL, Kelly DE (2013) Microbial cytochromes P450: biodiversity and biotechnology. Where do cytochromes P450 come from, what do they do and what can they do for us? Philos Trans R Soc B. 368: 20120476.
    • (2013) Philos Trans R Soc B. , vol.368 , pp. 20120476
    • Kelly, S.L.1    Kelly, D.E.2
  • 25
    • 0030893379 scopus 로고    scopus 로고
    • Characterization of saccharomyces cerevisiae cyp61, sterol delta(22)-desaturase, and inhibition by azole antifungal agents
    • Kelly SL, Lamb DC, Baldwin BC, Corran AJ, Kelly DE (1997) Characterization of Saccharomyces cerevisiae CYP61, sterol Delta(22)-desaturase, and inhibition by azole antifungal agents. J Biol Chem. 272: 9986-9988.
    • (1997) J Biol Chem. , vol.272 , pp. 9986-9988
    • Kelly, S.L.1    Lamb, D.C.2    Baldwin, B.C.3    Corran, A.J.4    Kelly, D.E.5
  • 28
    • 0037025384 scopus 로고    scopus 로고
    • The cytochrome p450 complement (cypome) of streptomyces coelicolor a3(2
    • Lamb DC, et al (2002) The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2). J Biol Chem. 277: 24000-24005.
    • (2002) J Biol Chem. , vol.277 , pp. 24000-24005
    • Lamb, D.C.1
  • 30
    • 0041664878 scopus 로고    scopus 로고
    • Conservation in the cyp51 family. Role of the b0 helix/bc loop and helices f and g in enzymatic function
    • Lepesheva GI, Virus C, Waterman MR (2003) Conservation in the CYP51 family. Role of the B0 helix/BC loop and helices F and G in enzymatic function. Biochemistry 42: 9091-9101.
    • (2003) Biochemistry , vol.42 , pp. 9091-9101
    • Lepesheva, G.I.1    Virus, C.2    Waterman, M.R.3
  • 32
    • 33846387040 scopus 로고    scopus 로고
    • Sterol 14 alpha-demethylase cytochrome p450 (cyp51), a p450 in all biological kingdoms
    • Lepesheva GI, Waterman MR (2007) Sterol 14 alpha-demethylase cytochrome P450 (CYP51), a P450 in all biological kingdoms. Biochim Biophys Acta. 1770: 467-477.
    • (2007) Biochim Biophys Acta. , vol.1770 , pp. 467-477
    • Lepesheva, G.I.1    Waterman, M.R.2
  • 33
    • 33845873289 scopus 로고    scopus 로고
    • Interactive tree of life (itol): An online tool for phylogenetic tree display and annotation
    • Letunic I, Bork P (2007) Interactive Tree of Life (iTOL): an online tool for phylogenetic tree display and annotation. Bioinformatics 23: 127-128.
    • (2007) Bioinformatics , vol.23 , pp. 127-128
    • Letunic, I.1    Bork, P.2
  • 34
    • 41449117994 scopus 로고    scopus 로고
    • Structures of prostacyclin synthase and its complexes with substrate analog and inhibitor reveal a ligand-specific heme conformation change
    • Li YC, et al (2008) Structures of prostacyclin synthase and its complexes with substrate analog and inhibitor reveal a ligand-specific heme conformation change. J Biol Chem. 283: 2917-2926.
    • (2008) J Biol Chem. , vol.283 , pp. 2917-2926
    • Li, Y.C.1
  • 36
    • 0031957137 scopus 로고    scopus 로고
    • Symbiosis between nitrogen-fixing cyanobacteria and plants-The establishment of symbiosis causes dramatic morphological and physiological changes in the cyanobacterium
    • Meeks JC (1998) Symbiosis between nitrogen-fixing cyanobacteria and plants-The establishment of symbiosis causes dramatic morphological and physiological changes in the cyanobacterium. Bioscience 48: 266-276.
    • (1998) Bioscience , vol.48 , pp. 266-276
    • Meeks, J.C.1
  • 37
    • 84866948231 scopus 로고    scopus 로고
    • Systematic and searchable classification of cytochrome p450 proteins encoded by fungal and oomycete genomes
    • Moktali V, et al (2012) Systematic and searchable classification of cytochrome P450 proteins encoded by fungal and oomycete genomes. BMC Genomics 13: 525.
    • (2012) BMC Genomics , vol.13 , pp. 525
    • Moktali, V.1
  • 38
    • 67349191068 scopus 로고    scopus 로고
    • Cyp710a genes encoding sterol c22-desaturase in physcomitrella patens as molecular evidence for the evolutionary conservation of a sterol biosynthetic pathway in plants
    • Morikawa T, Saga H, Hashizume H, Ohta D (2009) CYP710A genes encoding sterol C22-desaturase in Physcomitrella patens as molecular evidence for the evolutionary conservation of a sterol biosynthetic pathway in plants. Planta 229: 1311-1322.
    • (2009) Planta , vol.229 , pp. 1311-1322
    • Morikawa, T.1    Saga, H.2    Hashizume, H.3    Ohta, D.4
  • 39
    • 33745437728 scopus 로고    scopus 로고
    • Cytochrome p450 cyp710a encodes the sterol c-22 desaturase in arabidopsis and tomato
    • Morikawa T, et al (2006) Cytochrome P450 CYP710A encodes the sterol C-22 desaturase in Arabidopsis and tomato. Plant Cell 18: 1008-1022.
    • (2006) Plant Cell , vol.18 , pp. 1008-1022
    • Morikawa, T.1
  • 41
    • 0033199227 scopus 로고    scopus 로고
    • Cytochrome p450 and the individuality of species
    • Nelson DR (1999a. Cytochrome P450 and the individuality of species. Arch Biochem Biophys. 369: 1-10.
    • (1999) Arch Biochem Biophys. , vol.369 , pp. 1-10
    • Nelson, D.R.1
  • 42
    • 84940235010 scopus 로고    scopus 로고
    • [cited 2013 Aug 19]. Available from: Memphis (TN): The University of Tennessee Health Science Center
    • Nelson DR (1999b. Note on P450 evolution in yeasts and early eukaryotes. [cited 2013 Aug 19]. Available from: http: //drnelson.uthsc.edu/yeastP450.evol. html. Memphis (TN): The University of Tennessee Health Science Center.
    • (1999) Note on P450 Evolution in Yeasts and Early Eukaryotes
    • Nelson, D.R.1
  • 43
    • 33745177792 scopus 로고    scopus 로고
    • 2004) In: Phillips IR, Shephard EA, editors. Cytochrome P450 protocols. Totowa (NJ): Springer
    • Nelson DR (2006a. Cytochrome P450 nomenclature, 2004) In: Phillips IR, Shephard EA, editors. Cytochrome P450 protocols. Totowa (NJ): Springer. p. 1-10.
    • (2006) Cytochrome P450 Nomenclature , pp. 1-10
    • Nelson, D.R.1
  • 44
    • 33845431616 scopus 로고    scopus 로고
    • Plant cytochrome p450s from moss to poplar
    • Nelson DR (2006b. Plant cytochrome P450s from moss to poplar. Phytochem Rev. 5: 193-204.
    • (2006) Phytochem Rev. , vol.5 , pp. 193-204
    • Nelson, D.R.1
  • 45
    • 73249132581 scopus 로고    scopus 로고
    • The cytochrome p450 homepage
    • Nelson DR (2009) The cytochrome P450 homepage. Hum Genomics. 4: 59-65.
    • (2009) Hum Genomics. , vol.4 , pp. 59-65
    • Nelson, D.R.1
  • 46
    • 80052019696 scopus 로고    scopus 로고
    • Estimating the timing of early eukaryotic diversification with multigene molecular clocks
    • Parfrey LW, Lahr DJG, Knoll AH, Katz LA (2011) Estimating the timing of early eukaryotic diversification with multigene molecular clocks. Proc Natl Acad Sci U S A (108: 13624-13629.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 13624-13629
    • Parfrey, L.W.1    Lahr, D.J.G.2    Knoll, A.H.3    Katz, L.A.4
  • 47
    • 52449096190 scopus 로고    scopus 로고
    • Fungal cytochrome p450 database
    • Park J, et al (2008) Fungal cytochrome P450 database. BMC Genomics 9: 402.
    • (2008) BMC Genomics , vol.9 , pp. 402
    • Park, J.1
  • 48
    • 0035893831 scopus 로고    scopus 로고
    • Substrate recognition sites in 14 a-sterol demethylase from comparative analysis of amino acid sequences and x-ray structure of mycobacterium tuberculosis cyp51
    • Podust LM, Stojan J, Poulos TL, Waterman MR (2001) Substrate recognition sites in 14 a-sterol demethylase from comparative analysis of amino acid sequences and X-ray structure of Mycobacterium tuberculosis CYP51) J Inorg Biochem. 87: 227-235.
    • (2001) J Inorg Biochem. , vol.87 , pp. 227-235
    • Podust, L.M.1    Stojan, J.2    Poulos, T.L.3    Waterman, M.R.4
  • 49
    • 67649327176 scopus 로고    scopus 로고
    • Fasttree: Computing large minimum evolution trees with profiles instead of a distancematrix
    • Price MN, Dehal PS, Arkin AP (2009) FastTree: computing large minimum evolution trees with profiles instead of a distancematrix. Mol Biol Evol. 26: 1641-1650.
    • (2009) Mol Biol Evol. , vol.26 , pp. 1641-1650
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 50
    • 0036124296 scopus 로고    scopus 로고
    • New views on fungal evolution based on dna markers and the fossil record
    • Redecker D (2002) New views on fungal evolution based on DNA markers and the fossil record. Res Microbiol. 153: 125-130.
    • (2002) Res Microbiol. , vol.153 , pp. 125-130
    • Redecker, D.1
  • 51
    • 18844473326 scopus 로고    scopus 로고
    • New aspects on lanosterol 14 a-demethylase and cytochrome p450 evolution: Lanosterol/cycloartenol diversification and lateral transfer
    • Rezen T, Debeljak N, Kordis? D, Rozman D (2004) New aspects on lanosterol 14 a-demethylase and cytochrome P450 evolution: lanosterol/cycloartenol diversification and lateral transfer. J Mol Evol. 59: 51-58.
    • (2004) J Mol Evol. , vol.59 , pp. 51-58
    • Rezen, T.1    Debeljak, N.2    Kordis, D.3    Rozman, D.4
  • 52
    • 0024582440 scopus 로고
    • Characterization of the alkane inducible cytochrome p450 (p450alk) gene from the yeast candida tropicalis-identification of a new p450 gene family
    • Sanglard D, Loper JC (1989) Characterization of the alkane inducible cytochrome P450 (P450alk) gene from the yeast Candida tropicalis-identification of a new P450 gene family. Gene 76: 121-136.
    • (1989) Gene , vol.76 , pp. 121-136
    • Sanglard, D.1    Loper, J.C.2
  • 53
    • 0034710909 scopus 로고    scopus 로고
    • A single amino acid substitution (f363i) converts the regiochemistry of the spearmint (-limonene hydroxylase from a c6-to a c3-hydroxylase
    • Schalk M, Croteau R (2000) A single amino acid substitution (F363I) converts the regiochemistry of the spearmint (1)-limonene hydroxylase from a C6-to a C3-hydroxylase. Proc Natl Acad Sci U S A. 97: 11948-11953.
    • (2000) Proc Natl Acad Sci U S A. , vol.97 , pp. 11948-11953
    • Schalk, M.1    Croteau, R.2
  • 54
    • 0025008168 scopus 로고
    • Sequence logos-A newway to display consensus sequences
    • Schneider TD, Stephens RM (1990) Sequence logos-A newway to display consensus sequences. Nucleic Acids Res. 18: 6097-6100.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 56
    • 19544391219 scopus 로고    scopus 로고
    • Functional analysis of the cytochrome p450 monooxygenase gene bcbot1 of botrytis cinerea indicates that botrydial is a strain-specific virulence factor
    • Siewers V, et al (2005) Functional analysis of the cytochrome P450 monooxygenase gene bcbot1 of Botrytis cinerea indicates that botrydial is a strain-specific virulence factor. Mol Plant Microbe Ineract. 18: 602-612.
    • (2005) Mol Plant Microbe Ineract. , vol.18 , pp. 602-612
    • Siewers, V.1
  • 57
    • 48449101486 scopus 로고    scopus 로고
    • Comparative genome analysis of filamentous fungi reveals gene family expansions associatedwith fungal pathogenesis
    • Soanes DM, et al (2008) Comparative genome analysis of filamentous fungi reveals gene family expansions associatedwith fungal pathogenesis. PLoS One 3: e2300.
    • (2008) PLoS One , vol.3
    • Soanes, D.M.1
  • 58
    • 0027323306 scopus 로고
    • Molecular cloning of an allene oxide synthase-A cytochrome p450 specialized for the metabolism of fatty acid hydroperoxides
    • Song WC, Funk CD, Brash AR (1993) Molecular cloning of an allene oxide synthase-A cytochrome P450 specialized for the metabolism of fatty acid hydroperoxides. Proc Natl Acad Sci U S A. 90: 8519-8523.
    • (1993) Proc Natl Acad Sci U S A. , vol.90 , pp. 8519-8523
    • Song, W.C.1    Funk, C.D.2    Brash, A.R.3
  • 59
    • 77955490196 scopus 로고    scopus 로고
    • The amphimedon queenslandica genome and the evolution of animal complexity
    • Srivastava M, et al (2010) The Amphimedon queenslandica genome and the evolution of animal complexity. Nature 466: 720-723.
    • (2010) Nature , vol.466 , pp. 720-723
    • Srivastava, M.1
  • 60
    • 84867027657 scopus 로고    scopus 로고
    • P450 monooxygenases (p450ome) of the model white rot fungus phanerochaete chrysosporium
    • Syed K, Yadav JS (2012) P450 monooxygenases (P450ome) of the model white rot fungus Phanerochaete chrysosporium. Crit Rev Microbiol. 38: 339-363.
    • (2012) Crit Rev Microbiol. , vol.38 , pp. 339-363
    • Syed, K.1    Yadav, J.S.2
  • 61
    • 34247601439 scopus 로고    scopus 로고
    • Dating divergences in the fungal tree of life: Review and new analyses
    • Taylor JW, Berbee ML (2006) Dating divergences in the fungal tree of life: review and new analyses. Mycologia 98: 838-849.Waterhouse AM, Procter JB, Martin DMA, Clamp M, Barton GJ (2009) Jalview version 2-A multiple sequence alignment editor and analysis workbench. Bioinformatics 25: 1189-1191.
    • (2006) Mycologia , vol.98 , pp. 838-849
    • Taylor, J.W.1    Berbee, M.L.2
  • 64
    • 0021330643 scopus 로고
    • Yeast cytochrome p450 catalyzing lanosterol 14-alpha-demethylation. I. Purification and spectral properties
    • Yoshida Y, Aoyama Y (1984) Yeast cytochrome P450 catalyzing lanosterol 14-alpha-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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.