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Volumn 17, Issue 12, 2010, Pages 1295-1305

The CYPome of sorangium cellulosum so ce56 and identification of CYP109D1 as a new fatty acid hydroxylase

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; FATTY ACID; MIXED FUNCTION OXIDASE;

EID: 78650457236     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2010.10.010     Document Type: Article
Times cited : (49)

References (59)
  • 1
    • 0028794689 scopus 로고    scopus 로고
    • Cytochrome P450: Structure, function and generation of reactive oxygen species
    • R. Bernhardt Cytochrome P450: structure, function and generation of reactive oxygen species Rev. Physiol. Biochem. Pharmacol. 127 1996 137 221
    • (1996) Rev. Physiol. Biochem. Pharmacol. , vol.127 , pp. 137-221
    • Bernhardt, R.1
  • 2
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes P450 as versatile biocatalysts
    • R. Bernhardt Cytochromes P450 as versatile biocatalysts J. Biotechnol. 124 2006 128 145
    • (2006) J. Biotechnol. , vol.124 , pp. 128-145
    • Bernhardt, R.1
  • 3
    • 12944307859 scopus 로고    scopus 로고
    • Biosynthesis of iso-fatty acids in myxobacteria: Iso-even fatty acids are derived by alpha-oxidation from iso-odd fatty acids
    • H.B. Bode, J.S. Dickschat, R.M. Kroppenstedt, S. Schulz, and R. Muller Biosynthesis of iso-fatty acids in myxobacteria: iso-even fatty acids are derived by alpha-oxidation from iso-odd fatty acids J. Am. Chem. Soc. 127 2005 532 533
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 532-533
    • Bode, H.B.1    Dickschat, J.S.2    Kroppenstedt, R.M.3    Schulz, S.4    Muller, R.5
  • 4
    • 33746603596 scopus 로고    scopus 로고
    • Straight-chain fatty acids are dispensable in the myxobacterium Myxococcus xanthus for vegetative growth and fruiting body formation
    • H.B. Bode, M.W. Ring, D. Kaiser, A.C. David, R.M. Kroppenstedt, and G. Schwar Straight-chain fatty acids are dispensable in the myxobacterium Myxococcus xanthus for vegetative growth and fruiting body formation J. Bacteriol. 188 2006 5632 5634
    • (2006) J. Bacteriol. , vol.188 , pp. 5632-5634
    • Bode, H.B.1    Ring, M.W.2    Kaiser, D.3    David, A.C.4    Kroppenstedt, R.M.5    Schwar, G.6
  • 5
    • 59649111785 scopus 로고    scopus 로고
    • Identification of additional players in the alternative biosynthesis pathway to isovaleryl-CoA in the myxobacterium Myxococcus xanthus
    • H.B. Bode, M.W. Ring, G. Schwäre, O.M. Altmeyer, C. Kegler, R.I. Jose, M. Singer, and R. Müller Identification of additional players in the alternative biosynthesis pathway to isovaleryl-CoA in the myxobacterium Myxococcus xanthus ChemBioChem 10 2009 128 140
    • (2009) ChemBioChem , vol.10 , pp. 128-140
    • Bode, H.B.1    Ring, M.W.2    Schwäre, G.3    Altmeyer, O.M.4    Kegler, C.5    Jose, R.I.6    Singer, M.7    Müller, R.8
  • 6
    • 47149091298 scopus 로고    scopus 로고
    • Production of the antifungal isochromanone ajudazols A and B in Chondromyces crocatus Cm c5: Biosynthetic machinery and cytochrome P450 modifications
    • K. Buntin, S. Rachid, M. Scharfe, H. Blöcker, J.K. Weissman, and R. Müller Production of the antifungal isochromanone ajudazols A and B in Chondromyces crocatus Cm c5: biosynthetic machinery and cytochrome P450 modifications Angew. Chem. Int. Ed. Engl. 47 2008 4595 4599
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 4595-4599
    • Buntin, K.1    Rachid, S.2    Scharfe, M.3    Blöcker, H.4    Weissman, J.K.5    Müller, R.6
  • 7
    • 34547118130 scopus 로고    scopus 로고
    • Electron transport pathway for a Streptomyces cytochrome P450: Cytochrome P450 105D5-catalyzed fatty acid hydroxylation in Streptomyces coelicolor A3(2)
    • Y.J. Chun, T. Shimada, R. Sanchez-Ponce, M.V. Martin, L. Lei, B. Zhao, S.L. Kelly, M.R. Waterman, D.C. Lamb, and F.P. Guengerich Electron transport pathway for a Streptomyces cytochrome P450: cytochrome P450 105D5-catalyzed fatty acid hydroxylation in Streptomyces coelicolor A3(2) J. Biol. Chem. 282 2007 17486 17500
    • (2007) J. Biol. Chem. , vol.282 , pp. 17486-17500
    • Chun, Y.J.1    Shimada, T.2    Sanchez-Ponce, R.3    Martin, M.V.4    Lei, L.5    Zhao, B.6    Kelly, S.L.7    Waterman, M.R.8    Lamb, D.C.9    Guengerich, F.P.10
  • 8
    • 33747065060 scopus 로고    scopus 로고
    • Novel lipids in Myxococcus xanthus and their role in chemotaxis
    • P.D. Curtis, R. Geyer, D.C. White, and L.J. Shimkets Novel lipids in Myxococcus xanthus and their role in chemotaxis Environ. Microbiol. 8 2006 1935 1949
    • (2006) Environ. Microbiol. , vol.8 , pp. 1935-1949
    • Curtis, P.D.1    Geyer, R.2    White, D.C.3    Shimkets, L.J.4
  • 10
    • 0017302087 scopus 로고
    • Oxidized cytochrome P-450. Magnetic circular dichroism evidence for thiolate ligation in the substrate-bound form. Implications for the catalytic mechanism
    • J.H. Dawson, R.H. Holm, J.R. Trudell, G. Barth, R.E. Linder, E. Bunnenberg, C. Djerassi, and S.C. Tang Oxidized cytochrome P-450. Magnetic circular dichroism evidence for thiolate ligation in the substrate-bound form. Implications for the catalytic mechanism J. Am. Chem. Soc. 98 1976 3707 3708
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 3707-3708
    • Dawson, J.H.1    Holm, R.H.2    Trudell, J.R.3    Barth, G.4    Linder, R.E.5    Bunnenberg, E.6    Djerassi, C.7    Tang, S.C.8
  • 12
    • 70349648642 scopus 로고    scopus 로고
    • CYP704B1 is a long-chain fatty acid {omega}-hydroxylase essential for sporopollenin synthesis in pollen of arabidopsis
    • A.A. Dobritsa, J. Shrestha, M. Morant, F. Pinot, M. Matsuno, R. Swanson, B.L. Møller, and D. Preuss CYP704B1 is a long-chain fatty acid {omega}-hydroxylase essential for sporopollenin synthesis in pollen of arabidopsis Plant Physiol. 151 2009 574 589
    • (2009) Plant Physiol. , vol.151 , pp. 574-589
    • Dobritsa, A.A.1    Shrestha, J.2    Morant, M.3    Pinot, F.4    Matsuno, M.5    Swanson, R.6    Møller, B.L.7    Preuss, D.8
  • 13
    • 0030696965 scopus 로고    scopus 로고
    • Fatty acid signals in Bacillus megaterium are attenuated by cytochrome P-450-mediated hydroxylation
    • N. English, C.N.A. Palmer, W.L. Alworth, L. Kang, V. Hughes, and C.R. Wolf Fatty acid signals in Bacillus megaterium are attenuated by cytochrome P-450-mediated hydroxylation Biochem. J. 327 1997 363 368
    • (1997) Biochem. J. , vol.327 , pp. 363-368
    • English, N.1    Palmer, C.N.A.2    Alworth, W.L.3    Kang, L.4    Hughes, V.5    Wolf, C.R.6
  • 14
    • 0345275779 scopus 로고    scopus 로고
    • A passion for P450s (remembrances of the early history of research on cytochrome P450)
    • R.W. Estabrook A passion for P450s (remembrances of the early history of research on cytochrome P450) Drug Metab. Dispos. 31 2003 1461 1473
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 1461-1473
    • Estabrook, R.W.1
  • 15
    • 70350417516 scopus 로고    scopus 로고
    • Genome mining in Sorangium Cellulosum so ce56: Identification and characterization of the homologous electron transfer proteins of a myxobacterial cytochrome P450
    • K.M. Ewen, F. Hannemann, Y. Khatri, O. Perlova, R. Kappl, D. Krug, J. Hüttermann, R. Müller, and R. Bernhardt Genome mining in Sorangium Cellulosum So ce56: identification and characterization of the homologous electron transfer proteins of a myxobacterial cytochrome P450 J. Biol. Chem. 284 2009 28590 28598
    • (2009) J. Biol. Chem. , vol.284 , pp. 28590-28598
    • Ewen, K.M.1    Hannemann, F.2    Khatri, Y.3    Perlova, O.4    Kappl, R.5    Krug, D.6    Hüttermann, J.7    Müller, R.8    Bernhardt, R.9
  • 16
    • 0142164488 scopus 로고    scopus 로고
    • Myxobacteria: Proficient producers of novel natural products with various biological activities-past and future biotechnological aspects with the focus on the genus Sorangium
    • K. Gerth, S. Pradella, O. Perlova, S. Beyer, and R. Müller Myxobacteria: proficient producers of novel natural products with various biological activities-past and future biotechnological aspects with the focus on the genus Sorangium J. Biotechnol. 106 2003 233 253
    • (2003) J. Biotechnol. , vol.106 , pp. 233-253
    • Gerth, K.1    Pradella, S.2    Perlova, O.3    Beyer, S.4    Müller, R.5
  • 18
    • 34548071718 scopus 로고    scopus 로고
    • Cytochrome P450 monooxygenase from Clostridium acetobutylicum: A new alpha-fatty acid hydroxylase
    • M. Girhard, S. Schuster, M. Dietrich, P. Dürre, and V.B. Urlacher Cytochrome P450 monooxygenase from Clostridium acetobutylicum: a new alpha-fatty acid hydroxylase Biochem. Biophys. Res. Commun. 362 2007 114 119
    • (2007) Biochem. Biophys. Res. Commun. , vol.362 , pp. 114-119
    • Girhard, M.1    Schuster, S.2    Dietrich, M.3    Dürre, P.4    Urlacher, V.B.5
  • 19
    • 0032541989 scopus 로고    scopus 로고
    • Macrolide biosynthesis: A single cytochrome P450, PicK, is responsible for the hydroxylations that generate methymycin, neomethymycin, and picromycin in Streptomyces venezuelae
    • E.I. Graziani, D.E. Cane, M.C. Betlach, J.T. Kealey, and R. McDaniel Macrolide biosynthesis: A single cytochrome P450, PicK, is responsible for the hydroxylations that generate methymycin, neomethymycin, and picromycin in Streptomyces venezuelae Bioorg. Med. Chem. Lett. 8 1998 3117 3120
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 3117-3120
    • Graziani, E.I.1    Cane, D.E.2    Betlach, M.C.3    Kealey, J.T.4    McDaniel, R.5
  • 22
    • 33846473252 scopus 로고    scopus 로고
    • Cytochrome P450 systems-biological variations of electron transport chains
    • F. Hannemann, A. Bichet, K.M. Ewen, and R. Bernhardt Cytochrome P450 systems-biological variations of electron transport chains Biochim. Biophys. Acta 1770 2007 330 344
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 330-344
    • Hannemann, F.1    Bichet, A.2    Ewen, K.M.3    Bernhardt, R.4
  • 23
    • 33744821345 scopus 로고    scopus 로고
    • Design of an Escherichia coli system for whole cell mediated steroid synthesis and molecular evolution of steroid hydroxylases
    • F. Hannemann, C. Virus, and R. Bernhardt Design of an Escherichia coli system for whole cell mediated steroid synthesis and molecular evolution of steroid hydroxylases J. Biotechnol. 124 2006 172 181
    • (2006) J. Biotechnol. , vol.124 , pp. 172-181
    • Hannemann, F.1    Virus, C.2    Bernhardt, R.3
  • 24
    • 0029643786 scopus 로고
    • Structure and function of cytochromes P450: A comparative analysis of three crystal structures
    • C.A. Hasemann, R.G. Kurumbail, S.S. Boddupalli, J.A. Peterson, and J. Deisenhofer Structure and function of cytochromes P450: a comparative analysis of three crystal structures Structure 3 1995 41 62
    • (1995) Structure , vol.3 , pp. 41-62
    • Hasemann, C.A.1    Kurumbail, R.G.2    Boddupalli, S.S.3    Peterson, J.A.4    Deisenhofer, J.5
  • 25
    • 73949144656 scopus 로고    scopus 로고
    • Biochemical and structural characterization of CYP124: A methyl-branched lipid omega-hydroxylase from Mycobacterium tuberculosis
    • J.B. Johnston, P.M. Kells, L.M. Podust, and P.R. Ortiz de Montellano Biochemical and structural characterization of CYP124: a methyl-branched lipid omega-hydroxylase from Mycobacterium tuberculosis Proc. Natl. Acad. Sci. USA 106 2009 20687 20692
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20687-20692
    • Johnston, J.B.1    Kells, P.M.2    Podust, L.M.3    Ortiz De Montellano, P.R.4
  • 26
    • 1142267977 scopus 로고    scopus 로고
    • Coupling cell movement to multicellular development in myxobacteria
    • D. Kaiser Coupling cell movement to multicellular development in myxobacteria Nat. Rev. Microbiol. 1 2003 45 54
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 45-54
    • Kaiser, D.1
  • 27
    • 0025890074 scopus 로고
    • Iso- and anteiso-fatty acids in bacteria: Biosynthesis, function and taxonomic significance
    • T. Kaneda Iso- and anteiso-fatty acids in bacteria: biosynthesis, function and taxonomic significance Microbiol. Rev. 55 1991 288 302
    • (1991) Microbiol. Rev. , vol.55 , pp. 288-302
    • Kaneda, T.1
  • 28
    • 0036236942 scopus 로고    scopus 로고
    • Kinetic analysis of hydroxylation of saturated fatty acids by recombinant P450foxy produced by an Escherichia coli expression system
    • T. Kitazume, A. Tanaka, N. Takaya, A. Nakamura, S. Matsuyama, T. Suzuki, and H. Shoun Kinetic analysis of hydroxylation of saturated fatty acids by recombinant P450foxy produced by an Escherichia coli expression system Eur. J. Biochem. 269 2002 2075 2082
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2075-2082
    • Kitazume, T.1    Tanaka, A.2    Takaya, N.3    Nakamura, A.4    Matsuyama, S.5    Suzuki, T.6    Shoun, H.7
  • 29
    • 0037157130 scopus 로고    scopus 로고
    • Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119
    • L.S. Koo, C.E. Immoos, M.S. Cohen, P.J. Farmer, and P.R. Ortiz de Montellano Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119 J. Am. Chem. Soc. 124 2002 5684 5691
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5684-5691
    • Koo, L.S.1    Immoos, C.E.2    Cohen, M.S.3    Farmer, P.J.4    Ortiz De Montellano, P.R.5
  • 31
    • 0014670327 scopus 로고
    • Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds, and endogenous substrates
    • A.Y.H. Lu, K.W. Junk, and M.J. Coon Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds, and endogenous substrates J. Biol. Chem. 244 1969 3714 3721
    • (1969) J. Biol. Chem. , vol.244 , pp. 3714-3721
    • Lu, A.Y.H.1    Junk, K.W.2    Coon, M.J.3
  • 32
    • 0024832753 scopus 로고
    • A conserved residue of cytochrome P-450 is involved in heme-oxygen stability and activation
    • S.A. Martinis, W.M. Atkins, P.S. Stayton, and S. Sligar A conserved residue of cytochrome P-450 is involved in heme-oxygen stability and activation J. Am. Chem. Soc. 111 1989 9252 9253
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 9252-9253
    • Martinis, S.A.1    Atkins, W.M.2    Stayton, P.S.3    Sligar, S.4
  • 33
    • 0026452788 scopus 로고
    • Domains of the catalytically self-sufficient cytochrome P-450 BM-3. Genetic construction, overexpression, purification and spectroscopic characterization
    • J.S. Miles, A.W. Munro, B.N. Rospendowski, W.E. Smith, J. McKnight, and A.J. Thomson Domains of the catalytically self-sufficient cytochrome P-450 BM-3. Genetic construction, overexpression, purification and spectroscopic characterization Biochem. J. 288 1992 503 509
    • (1992) Biochem. J. , vol.288 , pp. 503-509
    • Miles, J.S.1    Munro, A.W.2    Rospendowski, B.N.3    Smith, W.E.4    McKnight, J.5    Thomson, A.J.6
  • 37
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • T. Omura, and R. Sato The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature J. Biol. Chem. 239 1964 2370 2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 39
    • 0030203863 scopus 로고    scopus 로고
    • Tree View: An application to display phylogenetic trees on personal computers
    • R.D.M. Page Tree View: An application to display phylogenetic trees on personal computers Comput. Appl. Biosci. 12 1996 357 358
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.M.1
  • 40
    • 29844452482 scopus 로고    scopus 로고
    • Identification and analysis of the chivosazol biosynthetic gene cluster from the myxobacterial model strain Sorangium cellulosum so ce56
    • O. Perlova, K. Gerth, O. Kaiser, A. Hans, and R. Müller Identification and analysis of the chivosazol biosynthetic gene cluster from the myxobacterial model strain Sorangium cellulosum So ce56 J. Biotechnol. 121 2006 174 191
    • (2006) J. Biotechnol. , vol.121 , pp. 174-191
    • Perlova, O.1    Gerth, K.2    Kaiser, O.3    Hans, A.4    Müller, R.5
  • 41
    • 0024722728 scopus 로고
    • Topological distribution of four-alpha-helix bundles
    • S.R. Presnell, and F.E. Cohen Topological distribution of four-alpha-helix bundles Proc. Natl. Acad. Sci. USA 86 1989 6592 6596
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6592-6596
    • Presnell, S.R.1    Cohen, F.E.2
  • 42
    • 67149127757 scopus 로고    scopus 로고
    • Biosynthesis of 2-hydroxy and iso-even fatty acids is connected to sphingolipid formation in myxobacteria
    • M.W. Ring, G. Schwär, and H.B. Bode Biosynthesis of 2-hydroxy and iso-even fatty acids is connected to sphingolipid formation in myxobacteria ChemBioChem 10 2009 2003 2010
    • (2009) ChemBioChem , vol.10 , pp. 2003-2010
    • Ring, M.W.1    Schwär, G.2    Bode, H.B.3
  • 45
    • 0027788060 scopus 로고
    • Cytochrome P450BM-3 (CYP102): Regiospecificity of oxidation of omega-unsaturated fatty acids and mechanism-based inactivation
    • N. Shirane, Z. Sui, J.A. Peterson, and P.R. Ortiz de Montellano Cytochrome P450BM-3 (CYP102): regiospecificity of oxidation of omega-unsaturated fatty acids and mechanism-based inactivation Biochemistry 32 1993 13732 13741
    • (1993) Biochemistry , vol.32 , pp. 13732-13741
    • Shirane, N.1    Sui, Z.2    Peterson, J.A.3    Ortiz De Montellano, P.R.4
  • 46
    • 0034708263 scopus 로고    scopus 로고
    • Substrate binding to 15beta-hydroxylase (CYP106A2) probed by FT infrared spectroscopic studies of the iron ligand CO stretch vibration
    • B. Simgen, J. Contzen, R. Schwarzer, R. Bernhardt, and C. Jung Substrate binding to 15beta-hydroxylase (CYP106A2) probed by FT infrared spectroscopic studies of the iron ligand CO stretch vibration Biochem. Biophys. Res. Commun. 269 2000 737 742
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 737-742
    • Simgen, B.1    Contzen, J.2    Schwarzer, R.3    Bernhardt, R.4    Jung, C.5
  • 47
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibriums in cytochrome P450
    • S.G. Sligar Coupling of spin, substrate, and redox equilibriums in cytochrome P450 Biochemistry 15 1976 5399 5406
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 48
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 49
    • 18044364585 scopus 로고    scopus 로고
    • Alkane-induced expression, substrate binding profile, and immunolocalization of a cytochrome P450 encoded on the nifD excision element of Anabaena 7120
    • S. Torres, C. Fjetland, and P. Lammers Alkane-induced expression, substrate binding profile, and immunolocalization of a cytochrome P450 encoded on the nifD excision element of Anabaena 7120 BMC Microbiol. 5 2005 16
    • (2005) BMC Microbiol. , vol.5 , pp. 16
    • Torres, S.1    Fjetland, C.2    Lammers, P.3
  • 50
    • 0032500154 scopus 로고    scopus 로고
    • Identification and sequencing of a cytochrome-P450 gene-cluster from Bradyrhizobium-japonicum
    • R.E. Tully, P. Vanberkum, K.W. Lovins, and D.L. Keister Identification and sequencing of a cytochrome-P450 gene-cluster from Bradyrhizobium-japonicum Biochim. Biophys. Acta 1398 1998 243 255
    • (1998) Biochim. Biophys. Acta , vol.1398 , pp. 243-255
    • Tully, R.E.1    Vanberkum, P.2    Lovins, K.W.3    Keister, D.L.4
  • 51
    • 0027979002 scopus 로고
    • C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450
    • H. Uhlmann, R. Kraft, and R. Bernhardt C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450 J. Biol. Chem. 269 1994 22557 22564
    • (1994) J. Biol. Chem. , vol.269 , pp. 22557-22564
    • Uhlmann, H.1    Kraft, R.2    Bernhardt, R.3
  • 52
    • 0032581042 scopus 로고    scopus 로고
    • Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect
    • M. Vidakovic, S.G. Sligar, H. Li, and T.L. Poulos Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect Biochemistry 37 1998 9211 9219
    • (1998) Biochemistry , vol.37 , pp. 9211-9219
    • Vidakovic, M.1    Sligar, S.G.2    Li, H.3    Poulos, T.L.4
  • 53
    • 57149131662 scopus 로고    scopus 로고
    • Molecular evolution of a steroid hydroxylating cytochrome P450 using a versatile steroid detection system for screening
    • C. Virus, and R. Bernhardt Molecular evolution of a steroid hydroxylating cytochrome P450 using a versatile steroid detection system for screening Lipids 43 2008 1133 1141
    • (2008) Lipids , vol.43 , pp. 1133-1141
    • Virus, C.1    Bernhardt, R.2
  • 54
    • 0015642684 scopus 로고
    • Fatty acids of Myxococcus xanthus
    • J.C. Ware, and M. Dworkin Fatty acids of Myxococcus xanthus J. Bacteriol. 115 1973 253 261
    • (1973) J. Bacteriol. , vol.115 , pp. 253-261
    • Ware, J.C.1    Dworkin, M.2
  • 55
    • 36348982083 scopus 로고    scopus 로고
    • Myxobacterial natural product assembly lines: Fascinating examples of curious biochemistry
    • S.C. Wenzel, and R. Müller Myxobacterial natural product assembly lines: fascinating examples of curious biochemistry Nat. Prod. Rep. 24 2007 1211 1224
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 1211-1224
    • Wenzel, S.C.1    Müller, R.2
  • 56
    • 65949116191 scopus 로고    scopus 로고
    • Myxobactria - 'microbial factories' for the production of bioactive secondary metabolites
    • C.S. Wenzel, and R. Müller Myxobactria - 'microbial factories' for the production of bioactive secondary metabolites Mol. Biosyst. 5 2009 567 574
    • (2009) Mol. Biosyst. , vol.5 , pp. 567-574
    • Wenzel, C.S.1    Müller, R.2
  • 58
    • 0034995739 scopus 로고    scopus 로고
    • The effect of water on the ion trap analysis of trimethylsilyl derivatives of long-chain fatty acids and alcohols
    • K.V. Wood, C.C. Bonham, and M.A. Jenks The effect of water on the ion trap analysis of trimethylsilyl derivatives of long-chain fatty acids and alcohols Rapid Commun. Mass Spectrom. 15 2001 873 877
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 873-877
    • Wood, K.V.1    Bonham, C.C.2    Jenks, M.A.3
  • 59
    • 43749088055 scopus 로고    scopus 로고
    • Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2)
    • B. Zhao, X. Lin, L. Lei, D.C. Lamb, S.L. Kelly, M.R. Waterman, and D.E. Cane Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2) J. Biol. Chem. 283 2008 8183 8189
    • (2008) J. Biol. Chem. , vol.283 , pp. 8183-8189
    • Zhao, B.1    Lin, X.2    Lei, L.3    Lamb, D.C.4    Kelly, S.L.5    Waterman, M.R.6    Cane, D.E.7


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