메뉴 건너뛰기




Volumn 287, Issue 46, 2012, Pages 39125-39138

Bacterial biosynthetic gene clusters encoding the anti-cancer haterumalide class of molecules: Biogenesis of the broad spectrum antifungal and anti-oomycete compound, oocydin A

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ANTI-FUNGAL; ANTITUMOR PROPERTY; BIOLOGICAL PROPERTIES; BIOSYNTHETIC GENE CLUSTER; BROAD SPECTRUM; CHEMICAL SYNTHESIS; COMPARATIVE GENOMICS; ENTEROBACTERIA; FLAVIN-DEPENDENT; GENE CLUSTERS; GENOME SEQUENCING; HYDROXYMETHYLGLUTARYL; IN-SILICO; MACROLIDES; MULTI-MODULAR; OOMYCETES; PATHOGENIC FUNGI; POLYKETIDE SYNTHASES; SERRATIA; SYNTHASES; SYNTHETIC ROUTES;

EID: 84869054540     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.401026     Document Type: Article
Times cited : (68)

References (84)
  • 3
    • 70349551727 scopus 로고    scopus 로고
    • Plant growth-promoting rhizobacteria
    • Lugtenberg, B., and Kamilova, F. (2009) Plant growth-promoting rhizobacteria. Annu. Rev. Microbiol. 63, 541-556
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 541-556
    • Lugtenberg, B.1    Kamilova, F.2
  • 5
    • 0033371299 scopus 로고    scopus 로고
    • Oocydin A, a chlorinated macrocyclic lactone with potent anti-oomycete activity from Serratia marcescens
    • Srobel, G., Li, J. Y., Sugawara, F., Koshino, H., Harper, J., and Hess, W. M. (1999) Oocydin A, a chlorinated macrocyclic lactone with potent anti-oomycete activity from Serratia marcescens. Microbiology 145, 3557-3564 (Pubitemid 30018799)
    • (1999) Microbiology , vol.145 , Issue.12 , pp. 3557-3564
    • Strobel, G.1    Li, J.-Y.2    Sugawara, F.3    Koshino, H.4    Harper, J.5    Hess, W.M.6
  • 6
    • 0033588149 scopus 로고    scopus 로고
    • Isolation and structures of haterumalides NA, NB, NC, ND, and NE, novel macrolides from an Okinawan sponge Ircinia sp.
    • DOI 10.1016/S0040-4039(99)01291-5, PII S0040403999012915
    • Takada, N., Sato, H., Suenaga, K., Arimoto, H., Yamada, K., Ueda, K., and Uemura, D. (1999) Isolation and structures of haterumalides NA, NB, NC, ND, and NE, novel macrolides from an Okinawan sponge Ircinia sp. Tetrahedron Lett. 40, 6309-6312 (Pubitemid 29378437)
    • (1999) Tetrahedron Letters , vol.40 , Issue.34 , pp. 6309-6312
    • Takada, N.1    Sato, H.2    Suenaga, K.3    Arimoto, H.4    Yamada, K.5    Ueda, K.6    Uemura, D.7
  • 7
    • 0034798256 scopus 로고    scopus 로고
    • Suppression of Sclerotinia sclerotiorum apothecial formation by the soil bacterium Serratia plymuthica: Identification of a chlorinated macrolide as one of the causal agents
    • DOI 10.1016/S0038-0717(01)00109-2, PII S0038071701001092
    • Thaning, C., Welch, C. J., Borowicz, J. J., Hedman, R., and Gerhardson, B. (2001) Suppression of Sclerotinia sclerotiorum apothecial formation by the soil bacterium Serratia plymuthica. Identification of a chlorinated macrolide as one of the causal agents. Soil Biol. Biochem. 33, 1817-1826 (Pubitemid 32961532)
    • (2001) Soil Biology and Biochemistry , vol.33 , Issue.12-13 , pp. 1817-1826
    • Thaning, C.1    Welch, C.J.2    Borowicz, J.J.3    Hedman, R.4    Gerhardson, B.5
  • 8
    • 28244486142 scopus 로고    scopus 로고
    • FR177391, a new anti-hyperlipidemic agent from Serratia: I. Taxonomy, fermentation, isolation, physico-chemical properties, structure elucidation and biological activities
    • Sato, B., Nakajima, H., Fujita, T., Takase, S., Yoshimura, S., Kinoshita, T., and Terano, H. (2005) FR177391, a new anti-hyperlipidemic agent from Serratia. I. Taxonomy, fermentation, isolation, physico-chemical properties, structure elucidation, and biological activities. J. Antibiot. 58, 634-639 (Pubitemid 41703746)
    • (2005) Journal of Antibiotics , vol.58 , Issue.10 , pp. 634-639
    • Sato, B.1    Nakajima, H.2    Fujita, T.3    Takase, S.4    Yoshimura, S.5    Kinoshita, T.6    Terano, H.7
  • 9
    • 66449122214 scopus 로고    scopus 로고
    • Total synthesis and cytotoxicity of haterumalides NA and B and their artificial analogs
    • Ueda, M., Yamaura, M., Ikeda, Y., Suzuki, Y., Yoshizato, K., Hayakawa, I., and Kigoshi, H. (2009) Total synthesis and cytotoxicity of haterumalides NA and B and their artificial analogs. J. Org. Chem. 74, 3370-3377
    • (2009) J. Org. Chem. , vol.74 , pp. 3370-3377
    • Ueda, M.1    Yamaura, M.2    Ikeda, Y.3    Suzuki, Y.4    Yoshizato, K.5    Hayakawa, I.6    Kigoshi, H.7
  • 10
    • 9344256043 scopus 로고    scopus 로고
    • Biselides A and B, novel macrolides from the okinawan ascidian didemnidae sp.
    • DOI 10.1246/cl.2004.1184
    • Teruya, T., Shimogawa, H., Suenaga K., and Kigoshi, H. (2004) Biselides A and B, novel macrolides from the Okinawan ascidian Didemnidae sp. Chem. Lett. 33, 1184-1185 (Pubitemid 39556105)
    • (2004) Chemistry Letters , vol.33 , Issue.9 , pp. 1184-1185
    • Teruya, T.1    Shimogawa, H.2    Suenaga, K.3    Kigoshi, H.4
  • 11
    • 20444502594 scopus 로고    scopus 로고
    • Biselides A-E: Novel polyketides from the Okinawan ascidian Didemnidae sp.
    • DOI 10.1016/j.tet.2005.04.052, PII S0040402005007349
    • Teruya, T., Suenaga, K., Maruyama, S., Kurotaki, M., and Kigoshi, H. (2005) Biselides A-E. Novel polyketides from the Okinawan ascidian Didemnidae sp. Tetrahedron 61, 6561-6567 (Pubitemid 40812957)
    • (2005) Tetrahedron , vol.61 , Issue.27 , pp. 6561-6567
    • Teruya, T.1    Suenaga, K.2    Maruyama, S.3    Kurotaki, M.4    Kigoshi, H.5
  • 12
    • 0141739284 scopus 로고    scopus 로고
    • Enantioselective synthesis of 15-epi-haterumalide NA methyl ester and revised structure of haterumalide NA
    • DOI 10.1021/ol0341804
    • Kigoshi, H., Kita, M., Ogawa, S., Itoh, M., and Uemura, D. (2003) Enantioselective synthesis of 15-epi-haterumalide NA methyl ester and revised structure of haterumalide NA. Org. Lett. 5, 957-960 (Pubitemid 37130659)
    • (2003) Organic Letters , vol.5 , Issue.6 , pp. 957-960
    • Kigoshi, H.1    Kita, M.2    Ogawa, S.3    Itoh, M.4    Uemura, D.5
  • 13
    • 18744411523 scopus 로고    scopus 로고
    • Alkyne haloallylation [with Pd(II)] as a core strategy for macrocycle synthesis: A total synthesis of (-)-haterumalide NA/(-)-oocydin A
    • DOI 10.1021/ja051749i
    • Hoye, T. R., and Wang, J. (2005) Alkyne haloallylation (with Pd(II)) as a core strategy for macrocycle synthesis. A total synthesis of (-)-haterumalide NA/(-)-oocydin A. J. Am. Chem. Soc. 127, 6950-6951 (Pubitemid 40676713)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.19 , pp. 6950-6951
    • Hoye, T.R.1    Wang, J.2
  • 14
    • 48249137414 scopus 로고    scopus 로고
    • Total biosynthesis. In vitro reconstitution of polyketide and nonribosomal peptide pathways
    • Sattely, E. S., Fischbach, M. A., and Walsh, C. T. (2008) Total biosynthesis. In vitro reconstitution of polyketide and nonribosomal peptide pathways. Nat. Prod. Rep. 25, 757-793
    • (2008) Nat. Prod. Rep. , vol.25 , pp. 757-793
    • Sattely, E.S.1    Fischbach, M.A.2    Walsh, C.T.3
  • 15
    • 39149099787 scopus 로고    scopus 로고
    • Halogenation Strategies In Natural Product Biosynthesis
    • DOI 10.1016/j.chembiol.2008.01.006, PII S1074552108000409
    • Neumann, C. S., Fujimori, D. G., and Walsh, C. T. (2008) Halogenation strategies in natural product biosynthesis. Chem. Biol. 15, 99-109 (Pubitemid 351253619)
    • (2008) Chemistry and Biology , vol.15 , Issue.2 , pp. 99-109
    • Neumann, C.S.1    Fujimori, D.G.2    Walsh, C.T.3
  • 16
    • 69249202590 scopus 로고    scopus 로고
    • The biosynthetic logic of polyketide diversity
    • Hertweck, C. (2009) The biosynthetic logic of polyketide diversity. Angew. Chem. Int. Ed. Engl. 48, 4688-4716
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 4688-4716
    • Hertweck, C.1
  • 17
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: Logic machinery, and mechanisms
    • DOI 10.1021/cr0503097
    • Fischbach, M. A., and Walsh, C. T. (2006) Assembly line enzymology for polyketide and nonribosomal peptide antibiotics. Logic, machinery, and mechanisms. Chem. Rev. 106, 3468-3496 (Pubitemid 44376945)
    • (2006) Chemical Reviews , vol.106 , Issue.8 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 19
    • 0025047590 scopus 로고
    • Transposon vectors containing non-antibiotic resistance selection markers for cloning and stable chromosomal insertion of foreign genes in gram-negative bacteria
    • Herrero, M., de Lorenzo, V., and Timmis, K. N. (1990) Transposon vectors containing nonantibiotic resistance selection markers for cloning and stable chromosomal insertion of foreign genes in Gram-negative bacteria. J. Bacteriol. 172, 6557-6567 (Pubitemid 20372801)
    • (1990) Journal of Bacteriology , vol.172 , Issue.11 , pp. 6557-6567
    • Herrero, M.1    De Lorenzo, V.2    Timmis, K.N.3
  • 20
    • 0025837193 scopus 로고
    • A wide-host range suicide vector for improving reverse genetics in Gram-negative bacteria. Inactivation of the blaA gene of Yersinia enterocolitica
    • Kaniga, K., Delor, I., and Cornelis, G. R. (1991) A wide-host range suicide vector for improving reverse genetics in Gram-negative bacteria. Inactivation of the blaA gene of Yersinia enterocolitica. Gene 109, 137-141
    • (1991) Gene , vol.109 , pp. 137-141
    • Kaniga, K.1    Delor, I.2    Cornelis, G.R.3
  • 21
    • 14644386907 scopus 로고    scopus 로고
    • A new family of mobilizable suicide plasmids based on broad host range R388 plasmid (IncW) and RP4 plasmid (IncPα) conjugative machineries and their cognate Escherichia coli host strains
    • DOI 10.1016/j.resmic.2004.09.007
    • Demarre, G., Guérout, A. M., Matsumoto-Mashimo, C., Rowe-Magnus, D. A., Marlière, P., and Mazel, D. (2005) A new family of mobilizable suicide plasmids based on broad host range R388 plasmid (IncW) and RP4 plasmid (IncPalpha) conjugative machineries and their cognate Escherichia coli host strains. Res. Microbiol. 156, 245-255 (Pubitemid 40320963)
    • (2005) Research in Microbiology , vol.156 , Issue.2 , pp. 245-255
    • Demarre, G.1    Guerout, A.-M.2    Matsumoto-Mashimo, C.3    Rowe-Magnus, D.A.4    Marliere, P.5    Mazel, D.6
  • 23
    • 0030617530 scopus 로고    scopus 로고
    • Biological control of cereal seed-borne diseases by seed bacterization with greenhouse-selected bacteria
    • Hökeberg, M., Gerhardson, B., and Johnsson, L. (1997) Biological control of cereal seed-borne diseases by seed bacterization with greenhouse-selected bacteria. Eur. J. Plant Pathol. 103, 25-33
    • (1997) Eur. J. Plant Pathol. , vol.103 , pp. 25-33
    • Hökeberg, M.1    Gerhardson, B.2    Johnsson, L.3
  • 24
    • 0036306048 scopus 로고    scopus 로고
    • Plant-dependent genotypic and phenotypic diversity of antagonistic rhizobacteria isolated from different Verticillium host plants
    • DOI 10.1128/AEM.68.7.3328-3338.2002
    • Berg, G., Roskot, N., Steidle, A., Eberl, L., Zock, A., and Smalla, K. (2002) Plant-dependent genotypic and phenotypic diversity of antagonistic rhizobacteria isolated from different Verticillium host plants. Appl. Environ. Microbiol. 68, 3328-3338 (Pubitemid 34734028)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.7 , pp. 3328-3338
    • Berg, G.1    Roskot, N.2    Steidle, A.3    Eberl, L.4    Zock, A.5    Smalla, K.6
  • 25
    • 0031869639 scopus 로고    scopus 로고
    • Plasposons: Modular self-cloning minitransposon derivatives for rapid genetic analysis of gram-negative bacterial genomes
    • Dennis, J. J., and Zylstra, G. J. (1998) Plasposons. Modular self-cloning minitransposon derivatives for rapid genetic analysis of Gram-negative bacterial genomes. Appl. Environ. Microbiol. 64, 2710-2715 (Pubitemid 28303324)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.7 , pp. 2710-2715
    • Dennis, J.J.1    Zylstra, G.J.2
  • 27
    • 0020622171 scopus 로고
    • A broad host range cloning vector transposable to various replicons
    • Grinter, N. J. (1983) A broad host range cloning vector transposable to various replicons. Gene 21, 133-143
    • (1983) Gene , vol.21 , pp. 133-143
    • Grinter, N.J.1
  • 30
    • 79959920872 scopus 로고    scopus 로고
    • Anti-SMASH. Rapid identification, annotation, and analysis of secondary metabolite biosynthesis gene clusters in bacterial and fungal genome sequences
    • Medema, M. H., Blin, K., Cimermancic, P., de Jager, V., Zakrzewski, P., Fischbach, M. A., Weber, T., Takano, E., and Breitling, R. (2011) anti-SMASH. Rapid identification, annotation, and analysis of secondary metabolite biosynthesis gene clusters in bacterial and fungal genome sequences. Nucleic Acids Res. 39, W339-W346
    • (2011) Nucleic Acids Res. , vol.39
    • Medema, M.H.1    Blin, K.2    Cimermancic, P.3    De Jager, V.4    Zakrzewski, P.5    Fischbach, M.A.6    Weber, T.7    Takano, E.8    Breitling, R.9
  • 31
  • 35
    • 29244449352 scopus 로고    scopus 로고
    • A GntR family transcriptional regulator (PigT) controls gluconate-mediated repression and defines a new, independent pathway for regulation of the tripyrrole antibiotic, prodigiosin, in Serratia
    • DOI 10.1099/mic.0.28251-0
    • Fineran, P. C., Everson, L., Slater, H., and Salmond, G. P. (2005) A GntR family transcriptional regulator (PigT) controls gluconate-mediated repression and defines a new, independent pathway for regulation of the tripyrrole antibiotic, prodigiosin, in Serratia. Microbiology 151, 3833-3845 (Pubitemid 41829965)
    • (2005) Microbiology , vol.151 , Issue.12 , pp. 3833-3845
    • Fineran, P.C.1    Everson, L.2    Slater, H.3    Salmond, G.P.C.4
  • 36
    • 33746049442 scopus 로고    scopus 로고
    • Metabolic and regulatory engineering of Serratia marcescens: Mimicking phage-mediated horizontal acquisition of antibiotic biosynthesis and quorum-sensing capacities
    • DOI 10.1099/mic.0.28803-0
    • Coulthurst, S. J., Williamson, N. R., Harris, A. K., Spring, D. R., and Salmond, G. P. (2006) Metabolic and regulatory engineering of Serratia marcescens: mimicking phage-mediated horizontal acquisition of antibiotic biosynthesis and quorum-sensing capacities. Microbiology 152, 1899-1911 (Pubitemid 44070448)
    • (2006) Microbiology , vol.152 , Issue.7 , pp. 1899-1911
    • Coulhurst, S.J.1    Williamson, N.R.2    Harris, A.K.P.3    Spring, D.R.4    Salmond, G.P.C.5
  • 37
    • 0037244560 scopus 로고    scopus 로고
    • Phosphate availability regulates biosynthesis of two antibiotics, prodigiosin and carbapenem, in Serratia via both quorum-sensing-dependent and -independent pathways
    • DOI 10.1046/j.1365-2958.2003.03295.x
    • Slater, H., Crow, M., Everson, L., and Salmond, G. P. (2003) Phosphate availability regulates biosynthesis of two antibiotics, prodigiosin and carbapenem, in Serratia via both quorum-sensing-dependent and -independent pathways. Mol. Microbiol. 47, 303-320 (Pubitemid 36121023)
    • (2003) Molecular Microbiology , vol.47 , Issue.2 , pp. 303-320
    • Slater, H.1    Crow, M.2    Everson, L.3    Salmond, G.P.C.4
  • 39
    • 0031970701 scopus 로고    scopus 로고
    • Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: A genetic analysis
    • DOI 10.1046/j.1365-2958.1998.00797.x
    • O'Toole, G. A., and Kolter, R. (1998) Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signaling pathways. A genetic analysis. Mol. Microbiol. 28, 449-461 (Pubitemid 28218392)
    • (1998) Molecular Microbiology , vol.28 , Issue.3 , pp. 449-461
    • O'Toole, G.A.1    Kolter, R.2
  • 40
    • 49749108516 scopus 로고    scopus 로고
    • Halogenase genes in nonribosomal peptide synthetase gene clusters of Microcystis (cyanobacteria). Sporadic distribution and evolution
    • Cadel-Six, S., Dauga, C., Castets, A. M., Rippka, R., Bouchier, C., Tandeau de Marsac, N., and Welker, M. (2008) Halogenase genes in nonribosomal peptide synthetase gene clusters of Microcystis (cyanobacteria). Sporadic distribution and evolution. Mol. Biol. Evol. 25, 2031-2041
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 2031-2041
    • Cadel-Six, S.1    Dauga, C.2    Castets, A.M.3    Rippka, R.4    Bouchier, C.5    Tandeau De Marsac, N.6    Welker, M.7
  • 41
    • 77955814236 scopus 로고    scopus 로고
    • Microbisporicin gene cluster reveals unusual features of lantibiotic biosynthesis in actinomycetes
    • Foulston, L. C., and Bibb, M. J. (2010) Microbisporicin gene cluster reveals unusual features of lantibiotic biosynthesis in actinomycetes. Proc. Natl. Acad. Sci. U.S.A. 107, 13461-13466
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 13461-13466
    • Foulston, L.C.1    Bibb, M.J.2
  • 43
    • 50049117282 scopus 로고    scopus 로고
    • Genes for the biosynthesis of the fungal polyketides hypothemycin from Hypomyces subiculosus and radicicol from Pochonia chlamydosporia
    • Reeves, C. D., Hu, Z., Reid, R., and Kealey, J. T. (2008) Genes for the biosynthesis of the fungal polyketides hypothemycin from Hypomyces subiculosus and radicicol from Pochonia chlamydosporia. Appl. Environ. Microbiol. 74, 5121-5129
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 5121-5129
    • Reeves, C.D.1    Hu, Z.2    Reid, R.3    Kealey, J.T.4
  • 44
    • 79851495866 scopus 로고    scopus 로고
    • Characterization of tiacumicin B biosynthetic gene cluster affording diversified tiacumicin analogs and revealing a tailoring dihalogenase
    • Xiao, Y., Li, S., Niu, S., Ma, L., Zhang, G., Zhang, H., Zhang, G., Ju, J., and Zhang, C. (2011) Characterization of tiacumicin B biosynthetic gene cluster affording diversified tiacumicin analogs and revealing a tailoring dihalogenase. J. Am. Chem. Soc. 133, 1092-1105
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 1092-1105
    • Xiao, Y.1    Li, S.2    Niu, S.3    Ma, L.4    Zhang, G.5    Zhang, H.6    Zhang, G.7    Ju, J.8    Zhang, C.9
  • 45
    • 65349170600 scopus 로고    scopus 로고
    • Biohalogenation. Nature's way to synthesize halogenated metabolites
    • Wagner, C., El Omari, M., and König, G. M. (2009) Biohalogenation. Nature's way to synthesize halogenated metabolites. J. Nat. Prod. 72, 540-553
    • (2009) J. Nat. Prod. , vol.72 , pp. 540-553
    • Wagner, C.1    El Omari, M.2    König, G.M.3
  • 47
    • 9144222164 scopus 로고    scopus 로고
    • The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation
    • DOI 10.1099/mic.0.27222-0
    • Harris, A. K., Williamson, N. R., Slater, H., Cox, A., Abbasi, S., Foulds, I., Simonsen, H. T., Leeper, F. J., and Salmond, G. P. (2004) The Serratia gene cluster encoding biosynthesis of the red antibiotic, prodigiosin, shows species- and strain-dependent genome context variation. Microbiology 150, 3547-3560 (Pubitemid 39545305)
    • (2004) Microbiology , vol.150 , Issue.11 , pp. 3547-3560
    • Harris, A.K.P.1    Williamson, N.R.2    Slater, H.3    Cox, A.4    Abbasi, S.5    Foulds, I.6    Simonsen, H.T.7    Leeper, F.J.8    Salmond, G.P.C.9
  • 48
    • 80052601285 scopus 로고    scopus 로고
    • A quorum-sensing molecule acts as a morphogen controlling gas vesicle organelle biogenesis and adaptive flotation in an enterobacterium
    • Ramsay, J. P., Williamson, N. R., Spring, D. R., and Salmond, G. P. (2011) A quorum-sensing molecule acts as a morphogen controlling gas vesicle organelle biogenesis and adaptive flotation in an enterobacterium. Proc. Natl. Acad. Sci. U.S.A. 108, 14932-14937
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14932-14937
    • Ramsay, J.P.1    Williamson, N.R.2    Spring, D.R.3    Salmond, G.P.4
  • 49
    • 18444391489 scopus 로고    scopus 로고
    • Biosynthesis of the red antibiotic, prodigiosin, in Serratia: Identification of a novel 2-methyl-3-n-amyl-pyrroie (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces
    • DOI 10.1111/j.1365-2958.2005.04602.x
    • Williamson, N. R., Simonsen, H. T., Ahmed, R. A., Goldet, G., Slater, H., Woodley, L., Leeper, F. J., and Salmond, G. P. (2005) Biosynthesis of the red antibiotic, prodigiosin, in Serratia. Identification of a novel 2-methyl- 3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces. Mol. Microbiol. 56, 971-989 (Pubitemid 40646769)
    • (2005) Molecular Microbiology , vol.56 , Issue.4 , pp. 971-989
    • Williamson, N.R.1    Simonsen, H.T.2    Ahmed, R.A.A.3    Goldet, G.4    Slater, H.5    Woodley, L.6    Leeper, F.J.7    Salmond, G.P.C.8
  • 50
    • 77954675603 scopus 로고    scopus 로고
    • Biosynthesis of polyketides by trans-AT polyketide synthases
    • Piel, J. (2010) Biosynthesis of polyketides by trans-AT polyketide synthases. Nat. Prod. Rep. 27, 996-1047
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 996-1047
    • Piel, J.1
  • 51
    • 0037314870 scopus 로고    scopus 로고
    • Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP Transacylase
    • DOI 10.1016/S0969-2126(03)00004-2, PII S0969212603000042
    • Keatinge-Clay, A. T., Shelat, A. A., Savage, D. F., Tsai, S. C., Miercke, L. J., O'Connell, J. D., 3rd, Khosla, C., and Stroud, R. M. (2003) Catalysis, specificity, and ACP-docking site of Streptomyces coelicolor malonyl-CoA: ACP transacylase. Structure 11, 147-154 (Pubitemid 36187417)
    • (2003) Structure , vol.11 , Issue.2 , pp. 147-154
    • Keatinge-Clay, A.T.1    Shelat, A.A.2    Savage, D.F.3    Tsai, S.-C.4    Miercke, L.J.W.5    O'Connell III, J.D.6    Khosla, C.7    Stroud, R.M.8
  • 52
    • 0037466331 scopus 로고    scopus 로고
    • Computational approach for prediction of domain organization and substrate specificity of modular polyketide synthases
    • DOI 10.1016/S0022-2836(03)00232-8
    • Yadav, G., Gokhale, R. S., and Mohanty, D. (2003) Computational approach for prediction of domain organization and substrate specificity of modular polyketide synthases. J. Mol. Biol. 328, 335-363 (Pubitemid 36407579)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.2 , pp. 335-363
    • Yadav, G.1    Gokhale, R.S.2    Mohanty, D.3
  • 55
    • 78650012665 scopus 로고    scopus 로고
    • Genome mining reveals trans-AT polyketide synthase directed antibiotic biosynthesis in the bacterial phylum bacteroidetes
    • Teta, R., Gurgui, M., Helfrich, E. J., Künne, S., Schneider, A., Van Echten-Deckert, G., Mangoni, A., and Piel, J. (2010) Genome mining reveals trans-AT polyketide synthase directed antibiotic biosynthesis in the bacterial phylum bacteroidetes. ChemBioChem 11, 2506-2512
    • (2010) ChemBioChem , vol.11 , pp. 2506-2512
    • Teta, R.1    Gurgui, M.2    Helfrich, E.J.3    Künne, S.4    Schneider, A.5    Van Echten-Deckert, G.6    Mangoni, A.7    Piel, J.8
  • 56
    • 54849419509 scopus 로고    scopus 로고
    • Stereochemical determination and complex biosynthetic assembly of etnangien, a highly potent RNA polymerase inhibitor from the myxobacterium Sorangium cellulosum
    • Menche, D., Arikan, F., Perlova, O., Horstmann, N., Ahlbrecht, W., Wenzel, S. C., Jansen, R., Irschik, H., and Müller, R. (2008) Stereochemical determination and complex biosynthetic assembly of etnangien, a highly potent RNA polymerase inhibitor from the myxobacterium Sorangium cellulosum. J. Am. Chem. Soc. 130, 14234-14243
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14234-14243
    • Menche, D.1    Arikan, F.2    Perlova, O.3    Horstmann, N.4    Ahlbrecht, W.5    Wenzel, S.C.6    Jansen, R.7    Irschik, H.8    Müller, R.9
  • 57
    • 39149122159 scopus 로고    scopus 로고
    • Molecular Analysis of the Kirromycin Biosynthetic Gene Cluster Revealed β-Alanine as Precursor of the Pyridone Moiety
    • DOI 10.1016/j.chembiol.2007.12.009, PII S1074552108000021
    • Weber, T., Laiple, K. J., Pross, E. K., Textor, A., Grond, S., Welzel, K., Pelzer, S., Vente, A., and Wohlleben, W. (2008) Molecular analysis of the kirromycin biosynthetic gene cluster revealed β-alanine as precursor of the pyridone moiety. Chem. Biol. 15, 175-188 (Pubitemid 351255583)
    • (2008) Chemistry and Biology , vol.15 , Issue.2 , pp. 175-188
    • Weber, T.1    Laiple, K.J.2    Pross, E.K.3    Textor, A.4    Grond, S.5    Welzel, K.6    Pelzer, S.7    Vente, A.8    Wohlleben, W.9
  • 58
    • 0038183856 scopus 로고    scopus 로고
    • Characterization of the mupirocin biosynthesis gene cluster from Pseudomonas fluorescens NCIMB 10586
    • DOI 10.1016/S1074-5521(03)00091-7
    • El-Sayed, A. K., Hothersall, J., Cooper, S. M., Stephens, E., Simpson, T. J., and Thomas, C. M. (2003) Characterization of the mupirocin biosynthesis gene cluster from Pseudomonas fluorescens NCIMB 10586. Chem. Biol. 10, 419-430 (Pubitemid 36599250)
    • (2003) Chemistry and Biology , vol.10 , Issue.5 , pp. 419-430
    • El-Sayed, A.K.1    Hothersall, J.2    Cooper, S.M.3    Stephens, E.4    Simpson, T.J.5    Thomas, C.M.6
  • 59
    • 0037195174 scopus 로고    scopus 로고
    • A polyketide synthase-peptide synthetase gene cluster from an uncultured bacterial symbiont of Paederus beetles
    • Piel, J. (2002) A polyketide synthase-peptide synthetase gene cluster from an uncultured bacterial symbiont of Paederus beetles. Proc. Natl. Acad. Sci. U.S.A. 99, 14002-14007
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 14002-14007
    • Piel, J.1
  • 60
    • 84856560505 scopus 로고    scopus 로고
    • Discovery of the rhizopodin biosynthetic gene cluster in Stigmatella aurantiaca Sg a15 by genome mining
    • Pistorius, D., and Müller, R. (2012) Discovery of the rhizopodin biosynthetic gene cluster in Stigmatella aurantiaca Sg a15 by genome mining. ChemBioChem 13, 416-426
    • (2012) ChemBioChem , vol.13 , pp. 416-426
    • Pistorius, D.1    Müller, R.2
  • 61
    • 33846294808 scopus 로고    scopus 로고
    • A gene cluster encoding rhizoxin biosynthesis in "Burkholderia rhizoxina", the bacterial endosymbiont of the fungus Rhizopus microsporus
    • DOI 10.1002/cbic.200600393
    • Partida-Martinez, L. P., and Hertweck, C. (2007) A gene cluster encoding rhizoxin biosynthesis in Burkholderia rhizoxina, the bacterial endosymbiont of the fungus Rhizopus microsporus. ChemBioChem. 8, 41-45 (Pubitemid 46121569)
    • (2007) ChemBioChem , vol.8 , Issue.1 , pp. 41-45
    • Partida-Martinez, L.P.1    Hertweck, C.2
  • 62
    • 77956252963 scopus 로고    scopus 로고
    • Analysis of the sorangicin gene cluster reinforces the utility of a combined phylogenetic/retrobiosynthetic analysis for deciphering natural product assembly by trans-AT PKS
    • Irschik, H., Kopp, M., Weissman, K. J., Buntin, K., Piel, J., and Müller, R. (2010) Analysis of the sorangicin gene cluster reinforces the utility of a combined phylogenetic/retrobiosynthetic analysis for deciphering natural product assembly by trans-AT PKS. ChemBioChem 11, 1840-1849
    • (2010) ChemBioChem , vol.11 , pp. 1840-1849
    • Irschik, H.1    Kopp, M.2    Weissman, K.J.3    Buntin, K.4    Piel, J.5    Müller, R.6
  • 63
    • 79954882372 scopus 로고    scopus 로고
    • Mupirocin. Biosynthesis, special features and applications of an antibiotic from a Gram-negative bacterium
    • Gurney, R., and Thomas, C. M. (2011) Mupirocin. Biosynthesis, special features and applications of an antibiotic from a Gram-negative bacterium. Appl. Microbiol. Biotechnol. 90, 11-21
    • (2011) Appl. Microbiol. Biotechnol. , vol.90 , pp. 11-21
    • Gurney, R.1    Thomas, C.M.2
  • 64
  • 66
    • 77049112083 scopus 로고    scopus 로고
    • Isolation and purification of a new kalimantacin/batumin-related polyketide antibiotic and elucidation of its biosynthesis gene cluster
    • Mattheus, W., Gao, L. J., Herdewijn, P., Landuyt, B., Verhaegen, J., Masschelein, J., Volckaert, G., and Lavigne, R. (2010) Isolation and purification of a new kalimantacin/batumin-related polyketide antibiotic and elucidation of its biosynthesis gene cluster. Chem. Biol. 17, 149-159
    • (2010) Chem. Biol. , vol.17 , pp. 149-159
    • Mattheus, W.1    Gao, L.J.2    Herdewijn, P.3    Landuyt, B.4    Verhaegen, J.5    Masschelein, J.6    Volckaert, G.7    Lavigne, R.8
  • 67
    • 0029872079 scopus 로고    scopus 로고
    • Organization of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: Analysis of the enzymatic domains in the modular polyketide synthase
    • DOI 10.1016/0378-1119(95)00800-4
    • Aparicio, J. F., Molnár, I., Schwecke, T., König, A., Haydock, S. F., Khaw, L. E., Staunton, J., and Leadlay, P. F. (1996) Organization of the biosynthetic gene cluster of rapamycin in Streptomyces hygroscopicus. Analysis of the enzymatic domains in the modular polyketide synthase. Gene 169, 9-16 (Pubitemid 26076611)
    • (1996) Gene , vol.169 , Issue.1 , pp. 9-16
    • Aparicio, J.F.1    Molnar, I.2    Schwecke, T.3    Konig, A.4    Haydock, S.F.5    Khaw, L.E.6    Staunton, J.7    Leadlay, P.F.8
  • 69
    • 56249096167 scopus 로고    scopus 로고
    • Crystal structure of the erythromycin polyketide synthase dehydratase
    • Keatinge-Clay, A. (2008) Crystal structure of the erythromycin polyketide synthase dehydratase. J. Mol. Biol. 384, 941-953
    • (2008) J. Mol. Biol. , vol.384 , pp. 941-953
    • Keatinge-Clay, A.1
  • 70
    • 33746032962 scopus 로고    scopus 로고
    • Metabolic coupling of dehydration and decarboxylation in the curacin A pathway: Functional identification of a mechanistically diverse enzyme pair
    • DOI 10.1021/ja0626382
    • Gu, L., Jia, J., Liu, H., Håkansson, K., Gerwick, W. H., and Sherman, D. H. (2006) Metabolic coupling of dehydration and decarboxylation in the curacin A pathway. Functional identification of a mechanistically diverse enzyme pair. J. Am. Chem. Soc. 128, 9014-9015 (Pubitemid 44078967)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.28 , pp. 9014-9015
    • Gu, L.1    Jia, J.2    Liu, H.3    Hakansson, K.4    Gerwick, W.H.5    Sherman, D.H.6
  • 71
    • 0033080078 scopus 로고    scopus 로고
    • How do peptide synthetases generate structural diversity?
    • DOI 10.1016/S1074-5521(99)80002-7
    • Konz, D., and Marahiel, M. A. (1999) How do peptide synthetases generate structural diversity? Chem. Biol. 6, R39-R48 (Pubitemid 29363156)
    • (1999) Chemistry and Biology , vol.6 , Issue.2
    • Konz, D.1    Marahiel, M.A.2
  • 72
    • 0031215148 scopus 로고    scopus 로고
    • Protein templates for the biosynthesis of peptide antibiotics
    • Marahiel, M. A. (1997) Protein templates for the biosynthesis of peptide antibiotics. Chem. Biol. 4, 561-567
    • (1997) Chem. Biol. , vol.4 , pp. 561-567
    • Marahiel, M.A.1
  • 73
    • 33847029508 scopus 로고    scopus 로고
    • Identification of the putative bryostatin polyketide synthase gene cluster from "Candidatus Endobugula sertula," the uncultivated microbial symbiont of the marine bryozoan Bugula neritina
    • Sudek, S., Lopanik, N. B., Waggoner, L. E., Hildebrand, M., Anderson, C., Liu, H., Patel, A., Sherman, D. H., and Haygood, M. G. (2007) Identification of the putative bryostatin polyketide synthase gene cluster from "Candidatus Endobugula sertula," the uncultivated microbial symbiont of the marine bryozoan Bugula neritina. J. Nat. Prod. 70, 67-74
    • (2007) J. Nat. Prod. , vol.70 , pp. 67-74
    • Sudek, S.1    Lopanik, N.B.2    Waggoner, L.E.3    Hildebrand, M.4    Anderson, C.5    Liu, H.6    Patel, A.7    Sherman, D.H.8    Haygood, M.G.9
  • 74
    • 38149064397 scopus 로고    scopus 로고
    • Glyceryl-S-acyl carrier protein as an intermediate in the biosynthesis of tetronate antibiotics
    • Sun, Y., Hong, H., Gillies, F., Spencer, J. B., and Leadlay, P. F. (2008) Glyceryl-S-acyl carrier protein as an intermediate in the biosynthesis of tetronate antibiotics. ChemBioChem. 9, 150-156
    • (2008) ChemBioChem. , vol.9 , pp. 150-156
    • Sun, Y.1    Hong, H.2    Gillies, F.3    Spencer, J.B.4    Leadlay, P.F.5
  • 75
    • 37248999755 scopus 로고    scopus 로고
    • 2 catalytic domain of CurF from Lyngbya majuscula: Insights into a decarboxylase involved in polyketide chain β-branching
    • DOI 10.1074/jbc.M703921200
    • Geders, T. W., Gu, L., Mowers, J. C., Liu, H., Gerwick, W. H., Håkansson, K., Sherman, D. H., and Smith, J. L. (2007) Crystal structure of the ECH2 catalytic domain of CurF from Lyngbya majuscula. Insights into a decarboxylase involved in polyketide chain β-branching. J. Biol. Chem. 282, 35954-35963 (Pubitemid 350277111)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35954-35963
    • Geders, T.W.1    Gu, L.2    Mowers, J.C.3    Liu, H.4    Gerwick, W.H.5    Hakansson, K.6    Sherman, D.H.7    Smith, J.L.8
  • 77
    • 33747191139 scopus 로고    scopus 로고
    • Myxovirescin A biosynthesis is directed by hybrid polyketide synthases/nonribosomal peptide synthetase, 3-hydroxy-3-methylglutaryl-CoA synthases, and trans-acting acyltransferases
    • DOI 10.1002/cbic.200600075
    • Simunovic, V., Zapp, J., Rachid, S., Krug, D., Meiser, P., and Müller, R. (2006) Myxovirescin A biosynthesis is directed by hybrid polyketide synthases/nonribosomal peptide synthetase, 3-hydroxy-3- methylglutaryl- CoA synthases, and trans-acting acyltransferases. ChemBioChem. 7, 1206-1220 (Pubitemid 44230844)
    • (2006) ChemBioChem , vol.7 , Issue.8 , pp. 1206-1220
    • Simunovic, V.1    Zapp, J.2    Rachid, S.3    Krug, D.4    Meiser, P.5    Muller, R.6
  • 78
    • 33646007621 scopus 로고    scopus 로고
    • Polyketide chain skipping mechanism in the biosynthesis of the hybrid nonribosomal peptide-polyketide antitumor antibiotic leinamycin in Streptomyces atroolivaceus S-140
    • Tang, G. L., Cheng, Y. Q., and Shen, B. (2006) Polyketide chain skipping mechanism in the biosynthesis of the hybrid nonribosomal peptide-polyketide antitumor antibiotic leinamycin in Streptomyces atroolivaceus S-140. J. Nat. Prod. 69, 387-393
    • (2006) J. Nat. Prod. , vol.69 , pp. 387-393
    • Tang, G.L.1    Cheng, Y.Q.2    Shen, B.3
  • 79
    • 29844452482 scopus 로고    scopus 로고
    • Identification and analysis of the chivosazol biosynthetic gene cluster from the myxobacterial model strain Sorangium cellulosum So ce56
    • DOI 10.1016/j.jbiotec.2005.10.011, PII S0168165605006541
    • Perlova, O., Gerth, K., Kaiser, O., Hans, A., and Müller, R. (2006) Identification and analysis of the chivosazol biosynthetic gene cluster from the myxobacterial model strain Sorangium cellulosum So ce56. J. Biotechnol. 121, 174-191 (Pubitemid 43038567)
    • (2006) Journal of Biotechnology , vol.121 , Issue.2 , pp. 174-191
    • Perlova, O.1    Gerth, K.2    Kaiser, O.3    Hans, A.4    Muller, R.5
  • 80
    • 77953799129 scopus 로고    scopus 로고
    • Oxazolomycin biosynthesis in Streptomyces albus JA3453 featuring an "acyltransferase-less" type i polyketide synthase that incorporates two distinct extender units
    • Zhao, C., Coughlin, J. M., Ju, J., Zhu, D., Wendt-Pienkowski, E., Zhou, X., Wang, Z., Shen, B., and Deng, Z. (2010) Oxazolomycin biosynthesis in Streptomyces albus JA3453 featuring an "acyltransferase-less" type I polyketide synthase that incorporates two distinct extender units. J. Biol. Chem. 285, 20097-20108
    • (2010) J. Biol. Chem. , vol.285 , pp. 20097-20108
    • Zhao, C.1    Coughlin, J.M.2    Ju, J.3    Zhu, D.4    Wendt-Pienkowski, E.5    Zhou, X.6    Wang, Z.7    Shen, B.8    Deng, Z.9
  • 81
    • 51349147485 scopus 로고    scopus 로고
    • Polyunsaturated fatty-acid-like trans-enoyl reductases utilized in polyketide biosynthesis
    • Bumpus, S. B., Magarvey, N. A., Kelleher, N. L., Walsh, C. T., and Calderone, C. T. (2008) Polyunsaturated fatty-acid-like trans-enoyl reductases utilized in polyketide biosynthesis. J. Am. Chem. Soc. 130, 11614-11616
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11614-11616
    • Bumpus, S.B.1    Magarvey, N.A.2    Kelleher, N.L.3    Walsh, C.T.4    Calderone, C.T.5
  • 82
    • 33745934456 scopus 로고    scopus 로고
    • Molecular mechanisms of enzyme-catalyzed halogenation
    • Anderson, J. L., and Chapman, S. K. (2006) Molecular mechanisms of enzyme-catalyzed halogenation. Mol. BioSyst. 2, 350-357
    • (2006) Mol. BioSyst. , vol.2 , pp. 350-357
    • Anderson, J.L.1    Chapman, S.K.2
  • 83
    • 77249101987 scopus 로고    scopus 로고
    • Chloramphenicol biosynthesis. The structure of CmlS, a flavin-dependent halogenase showing a covalent flavin-aspartate bond
    • Podzelinska, K., Latimer, R., Bhattacharya, A., Vining, L. C., Zechel, D. L., and Jia, Z. (2010) Chloramphenicol biosynthesis. The structure of CmlS, a flavin-dependent halogenase showing a covalent flavin-aspartate bond. J. Mol. Biol. 397, 316-331
    • (2010) J. Mol. Biol. , vol.397 , pp. 316-331
    • Podzelinska, K.1    Latimer, R.2    Bhattacharya, A.3    Vining, L.C.4    Zechel, D.L.5    Jia, Z.6
  • 84
    • 3142745329 scopus 로고    scopus 로고
    • luxS mutants of Serratia defective in autoinducer-2-dependent 'quorum sensing' show strain-dependent impacts on virulence and production of carbapenem and prodigiosin
    • Coulthurst, S. J., Kurz, C. L., and Salmond, G. P. (2004) luxS mutants of Serratia defective in autoinducer-2-dependent "quorum sensing" show strain-dependent impacts on virulence and production of carbapenem and prodigiosin. Microbiology 150, 1901-1910 (Pubitemid 38923688)
    • (2004) Microbiology , vol.150 , Issue.6 , pp. 1901-1910
    • Coulthurst, S.J.1    Kurz, C.L.2    Salmond, G.P.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.