메뉴 건너뛰기




Volumn 15, Issue 1, 2014, Pages

Complete genome sequence of producer of the glycopeptide antibiotic Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus of Pseudonocardiaceae

Author keywords

Aculeximycin; Genome; Genomic islands; Kutzneria; Secondary metabolism

Indexed keywords

ACULEXIMYCIN; RIBOSOME RNA; TRANSFER RNA; ANTIINFECTIVE AGENT; GLYCOPEPTIDE; MACROLIDE;

EID: 84988805355     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-15-885     Document Type: Article
Times cited : (25)

References (99)
  • 1
    • 38949203861 scopus 로고    scopus 로고
    • Contributions of microorganisms to industrial biology
    • Demain AL, Adrio JL: Contributions of microorganisms to industrial biology. Mol Biotechnol 2008, 38(1):41-55.
    • (2008) Mol Biotechnol , vol.38 , Issue.1 , pp. 41-55
    • Demain, A.L.1    Adrio, J.L.2
  • 6
    • 0014265130 scopus 로고
    • Taxonomic study on Streptosporangium albidum nov. sp
    • Furumai T, Ogawa H, Okuda T: Taxonomic study on Streptosporangium albidum nov. sp. J Antibiot (Tokyo) 1968, 21(3):179-181.
    • (1968) J Antibiot (Tokyo) , vol.21 , Issue.3 , pp. 179-181
    • Furumai, T.1    Ogawa, H.2    Okuda, T.3
  • 7
    • 0033960223 scopus 로고    scopus 로고
    • Phylogenetic analysis of Saccharothrix and related taxa: proposal for Actinosynnemataceae fam. nov
    • Labeda DP, Kroppenstedt RM: Phylogenetic analysis of Saccharothrix and related taxa: proposal for Actinosynnemataceae fam. nov. Int J Syst Evol Microbiol 2000, 50(1):331-336.
    • (2000) Int J Syst Evol Microbiol , vol.50 , Issue.1 , pp. 331-336
    • Labeda, D.P.1    Kroppenstedt, R.M.2
  • 9
    • 33846443967 scopus 로고    scopus 로고
    • Low-abundance kutznerides from Kutzneria sp. 744
    • Pohanka A, Menkis A, Levenfors J, Broberg A: Low-abundance kutznerides from Kutzneria sp. 744. J Nat Prod 2006, 69(12):1776-1781.
    • (2006) J Nat Prod , vol.69 , Issue.12 , pp. 1776-1781
    • Pohanka, A.1    Menkis, A.2    Levenfors, J.3    Broberg, A.4
  • 10
    • 0028299633 scopus 로고
    • Transfer of Streptosporangium-Viridogriseum (Okuda Et-Al 1966), Streptosporangium-Viridogriseum Subsp Kofuense (Nonomura and Ohara 1969), and Streptosporangium-Albidum (Furumai Et-Al 1968) to Kutzneria Gen-Nov as Kutzneria-Viridogrisea Comb-Nov, Kutzneria-Kofuensis Comb-Nov, and Kutzneria-Albida Comb-Nov, Respectively, and Emendation of the Genus Streptosporangium
    • Stackebrandt E, Kroppenstedt RM, Jahnke KD, Kemmerling C, Gurtler H: Transfer of Streptosporangium-Viridogriseum (Okuda Et-Al 1966), Streptosporangium-Viridogriseum Subsp Kofuense (Nonomura and Ohara 1969), and Streptosporangium-Albidum (Furumai Et-Al 1968) to Kutzneria Gen-Nov as Kutzneria-Viridogrisea Comb-Nov, Kutzneria-Kofuensis Comb-Nov, and Kutzneria-Albida Comb-Nov, Respectively, and Emendation of the Genus Streptosporangium. Int J Syst Bacteriol 1994, 44(2):265-269.
    • (1994) Int J Syst Bacteriol , vol.44 , Issue.2 , pp. 265-269
    • Stackebrandt, E.1    Kroppenstedt, R.M.2    Jahnke, K.D.3    Kemmerling, C.4    Gurtler, H.5
  • 11
    • 0021023232 scopus 로고
    • Aculeximycin, a new antibiotic from Streptosporangium albidum. I. Taxonomy of producing organism and fermentation
    • Ikemoto T, Matsunaga H, Konishi K, Okazaki T, Enokita R, Torikata A: Aculeximycin, a new antibiotic from Streptosporangium albidum. I. Taxonomy of producing organism and fermentation. J Antibiot (Tokyo) 1983, 36(9):1093-1096.
    • (1983) J Antibiot (Tokyo) , vol.36 , Issue.9 , pp. 1093-1096
    • Ikemoto, T.1    Matsunaga, H.2    Konishi, K.3    Okazaki, T.4    Enokita, R.5    Torikata, A.6
  • 12
    • 0021056808 scopus 로고
    • Aculeximycin, a new antibiotic from Streptosporangium albidum. II. Isolation, physicochemical and biological properties
    • Ikemoto T, Katayama T, Shiraishi A, Haneishi T: Aculeximycin, a new antibiotic from Streptosporangium albidum. II. Isolation, physicochemical and biological properties. J Antibiot (Tokyo) 1983, 36(9):1097-1100.
    • (1983) J Antibiot (Tokyo) , vol.36 , Issue.9 , pp. 1097-1100
    • Ikemoto, T.1    Katayama, T.2    Shiraishi, A.3    Haneishi, T.4
  • 18
    • 78651076675 scopus 로고    scopus 로고
    • Comprehensive prediction of chromosome dimer resolution sites in bacterial genomes
    • Kono N, Arakawa K, Tomita M: Comprehensive prediction of chromosome dimer resolution sites in bacterial genomes. BMC Genomics 2011, 12:19.
    • (2011) BMC Genomics , vol.12 , pp. 19
    • Kono, N.1    Arakawa, K.2    Tomita, M.3
  • 20
    • 79955042499 scopus 로고    scopus 로고
    • Chromosome diversity and similarity within the Actinomycetales
    • Kirby R: Chromosome diversity and similarity within the Actinomycetales. FEMS Microbiol Lett 2011, 319(1):1-10.
    • (2011) FEMS Microbiol Lett , vol.319 , Issue.1 , pp. 1-10
    • Kirby, R.1
  • 26
    • 84868529483 scopus 로고    scopus 로고
    • Complete genome sequence of Amycolatopsis mediterranei S699 based on de novo assembly via a combinatorial sequencing strategy
    • Tang B, Zhao W, Zheng H, Zhuo Y, Zhang L, Zhao GP: Complete genome sequence of Amycolatopsis mediterranei S699 based on de novo assembly via a combinatorial sequencing strategy. J Bacteriol 2012, 194(20):5699-5700.
    • (2012) J Bacteriol , vol.194 , Issue.20 , pp. 5699-5700
    • Tang, B.1    Zhao, W.2    Zheng, H.3    Zhuo, Y.4    Zhang, L.5    Zhao, G.P.6
  • 27
    • 23144460836 scopus 로고    scopus 로고
    • The tRNAscan-SE, snoscan and snoGPS web servers for the detection of tRNAs and snoRNAs
    • Schattner P, Brooks AN, Lowe TM: The tRNAscan-SE, snoscan and snoGPS web servers for the detection of tRNAs and snoRNAs. Nucleic Acids Res 2005, 33:W686-W689.
    • (2005) Nucleic Acids Res , vol.33 , pp. W686-W689
    • Schattner, P.1    Brooks, A.N.2    Lowe, T.M.3
  • 29
  • 30
    • 2942519433 scopus 로고    scopus 로고
    • SIGI: score-based identification of genomic islands
    • Merkl R: SIGI: score-based identification of genomic islands. BMC Bioinformatics 2004, 5:22.
    • (2004) BMC Bioinformatics , vol.5 , pp. 22
    • Merkl, R.1
  • 35
    • 0041620248 scopus 로고    scopus 로고
    • SEARCHPKS: A program for detection and analysis of polyketide synthase domains
    • Yadav G, Gokhale RS, Mohanty D: SEARCHPKS: A program for detection and analysis of polyketide synthase domains. Nucleic Acids Res 2003, 31(13):3654-3658.
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3654-3658
    • Yadav, G.1    Gokhale, R.S.2    Mohanty, D.3
  • 36
    • 7744235042 scopus 로고    scopus 로고
    • Loss of co-linearity by modular polyketide synthases: a mechanism for the evolution of chemical diversity
    • Moss SJ, Martin CJ, Wilkinson B: Loss of co-linearity by modular polyketide synthases: a mechanism for the evolution of chemical diversity. Nat Prod Rep 2004, 21(5):575-593.
    • (2004) Nat Prod Rep , vol.21 , Issue.5 , pp. 575-593
    • Moss, S.J.1    Martin, C.J.2    Wilkinson, B.3
  • 37
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal Peptide antibiotics: logic, machinery, and mechanisms
    • Fischbach MA, Walsh CT: Assembly-line enzymology for polyketide and nonribosomal Peptide antibiotics: logic, machinery, and mechanisms. Chem Rev 2006, 106(8):3468-3496.
    • (2006) Chem Rev , vol.106 , Issue.8 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 39
    • 84860629118 scopus 로고    scopus 로고
    • 6-Deoxyerythronolide B synthase thioesterase-catalyzed macrocyclization is highly stereoselective
    • Pinto A, Wang M, Horsman M, Boddy CN: 6-Deoxyerythronolide B synthase thioesterase-catalyzed macrocyclization is highly stereoselective. Org Lett 2012, 14(9):2278-2281.
    • (2012) Org Lett , vol.14 , Issue.9 , pp. 2278-2281
    • Pinto, A.1    Wang, M.2    Horsman, M.3    Boddy, C.N.4
  • 40
    • 33744486328 scopus 로고    scopus 로고
    • Biosynthetic pathway for mannopeptimycins, lipoglycopeptide antibiotics active against drugresistant gram-positive pathogens
    • Magarvey NA, Haltli B, He M, Greenstein M, Hucul JA: Biosynthetic pathway for mannopeptimycins, lipoglycopeptide antibiotics active against drugresistant gram-positive pathogens. Antimicrob Agents Chemother 2006, 50(6):2167-2177.
    • (2006) Antimicrob Agents Chemother , vol.50 , Issue.6 , pp. 2167-2177
    • Magarvey, N.A.1    Haltli, B.2    He, M.3    Greenstein, M.4    Hucul, J.A.5
  • 41
    • 1642364447 scopus 로고    scopus 로고
    • Biosynthesis of deoxyaminosugars in antibioticproducing bacteria
    • Nedal A, Zotchev SB: Biosynthesis of deoxyaminosugars in antibioticproducing bacteria. Appl Microbiol Biotechnol 2004, 64(1):7-15.
    • (2004) Appl Microbiol Biotechnol , vol.64 , Issue.1 , pp. 7-15
    • Nedal, A.1    Zotchev, S.B.2
  • 42
    • 27944503314 scopus 로고    scopus 로고
    • Biosynthesis pathways for deoxysugars in antibioticproducing actinomycetes: isolation, characterization and generation of novel glycosylated derivatives
    • Salas JA, Mendez C: Biosynthesis pathways for deoxysugars in antibioticproducing actinomycetes: isolation, characterization and generation of novel glycosylated derivatives. J Mol Microbiol Biotechnol 2005, 9(2):77-85.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , Issue.2 , pp. 77-85
    • Salas, J.A.1    Mendez, C.2
  • 43
    • 0034710989 scopus 로고    scopus 로고
    • Deoxysugars in glycopeptide antibiotics: enzymatic synthesis of TDP-Lepivancosamine in chloroeremomycin biosynthesis
    • Chen H, Thomas MG, Hubbard BK, Losey HC, Walsh CT, Burkart MD: Deoxysugars in glycopeptide antibiotics: enzymatic synthesis of TDP-Lepivancosamine in chloroeremomycin biosynthesis. Proc Natl Acad Sci U S A 2000, 97(22):11942-11947.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.22 , pp. 11942-11947
    • Chen, H.1    Thomas, M.G.2    Hubbard, B.K.3    Losey, H.C.4    Walsh, C.T.5    Burkart, M.D.6
  • 44
    • 0028394623 scopus 로고
    • Intracellular glycosylation and active efflux as mechanisms for resistance to oleandomycin in Streptomyces antibioticus, the producer organism
    • Salas JA, Hernandez C, Mendez C, Olano C, Quiros LM, Rodriguez AM, Vilches C: Intracellular glycosylation and active efflux as mechanisms for resistance to oleandomycin in Streptomyces antibioticus, the producer organism. Microbiologia 1994, 10(1-2):37-48.
    • (1994) Microbiologia , vol.10 , Issue.1-2 , pp. 37-48
    • Salas, J.A.1    Hernandez, C.2    Mendez, C.3    Olano, C.4    Quiros, L.M.5    Rodriguez, A.M.6    Vilches, C.7
  • 45
    • 0026526159 scopus 로고
    • Role of glycosylation and deglycosylation in biosynthesis of and resistance to oleandomycin in the producer organism, Streptomyces antibioticus
    • Vilches C, Hernandez C, Mendez C, Salas JA: Role of glycosylation and deglycosylation in biosynthesis of and resistance to oleandomycin in the producer organism, Streptomyces antibioticus. J Bacteriol 1992, 174(1):161-165.
    • (1992) J Bacteriol , vol.174 , Issue.1 , pp. 161-165
    • Vilches, C.1    Hernandez, C.2    Mendez, C.3    Salas, J.A.4
  • 46
    • 0343831467 scopus 로고    scopus 로고
    • The role of ABC transporters in antibiotic-producing organisms: drug secretion and resistance mechanisms
    • Mendez C, Salas JA: The role of ABC transporters in antibiotic-producing organisms: drug secretion and resistance mechanisms. Res Microbiol 2001, 152(3-4):341-350.
    • (2001) Res Microbiol , vol.152 , Issue.3-4 , pp. 341-350
    • Mendez, C.1    Salas, J.A.2
  • 47
    • 0031910748 scopus 로고    scopus 로고
    • ABC transporters in antibiotic-producing actinomycetes
    • Mendez C, Salas JA: ABC transporters in antibiotic-producing actinomycetes. FEMS Microbiol Lett 1998, 158(1):1-8.
    • (1998) FEMS Microbiol Lett , vol.158 , Issue.1 , pp. 1-8
    • Mendez, C.1    Salas, J.A.2
  • 48
    • 80053201949 scopus 로고    scopus 로고
    • Role and regulation of bacterial LuxR-like regulators
    • Chen J, Xie J: Role and regulation of bacterial LuxR-like regulators. J Cell Biochem 2011, 112(10):2694-2702.
    • (2011) J Cell Biochem , vol.112 , Issue.10 , pp. 2694-2702
    • Chen, J.1    Xie, J.2
  • 50
    • 4344588817 scopus 로고    scopus 로고
    • Functional characterization of an aminotransferase required for pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa PAO1
    • Vandenende CS, Vlasschaert M, Seah SY: Functional characterization of an aminotransferase required for pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa PAO1. J Bacteriol 2004, 186(17):5596-5602.
    • (2004) J Bacteriol , vol.186 , Issue.17 , pp. 5596-5602
    • Vandenende, C.S.1    Vlasschaert, M.2    Seah, S.Y.3
  • 51
    • 0030744737 scopus 로고    scopus 로고
    • Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii
    • Ikai H, Yamamoto S: Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii. J Bacteriol 1997, 179(16):5118-5125.
    • (1997) J Bacteriol , vol.179 , Issue.16 , pp. 5118-5125
    • Ikai, H.1    Yamamoto, S.2
  • 52
    • 0042337135 scopus 로고    scopus 로고
    • Irp9, encoded by the high-pathogenicity island of Yersinia enterocolitica, is able to convert chorismate into salicylate, the precursor of the siderophore yersiniabactin
    • Pelludat C, Brem D, Heesemann J: Irp9, encoded by the high-pathogenicity island of Yersinia enterocolitica, is able to convert chorismate into salicylate, the precursor of the siderophore yersiniabactin. J Bacteriol 2003, 185(18):5648-5653.
    • (2003) J Bacteriol , vol.185 , Issue.18 , pp. 5648-5653
    • Pelludat, C.1    Brem, D.2    Heesemann, J.3
  • 53
    • 33749033361 scopus 로고    scopus 로고
    • The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase
    • Harrison AJ, Yu M, Gardenborg T, Middleditch M, Ramsay RJ, Baker EN, Lott JS: The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase. J Bacteriol 2006, 188(17):6081-6091.
    • (2006) J Bacteriol , vol.188 , Issue.17 , pp. 6081-6091
    • Harrison, A.J.1    Yu, M.2    Gardenborg, T.3    Middleditch, M.4    Ramsay, R.J.5    Baker, E.N.6    Lott, J.S.7
  • 54
    • 33749649804 scopus 로고    scopus 로고
    • Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa
    • Ge L, Seah SY: Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa. J Bacteriol 2006, 188(20):7205-7210.
    • (2006) J Bacteriol , vol.188 , Issue.20 , pp. 7205-7210
    • Ge, L.1    Seah, S.Y.2
  • 55
    • 33747074333 scopus 로고    scopus 로고
    • Identification of genes involved in siderophore transport in Streptomyces coelicolor A3(2)
    • Bunet R, Brock A, Rexer HU, Takano E: Identification of genes involved in siderophore transport in Streptomyces coelicolor A3(2). FEMS Microbiol Lett 2006, 262(1):57-64.
    • (2006) FEMS Microbiol Lett , vol.262 , Issue.1 , pp. 57-64
    • Bunet, R.1    Brock, A.2    Rexer, H.U.3    Takano, E.4
  • 56
    • 70350643410 scopus 로고    scopus 로고
    • The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis
    • Oves-Costales D, Kadi N, Challis GL: The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem Commun (Camb) 2009, 43:6530-6541.
    • (2009) Chem Commun (Camb) , vol.43 , pp. 6530-6541
    • Oves-Costales, D.1    Kadi, N.2    Challis, G.L.3
  • 58
    • 0026657817 scopus 로고
    • Molecular cloning and sequencing of the gene for mycocerosic acid synthase, a novel fatty acid elongating multifunctional enzyme, from Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin
    • Mathur M, Kolattukudy PE: Molecular cloning and sequencing of the gene for mycocerosic acid synthase, a novel fatty acid elongating multifunctional enzyme, from Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. J Biol Chem 1992, 267(27):19388-19395.
    • (1992) J Biol Chem , vol.267 , Issue.27 , pp. 19388-19395
    • Mathur, M.1    Kolattukudy, P.E.2
  • 59
    • 0035987331 scopus 로고    scopus 로고
    • Structure and regulation of the omega-3 polyunsaturated fatty acid synthase genes from the deep-sea bacterium Photobacterium profundum strain SS9
    • Allen EE, Bartlett DH: Structure and regulation of the omega-3 polyunsaturated fatty acid synthase genes from the deep-sea bacterium Photobacterium profundum strain SS9. Microbiology 2002, 148(Pt 6):1903-1913.
    • (2002) Microbiology , vol.148 , pp. 1903-1913
    • Allen, E.E.1    Bartlett, D.H.2
  • 60
    • 0036710533 scopus 로고    scopus 로고
    • Polyunsaturated fatty acid synthesis: what will they think of next?
    • Wallis JG, Watts JL, Browse J: Polyunsaturated fatty acid synthesis: what will they think of next? Trends Biochem Sci 2002, 27(9):467.
    • (2002) Trends Biochem Sci , vol.27 , Issue.9 , pp. 467
    • Wallis, J.G.1    Watts, J.L.2    Browse, J.3
  • 61
    • 0027317343 scopus 로고
    • Hybridization and DNA sequence analyses suggest an early evolutionary divergence of related biosynthetic gene sets encoding polyketide antibiotics and spore pigments in Streptomyces spp
    • Blanco G, Brian P, Pereda A, Mendez C, Salas JA, Chater KF: Hybridization and DNA sequence analyses suggest an early evolutionary divergence of related biosynthetic gene sets encoding polyketide antibiotics and spore pigments in Streptomyces spp. Gene 1993, 130(1):107-116.
    • (1993) Gene , vol.130 , Issue.1 , pp. 107-116
    • Blanco, G.1    Brian, P.2    Pereda, A.3    Mendez, C.4    Salas, J.A.5    Chater, K.F.6
  • 62
    • 0025129406 scopus 로고
    • Spore colour in Streptomyces coelicolor A3(2) involves the developmentally regulated synthesis of a compound biosynthetically related to polyketide antibiotics
    • Davis NK, Chater KF: Spore colour in Streptomyces coelicolor A3(2) involves the developmentally regulated synthesis of a compound biosynthetically related to polyketide antibiotics. Mol Microbiol 1990, 4(10):1679-1691.
    • (1990) Mol Microbiol , vol.4 , Issue.10 , pp. 1679-1691
    • Davis, N.K.1    Chater, K.F.2
  • 63
    • 0032902411 scopus 로고    scopus 로고
    • The mithramycin gene cluster of Streptomyces argillaceus contains a positive regulatory gene and two repeated DNA sequences that are located at both ends of the cluster
    • Lombo F, Brana AF, Mendez C, Salas JA: The mithramycin gene cluster of Streptomyces argillaceus contains a positive regulatory gene and two repeated DNA sequences that are located at both ends of the cluster. J Bacteriol 1999, 181(2):642-647.
    • (1999) J Bacteriol , vol.181 , Issue.2 , pp. 642-647
    • Lombo, F.1    Brana, A.F.2    Mendez, C.3    Salas, J.A.4
  • 64
    • 0034785026 scopus 로고    scopus 로고
    • The entire nogalamycin biosynthetic gene cluster of Streptomyces nogalater: characterization of a 20-kb DNA region and generation of hybrid structures
    • Torkkell S, Kunnari T, Palmu K, Mantsala P, Hakala J, Ylihonko K: The entire nogalamycin biosynthetic gene cluster of Streptomyces nogalater: characterization of a 20-kb DNA region and generation of hybrid structures. Mol Genet Genomics 2001, 266(2):276-288.
    • (2001) Mol Genet Genomics , vol.266 , Issue.2 , pp. 276-288
    • Torkkell, S.1    Kunnari, T.2    Palmu, K.3    Mantsala, P.4    Hakala, J.5    Ylihonko, K.6
  • 65
    • 0035065966 scopus 로고    scopus 로고
    • Biosynthesis of hybrid peptide-polyketide natural products
    • Du L, Shen B: Biosynthesis of hybrid peptide-polyketide natural products. Curr Opin Drug Discov Devel 2001, 4(2):215-228.
    • (2001) Curr Opin Drug Discov Devel , vol.4 , Issue.2 , pp. 215-228
    • Du, L.1    Shen, B.2
  • 67
    • 38349074340 scopus 로고    scopus 로고
    • Mycobacterial phenolic glycolipid virulence factor biosynthesis: mechanism and small-molecule inhibition of polyketide chain initiation
    • Ferreras JA, Stirrett KL, Lu X, Ryu JS, Soll CE, Tan DS, Quadri LE: Mycobacterial phenolic glycolipid virulence factor biosynthesis: mechanism and small-molecule inhibition of polyketide chain initiation. Chem Biol 2008, 15(1):51-61.
    • (2008) Chem Biol , vol.15 , Issue.1 , pp. 51-61
    • Ferreras, J.A.1    Stirrett, K.L.2    Lu, X.3    Ryu, J.S.4    Soll, C.E.5    Tan, D.S.6    Quadri, L.E.7
  • 68
    • 33745484154 scopus 로고    scopus 로고
    • Control of iron metabolism in Mycobacterium tuberculosis
    • Rodriguez GM: Control of iron metabolism in Mycobacterium tuberculosis. Trends Microbiol 2006, 14(7):320-327.
    • (2006) Trends Microbiol , vol.14 , Issue.7 , pp. 320-327
    • Rodriguez, G.M.1
  • 69
    • 84860780250 scopus 로고    scopus 로고
    • Two distinct pathways for essential metabolic precursors for isoprenoid biosynthesis
    • Kuzuyama T, Seto H: Two distinct pathways for essential metabolic precursors for isoprenoid biosynthesis. Proc Jpn Acad Ser B Phys Biol Sci 2012, 88(3):41-52.
    • (2012) Proc Jpn Acad Ser B Phys Biol Sci , vol.88 , Issue.3 , pp. 41-52
    • Kuzuyama, T.1    Seto, H.2
  • 70
    • 0035753787 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis via 1-deoxy-D-xylulose 5-phosphate/2-C-methyl-D-erythritol 4-phosphate (DOXP/MEP) pathway
    • Wanke M, Skorupinska-Tudek K, Swiezewska E: Isoprenoid biosynthesis via 1-deoxy-D-xylulose 5-phosphate/2-C-methyl-D-erythritol 4-phosphate (DOXP/MEP) pathway. Acta Biochim Pol 2001, 48(3):663-672.
    • (2001) Acta Biochim Pol , vol.48 , Issue.3 , pp. 663-672
    • Wanke, M.1    Skorupinska-Tudek, K.2    Swiezewska, E.3
  • 71
    • 84858676944 scopus 로고    scopus 로고
    • Exploration and mining of the bacterial terpenome
    • Cane DE, Ikeda H: Exploration and mining of the bacterial terpenome. Acc Chem Res 2012, 45(3):463-472.
    • (2012) Acc Chem Res , vol.45 , Issue.3 , pp. 463-472
    • Cane, D.E.1    Ikeda, H.2
  • 72
    • 44949176042 scopus 로고    scopus 로고
    • Identification and functional analysis of genes controlling biosynthesis of 2-methylisoborneol
    • Komatsu M, Tsuda M, Omura S, Oikawa H, Ikeda H: Identification and functional analysis of genes controlling biosynthesis of 2-methylisoborneol. Proc Natl Acad Sci U S A 2008, 105(21):7422-7427.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.21 , pp. 7422-7427
    • Komatsu, M.1    Tsuda, M.2    Omura, S.3    Oikawa, H.4    Ikeda, H.5
  • 73
    • 33745013076 scopus 로고    scopus 로고
    • Structural diversity and functional novelty of new carotenoid biosynthesis genes
    • Cheng Q: Structural diversity and functional novelty of new carotenoid biosynthesis genes. J Ind Microbiol Biotechnol 2006, 33(7):552-559.
    • (2006) J Ind Microbiol Biotechnol , vol.33 , Issue.7 , pp. 552-559
    • Cheng, Q.1
  • 74
    • 0032943554 scopus 로고    scopus 로고
    • Hopanoid biosynthesis and function in bacteria
    • Kannenberg EL, Poralla K: Hopanoid biosynthesis and function in bacteria. Naturwissenschaften 1999, 86(4):168-176.
    • (1999) Naturwissenschaften , vol.86 , Issue.4 , pp. 168-176
    • Kannenberg, E.L.1    Poralla, K.2
  • 75
    • 57149120517 scopus 로고    scopus 로고
    • Synthesis and uptake of the compatible solutes ectoine and 5-hydroxyectoine by Streptomyces coelicolor A3(2) in response to salt and heat stresses
    • Bursy J, Kuhlmann AU, Pittelkow M, Hartmann H, Jebbar M, Pierik AJ, Bremer E: Synthesis and uptake of the compatible solutes ectoine and 5-hydroxyectoine by Streptomyces coelicolor A3(2) in response to salt and heat stresses. Appl Environ Microbiol 2008, 74(23):7286-7296.
    • (2008) Appl Environ Microbiol , vol.74 , Issue.23 , pp. 7286-7296
    • Bursy, J.1    Kuhlmann, A.U.2    Pittelkow, M.3    Hartmann, H.4    Jebbar, M.5    Pierik, A.J.6    Bremer, E.7
  • 77
    • 62449239363 scopus 로고    scopus 로고
    • Chemical biology of natural indolocarbazole products: 30 years since the discovery of staurosporine
    • Nakano H, Omura S: Chemical biology of natural indolocarbazole products: 30 years since the discovery of staurosporine. J Antibiot (Tokyo) 2009, 62(1):17-26.
    • (2009) J Antibiot (Tokyo) , vol.62 , Issue.1 , pp. 17-26
    • Nakano, H.1    Omura, S.2
  • 78
    • 33751335837 scopus 로고    scopus 로고
    • Indolocarbazole natural products: occurrence, biosynthesis, and biological activity
    • Sanchez C, Mendez C, Salas JA: Indolocarbazole natural products: occurrence, biosynthesis, and biological activity. Nat Prod Rep 2006, 23(6):1007-1045.
    • (2006) Nat Prod Rep , vol.23 , Issue.6 , pp. 1007-1045
    • Sanchez, C.1    Mendez, C.2    Salas, J.A.3
  • 79
    • 84861308350 scopus 로고    scopus 로고
    • YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations
    • Dunbar KL, Melby JO, Mitchell DA: YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations. Nat Chem Biol 2012, 8(6):569-575.
    • (2012) Nat Chem Biol , vol.8 , Issue.6 , pp. 569-575
    • Dunbar, K.L.1    Melby, J.O.2    Mitchell, D.A.3
  • 80
    • 79957973597 scopus 로고    scopus 로고
    • Thiazole/oxazole-modified microcins: complex natural products from ribosomal templates
    • Melby JO, Nard NJ, Mitchell DA: Thiazole/oxazole-modified microcins: complex natural products from ribosomal templates. Curr Opin Chem Biol 2011, 15(3):369-378.
    • (2011) Curr Opin Chem Biol , vol.15 , Issue.3 , pp. 369-378
    • Melby, J.O.1    Nard, N.J.2    Mitchell, D.A.3
  • 81
    • 0028075093 scopus 로고
    • Isolation and characterization of Linocin M18, a bacteriocin produced by Brevibacterium linens
    • Valdes-Stauber N, Scherer S: Isolation and characterization of Linocin M18, a bacteriocin produced by Brevibacterium linens. Appl Environ Microbiol 1994, 60(10):3809-3814.
    • (1994) Appl Environ Microbiol , vol.60 , Issue.10 , pp. 3809-3814
    • Valdes-Stauber, N.1    Scherer, S.2
  • 83
    • 0037362042 scopus 로고    scopus 로고
    • Evaluation of similarity measures for searching the Dictionary of Natural Products database
    • Whittle M, Willett P, Klaffke W, Van Noort P: Evaluation of similarity measures for searching the Dictionary of Natural Products database. J Chem Inf Comput Sci 2003, 43(2):449-457.
    • (2003) J Chem Inf Comput Sci , vol.43 , Issue.2 , pp. 449-457
    • Whittle, M.1    Willett, P.2    Klaffke, W.3    Van Noort, P.4
  • 85
    • 84879332100 scopus 로고    scopus 로고
    • Insights into the Generation of Structural Diversity in a tRNA-Dependent Pathway for Highly Modified Bioactive Cyclic Dipeptides
    • Giessen TW, Von Tesmar AM, Marahiel MA: Insights into the Generation of Structural Diversity in a tRNA-Dependent Pathway for Highly Modified Bioactive Cyclic Dipeptides. Chem Biol 2013, 20(6):828-838.
    • (2013) Chem Biol , vol.20 , Issue.6 , pp. 828-838
    • Giessen, T.W.1    Von Tesmar, A.M.2    Marahiel, M.A.3
  • 86
    • 84865007362 scopus 로고    scopus 로고
    • The nonribosomal synthesis of diketopiperazines in tRNA-dependent cyclodipeptide synthase pathways
    • Belin P, Moutiez M, Lautru S, Seguin J, Pernodet JL, Gondry M: The nonribosomal synthesis of diketopiperazines in tRNA-dependent cyclodipeptide synthase pathways. Nat Prod Rep 2012, 29(9):961-979.
    • (2012) Nat Prod Rep , vol.29 , Issue.9 , pp. 961-979
    • Belin, P.1    Moutiez, M.2    Lautru, S.3    Seguin, J.4    Pernodet, J.L.5    Gondry, M.6
  • 89
    • 79961209508 scopus 로고    scopus 로고
    • Sequencing of high G + C microbial genomes using the ultrafast pyrosequencing technology
    • Schwientek P, Szczepanowski R, Rückert C, Stoye J, Puhler A: Sequencing of high G + C microbial genomes using the ultrafast pyrosequencing technology. J Biotechnol 2011, 155(1):68-77.
    • (2011) J Biotechnol , vol.155 , Issue.1 , pp. 68-77
    • Schwientek, P.1    Szczepanowski, R.2    Rückert, C.3    Stoye, J.4    Puhler, A.5
  • 90
    • 0031955116 scopus 로고    scopus 로고
    • Consed: A graphical tool for sequence finishing
    • Gordon D, Abajian C, Green P: Consed: A graphical tool for sequence finishing. Genome Res 1998, 8(3):195-202.
    • (1998) Genome Res , vol.8 , Issue.3 , pp. 195-202
    • Gordon, D.1    Abajian, C.2    Green, P.3
  • 96
    • 33747892409 scopus 로고    scopus 로고
    • Automatic clustering of orthologs and inparalogs shared by multiple proteomes
    • Alexeyenko A, Tamas I, Liu G, Sonnhammer ELL: Automatic clustering of orthologs and inparalogs shared by multiple proteomes. Bioinformatics 2006, 22(14):E9-E15.
    • (2006) Bioinformatics , vol.22 , Issue.14 , pp. E9-E15
    • Alexeyenko, A.1    Tamas, I.2    Liu, G.3    Sonnhammer, E.L.L.4
  • 99
    • 0038325632 scopus 로고    scopus 로고
    • Production of landomycins in Streptomyces globisporus 1912 and S cyanogenus S136 is regulated by genes encoding putative transcriptional activators
    • Rebets Y, Ostash B, Luzhetskyy A, Hoffmeister D, Brana A, Mendez C, Salas JA, Bechtold A, Fedorenko V: Production of landomycins in Streptomyces globisporus 1912 and S cyanogenus S136 is regulated by genes encoding putative transcriptional activators. FEMS Microbiol Lett 2003, 222(1):149-153.
    • (2003) FEMS Microbiol Lett , vol.222 , Issue.1 , pp. 149-153
    • Rebets, Y.1    Ostash, B.2    Luzhetskyy, A.3    Hoffmeister, D.4    Brana, A.5    Mendez, C.6    Salas, J.A.7    Bechtold, A.8    Fedorenko, V.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.