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Volumn 51, Issue 3, 2007, Pages 1028-1037

Sequencing and analysis of the biosynthetic gene cluster of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis

Author keywords

[No Author keywords available]

Indexed keywords

2,3 DIAMINOBUTYRIC ACID; AMINO ACID; AMINO ACID DERIVATIVE; ANTIBIOTIC AGENT; CYCLOPEPTIDE; DEAMINASE; FATTY ACID DERIVATIVE; FRIULIMICIN; LIPOPEPTIDE; METHYLASPARTIC ACID; PIPECOLINIC ACID; UNCLASSIFIED DRUG;

EID: 33847644980     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.00942-06     Document Type: Article
Times cited : (62)

References (54)
  • 1
    • 0026024490 scopus 로고
    • Genetic analysis of the phosphinothricin-tripeptide biosynthetic pathway of Streptomyces viridochromogenes Tu494
    • Alijah, R., J. Dorendorf, S. Talay, A. Puhler, and W. Wohlleben. 1991. Genetic analysis of the phosphinothricin-tripeptide biosynthetic pathway of Streptomyces viridochromogenes Tu494. Appl. Microbiol. Biotechnol. 34:749-755.
    • (1991) Appl. Microbiol. Biotechnol , vol.34 , pp. 749-755
    • Alijah, R.1    Dorendorf, J.2    Talay, S.3    Puhler, A.4    Wohlleben, W.5
  • 3
    • 3442896886 scopus 로고    scopus 로고
    • posting date. NRPS-PKS: A knowledge-based resource for analysis of NRPS/PKS megasynthases
    • 1 July
    • Ansari, M. Z., G. Yadav, R. S. Gokhale, and D. Mohanty. 1 July 2004, posting date. NRPS-PKS: a knowledge-based resource for analysis of NRPS/PKS megasynthases. Nucleic Acids Res. 32:W405-W413.
    • (2004) Nucleic Acids Res , vol.32
    • Ansari, M.Z.1    Yadav, G.2    Gokhale, R.S.3    Mohanty, D.4
  • 4
    • 0033850685 scopus 로고    scopus 로고
    • Friulimicins: Novel lipopeptide antibiotics with peptidoglycan synthesis inhibiting activity from Actinoplanes friuliensis sp. nov. I. Taxonomic studies of the producing microorganism and fermentation
    • Aretz, W., J. Meiwes, G. Seibert, G. Vobis, and J. Wink. 2000. Friulimicins: novel lipopeptide antibiotics with peptidoglycan synthesis inhibiting activity from Actinoplanes friuliensis sp. nov. I. Taxonomic studies of the producing microorganism and fermentation. J. Antibiot. (Tokyo) 53:807-815.
    • (2000) J. Antibiot. (Tokyo) , vol.53 , pp. 807-815
    • Aretz, W.1    Meiwes, J.2    Seibert, G.3    Vobis, G.4    Wink, J.5
  • 5
    • 0024498350 scopus 로고
    • Amphomycin inhibits mannosylphosphoryldolichol synthesis by forming a complex with dolichylmonophosphate
    • Banerjee, D. K. 1989. Amphomycin inhibits mannosylphosphoryldolichol synthesis by forming a complex with dolichylmonophosphate. J. Biol. Chem. 264:2024-2028.
    • (1989) J. Biol. Chem , vol.264 , pp. 2024-2028
    • Banerjee, D.K.1
  • 6
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • Bierman, M., R. Logan, K. O'Brien, E. T. Seno, R. N. Rao, and B. E. Schoner. 1992. Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp. Gene 116:43-49.
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    O'Brien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 7
    • 0014655866 scopus 로고    scopus 로고
    • Bodanszky, M., N. C. Chaturvedi, J. A. Scozzie, R. K. Griffith, and A. Bodanszky. 1969. Constituents of amphomycin. Antimicrob. Agents Chemother. mother. 9:135-138.
    • Bodanszky, M., N. C. Chaturvedi, J. A. Scozzie, R. K. Griffith, and A. Bodanszky. 1969. Constituents of amphomycin. Antimicrob. Agents Chemother. mother. 9:135-138.
  • 8
    • 0035902497 scopus 로고    scopus 로고
    • Chiu, H. T., B. K. Hubbard, A. N. Shah, J. Eide, R. A. Fredenburg, C. T. Walsh, and C. Khosla. 10 July 2001. Molecular cloning and sequence analysis of the complestatin biosynthetic gene cluster. Proc. Natl. Acad. Sci. USA 98:8548-8553. [Epub ahead of print.]
    • Chiu, H. T., B. K. Hubbard, A. N. Shah, J. Eide, R. A. Fredenburg, C. T. Walsh, and C. Khosla. 10 July 2001. Molecular cloning and sequence analysis of the complestatin biosynthetic gene cluster. Proc. Natl. Acad. Sci. USA 98:8548-8553. [Epub ahead of print.]
  • 9
    • 0031572413 scopus 로고    scopus 로고
    • High efficiency intergeneric conjugal transfer of plasmid DNA from Escherichia coli to methyl DNA-restricting streptomycetes
    • Flett, F., V. Mersinias, and C. P. Smith. 1997. High efficiency intergeneric conjugal transfer of plasmid DNA from Escherichia coli to methyl DNA-restricting streptomycetes. FEMS Microbiol. Lett. 155:223-229.
    • (1997) FEMS Microbiol. Lett , vol.155 , pp. 223-229
    • Flett, F.1    Mersinias, V.2    Smith, C.P.3
  • 10
    • 33645392725 scopus 로고    scopus 로고
    • Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster
    • Gatto, G. J., Jr., M. T. Boyne II, N. L. Kelleher, and C. T. Walsh. 2006. Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster. J. Am. Chem. Soc. 128:3838-3847.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 3838-3847
    • Gatto Jr., G.J.1    Boyne II, M.T.2    Kelleher, N.L.3    Walsh, C.T.4
  • 11
    • 11244286128 scopus 로고    scopus 로고
    • Synthesis and derivatization of daptomycin: A chemoenzymatic route to acidic lipopeptide antibiotics
    • Grunewald, J., S. A. Sieber, C. Mahlert, U. Linne, and M. A. Marahiel. 2004a. Synthesis and derivatization of daptomycin: a chemoenzymatic route to acidic lipopeptide antibiotics. J. Am. Chem. Soc. 126:17025-17031.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 17025-17031
    • Grunewald, J.1    Sieber, S.A.2    Mahlert, C.3    Linne, U.4    Marahiel, M.A.5
  • 12
    • 12144287553 scopus 로고    scopus 로고
    • Chemo- and regioselective peptide cyclization triggered by the N-terminal fatty acid chain length: The recombinant cyclase of the calcium-dependent antibiotic from Streptomyces coelicolor
    • Grunewald, J., S. A. Sieber, and M. A. Marahiel. 2004b. Chemo- and regioselective peptide cyclization triggered by the N-terminal fatty acid chain length: the recombinant cyclase of the calcium-dependent antibiotic from Streptomyces coelicolor. Biochemistry 43:2915-2925.
    • (2004) Biochemistry , vol.43 , pp. 2915-2925
    • Grunewald, J.1    Sieber, S.A.2    Marahiel, M.A.3
  • 13
    • 0032549502 scopus 로고    scopus 로고
    • An efficient asymmetric route to 2,3-diaminobutanoic acid
    • Han, H., J. Yoon, and K. D. Janda. 1998. An efficient asymmetric route to 2,3-diaminobutanoic acid. J. Org. Chem. 63:2045-2048.
    • (1998) J. Org. Chem , vol.63 , pp. 2045-2048
    • Han, H.1    Yoon, J.2    Janda, K.D.3
  • 14
    • 21344467263 scopus 로고    scopus 로고
    • An acyl-CoA dehydrogenase is involved in the formation of the Δcis3 double bond in the acyl residue of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis
    • Heinzelmann, E., S. Berger, C. Müller, T. Härtner, K. Poralla, W. Wohlleben, and D. Schwartz. 2005. An acyl-CoA dehydrogenase is involved in the formation of the Δcis3 double bond in the acyl residue of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis. Microbiology 151:1963-1974.
    • (2005) Microbiology , vol.151 , pp. 1963-1974
    • Heinzelmann, E.1    Berger, S.2    Müller, C.3    Härtner, T.4    Poralla, K.5    Wohlleben, W.6    Schwartz, D.7
  • 15
    • 0037310949 scopus 로고    scopus 로고
    • A glutamate mutase is involved in the biosynthesis of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis
    • Heinzelmann, E., S. Berger, O. Puk, B. Reichenstein, W. Wohlleben, and D. Schwartz. 2003. A glutamate mutase is involved in the biosynthesis of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis. Antimicrob. Agents Chemother. 47:447-457.
    • (2003) Antimicrob. Agents Chemother , vol.47 , pp. 447-457
    • Heinzelmann, E.1    Berger, S.2    Puk, O.3    Reichenstein, B.4    Wohlleben, W.5    Schwartz, D.6
  • 16
    • 0035434674 scopus 로고    scopus 로고
    • The phosphinomethylmalate isomerase gene pmi, encoding an aconitase-like enzyme, is involved in the synthesis of phosphinothricin tripeptide in Streptomyces viridochromogenes
    • Heinzelmann, E., G. Kienzlen, S. Kaspar, J. Recktenwald, W. Wohlleben, and D. Schwartz. 2001. The phosphinomethylmalate isomerase gene pmi, encoding an aconitase-like enzyme, is involved in the synthesis of phosphinothricin tripeptide in Streptomyces viridochromogenes. Appl. Environ. Microbiol. 67:3603-3609.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 3603-3609
    • Heinzelmann, E.1    Kienzlen, G.2    Kaspar, S.3    Recktenwald, J.4    Wohlleben, W.5    Schwartz, D.6
  • 19
    • 2642591970 scopus 로고    scopus 로고
    • Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase
    • Khaw, L. E., G. A. Bohm, S. Metcalfe, J. Staunton, and P. F. Leadlay. 1998. Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase. J. Bacteriol. 180:809-814.
    • (1998) J. Bacteriol , vol.180 , pp. 809-814
    • Khaw, L.E.1    Bohm, G.A.2    Metcalfe, S.3    Staunton, J.4    Leadlay, P.F.5
  • 21
    • 0031319043 scopus 로고    scopus 로고
    • Applications of peptide synthetases in the synthesis of peptide analogues
    • Kleinkauf, H., and H. von Döhren. 1997. Applications of peptide synthetases in the synthesis of peptide analogues. Acta Biochim. Pol. 44:839-847.
    • (1997) Acta Biochim. Pol , vol.44 , pp. 839-847
    • Kleinkauf, H.1    von Döhren, H.2
  • 22
    • 1142306159 scopus 로고    scopus 로고
    • Biosynthetic gene cluster of the glycopeptide antibiotic teicoplanin: Characterization of two glycosyltransferases and the key acyltransferase
    • Li, T. L., F. Huang, S. F. Haydock, T. Mironenko, P. F. Leadlay, and J. B. Spencer. 2004. Biosynthetic gene cluster of the glycopeptide antibiotic teicoplanin: characterization of two glycosyltransferases and the key acyltransferase. Chem. Biol. 11:107-119.
    • (2004) Chem. Biol , vol.11 , pp. 107-119
    • Li, T.L.1    Huang, F.2    Haydock, S.F.3    Mironenko, T.4    Leadlay, P.F.5    Spencer, J.B.6
  • 23
    • 0031910748 scopus 로고    scopus 로고
    • ABC transporters in antibiotic-producing actinomycetes
    • Mendez, C., and J. A. Salas. 1998. ABC transporters in antibiotic-producing actinomycetes. FEMS Microbiol. Lett. 158:1-8.
    • (1998) FEMS Microbiol. Lett , vol.158 , pp. 1-8
    • Mendez, C.1    Salas, J.A.2
  • 24
    • 30844453153 scopus 로고    scopus 로고
    • Miao, V., R. Brost, J. Chapple, K. She, M. F. Gal, and R. H. Baltz. 6 October 2005. The lipopeptide antibiotic A54145 biosynthetic gene cluster from Streptomyces fradiae. J. Ind. Microbiol. Biotechnol. 33:129-140. [Epub ahead of print.]
    • Miao, V., R. Brost, J. Chapple, K. She, M. F. Gal, and R. H. Baltz. 6 October 2005. The lipopeptide antibiotic A54145 biosynthetic gene cluster from Streptomyces fradiae. J. Ind. Microbiol. Biotechnol. 33:129-140. [Epub ahead of print.]
  • 27
    • 0029883934 scopus 로고    scopus 로고
    • Organisation of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: Analysis of genes flanking the polyketide synthase
    • Molnar, I., J. F. Aparicio, S. F. Haydock, L. E. Khaw, T. Schwecke, A. Konig, J. Staunton, and P. F. Leadlay. 1996. Organisation of the biosynthetic gene cluster for rapamycin in Streptomyces hygroscopicus: analysis of genes flanking the polyketide synthase. Gene 169:1-7.
    • (1996) Gene , vol.169 , pp. 1-7
    • Molnar, I.1    Aparicio, J.F.2    Haydock, S.F.3    Khaw, L.E.4    Schwecke, T.5    Konig, A.6    Staunton, J.7    Leadlay, P.F.8
  • 28
    • 0342614926 scopus 로고    scopus 로고
    • Codon usage tabulated from international DNA sequence databases: Status for the year 2000
    • Nakamura, Y., T. Gojobori, and T. Ikemura. 2000. Codon usage tabulated from international DNA sequence databases: status for the year 2000. Nucleic Acids Res. 28:292.
    • (2000) Nucleic Acids Res , vol.28 , pp. 292
    • Nakamura, Y.1    Gojobori, T.2    Ikemura, T.3
  • 30
    • 0031799094 scopus 로고    scopus 로고
    • Two glycosyltransferases and a glycosidase are involved in oleandomycin modification during its biosynthesis by Streptomyces antibioticus
    • Quiros, L. M., I. Aguirrezabalaga, C. Olano, C. Mendez, and J. A. Salas. 1998. Two glycosyltransferases and a glycosidase are involved in oleandomycin modification during its biosynthesis by Streptomyces antibioticus. Mol. Microbiol. 28:1177-1185.
    • (1998) Mol. Microbiol , vol.28 , pp. 1177-1185
    • Quiros, L.M.1    Aguirrezabalaga, I.2    Olano, C.3    Mendez, C.4    Salas, J.A.5
  • 31
    • 0025814821 scopus 로고
    • Nucleotide sequence analysis reveals linked N-acetyl hydrolase, thioesterase, transport, and regulatory genes encoded by the bialaphos biosynthetic gene cluster of Streptomyces hygroscopicus
    • Raibaud, A., M. Zalacain, T. G. Holt, R. Tizard, and C. J. Thompson. 1991. Nucleotide sequence analysis reveals linked N-acetyl hydrolase, thioesterase, transport, and regulatory genes encoded by the bialaphos biosynthetic gene cluster of Streptomyces hygroscopicus. J. Bacteriol. 173:4454-4463.
    • (1991) J. Bacteriol , vol.173 , pp. 4454-4463
    • Raibaud, A.1    Zalacain, M.2    Holt, T.G.3    Tizard, R.4    Thompson, C.J.5
  • 32
    • 0023504683 scopus 로고
    • Cosmid shuttle vectors for cloning and analysis of Streptomyces DNA
    • Rao, R. N., M. A. Richardson, and S. Kuhstoss. 1987. Cosmid shuttle vectors for cloning and analysis of Streptomyces DNA. Methods Enzymol. 153:166-198.
    • (1987) Methods Enzymol , vol.153 , pp. 166-198
    • Rao, R.N.1    Richardson, M.A.2    Kuhstoss, S.3
  • 35
    • 0032486418 scopus 로고    scopus 로고
    • Short syntheses of (S)-pipecolic acid, (R)-coniine, and (S)-δ-coniceine using biocatalytically-generated chiral building blocks
    • Sanchez-Sancho, F., and B. Herradon. 1998. Short syntheses of (S)-pipecolic acid, (R)-coniine, and (S)-δ-coniceine using biocatalytically-generated chiral building blocks. Tetrahedron Asymmetry 9:1951-1965.
    • (1998) Tetrahedron Asymmetry , vol.9 , pp. 1951-1965
    • Sanchez-Sancho, F.1    Herradon, B.2
  • 36
    • 0015514196 scopus 로고
    • The mechanism of the inhibition of gramicidin-S synthesis by D-leucine
    • Saxholm, H., T. L. Zimmer, and S. G. Laland. 1972. The mechanism of the inhibition of gramicidin-S synthesis by D-leucine. Eur. J. Biochem. 30:138-144.
    • (1972) Eur. J. Biochem , vol.30 , pp. 138-144
    • Saxholm, H.1    Zimmer, T.L.2    Laland, S.G.3
  • 37
    • 0025239615 scopus 로고
    • High-frequency conjugal plasmid transfer from gram-negative Escherichia coli to various gram-positive coryneform bacteria
    • Schäfer, A., J. Kalinowski, R. Simon, A. H. Seep-Feldhaus, and A. Puhler. 1990. High-frequency conjugal plasmid transfer from gram-negative Escherichia coli to various gram-positive coryneform bacteria. J. Bacteriol. 172: 1663-1666.
    • (1990) J. Bacteriol , vol.172 , pp. 1663-1666
    • Schäfer, A.1    Kalinowski, J.2    Simon, R.3    Seep-Feldhaus, A.H.4    Puhler, A.5
  • 38
    • 10444251153 scopus 로고    scopus 로고
    • Biosynthetic gene cluster of the herbicide phosphinothricin tripeptide from Streptomyces viridochromogenes Tü494
    • Schwartz, D., S. Berger, E. Heinzelmann, K. Muschko, K. Welzel, and W. Wohlleben. 2004. Biosynthetic gene cluster of the herbicide phosphinothricin tripeptide from Streptomyces viridochromogenes Tü494. Appl. Environ. Microbiol. 70:7093-7102.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 7093-7102
    • Schwartz, D.1    Berger, S.2    Heinzelmann, E.3    Muschko, K.4    Welzel, K.5    Wohlleben, W.6
  • 39
    • 0037524493 scopus 로고    scopus 로고
    • Nonribosomal peptides: From genes to products
    • Schwarzer, D., R. Finking, and M. A. Marahiel. 2003. Nonribosomal peptides: from genes to products. Nat. Prod. Rep. 20:275-287.
    • (2003) Nat. Prod. Rep , vol.20 , pp. 275-287
    • Schwarzer, D.1    Finking, R.2    Marahiel, M.A.3
  • 40
    • 1542425864 scopus 로고
    • Interaction of Rhizobium loti strain and host on the biosynthesis of unusual amino acids in leguminous plants
    • Shaw, G. J., D. B. Scott, and P. J. Ellingham. 1986. Interaction of Rhizobium loti strain and host on the biosynthesis of unusual amino acids in leguminous plants. Experientia 42:42-43.
    • (1986) Experientia , vol.42 , pp. 42-43
    • Shaw, G.J.1    Scott, D.B.2    Ellingham, P.J.3
  • 42
    • 4444252771 scopus 로고    scopus 로고
    • Initiation of surfactin biosynthesis and the role of the SrfD-thioesterase protein
    • Steller, S., A. Sokoll, C. Wilde, F. Bernhard, P. Franke, and J. Vater. 2004. Initiation of surfactin biosynthesis and the role of the SrfD-thioesterase protein. Biochemistry 43:11331-11343.
    • (2004) Biochemistry , vol.43 , pp. 11331-11343
    • Steller, S.1    Sokoll, A.2    Wilde, C.3    Bernhard, F.4    Franke, P.5    Vater, J.6
  • 44
    • 0032503564 scopus 로고    scopus 로고
    • Conformational analysis of reverse-turn constraints by N-methylation and N-hydroxylation of amide bonds in peptides and non-peptide mimetics
    • Takeuchi, Y., and G. R. Marshall. 1998. Conformational analysis of reverse-turn constraints by N-methylation and N-hydroxylation of amide bonds in peptides and non-peptide mimetics. J. Am. Chem. Soc. 120:5363-5372.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 5363-5372
    • Takeuchi, Y.1    Marshall, G.R.2
  • 45
    • 0020468391 scopus 로고
    • Studies on bacterial cell wall inhibitors. X. Properties of phosph-N-acetyl-muramoyl-pentapeptide-transferase in peptidoglycan synthesis of Bacillus megaterium and its inhibition by amphomycin
    • Tanaka, H., R. Oiwa, S. Matsukura, J. Inokoshi, and S. Omura. 1982. Studies on bacterial cell wall inhibitors. X. Properties of phosph-N-acetyl-muramoyl-pentapeptide-transferase in peptidoglycan synthesis of Bacillus megaterium and its inhibition by amphomycin. J. Antibiot. (Tokyo) 35:1216-1221.
    • (1982) J. Antibiot. (Tokyo) , vol.35 , pp. 1216-1221
    • Tanaka, H.1    Oiwa, R.2    Matsukura, S.3    Inokoshi, J.4    Omura, S.5
  • 46
    • 0041422181 scopus 로고    scopus 로고
    • Deciphering tuberactinomycin biosynthesis: Isolation, sequencing, and annotation of the viomycin biosynthetic gene cluster
    • Thomas, M. G., Y. A. Chan, and S. G. Ozanick. 2003. Deciphering tuberactinomycin biosynthesis: isolation, sequencing, and annotation of the viomycin biosynthetic gene cluster. Antimicrob. Agents Chemother. 47:2823-2830.
    • (2003) Antimicrob. Agents Chemother , vol.47 , pp. 2823-2830
    • Thomas, M.G.1    Chan, Y.A.2    Ozanick, S.G.3
  • 47
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 48
    • 0033856211 scopus 로고    scopus 로고
    • Friulimicins: Novel lipopeptide antibiotics with peptidoglycan synthesis inhibiting activity from Actinoplanes friuliensis sp. nov. II. Isolation and structural characterization
    • Vertesy, L., E. Ehlers, H. Kogler, M. Kurz, J. Meiwes, G. Seibert, M. Vogel, and P. Hammann. 2000. Friulimicins: novel lipopeptide antibiotics with peptidoglycan synthesis inhibiting activity from Actinoplanes friuliensis sp. nov. II. Isolation and structural characterization. J. Antibiot. (Tokyo) 53: 816-827.
    • (2000) J. Antibiot. (Tokyo) , vol.53 , pp. 816-827
    • Vertesy, L.1    Ehlers, E.2    Kogler, H.3    Kurz, M.4    Meiwes, J.5    Seibert, G.6    Vogel, M.7    Hammann, P.8
  • 49
    • 0025809486 scopus 로고
    • New pUC-derived cloning vectors with different selectable markers and DNA replication origins
    • Vieira, J., and J. Messing. 1991. New pUC-derived cloning vectors with different selectable markers and DNA replication origins. Gene 100:189-194.
    • (1991) Gene , vol.100 , pp. 189-194
    • Vieira, J.1    Messing, J.2
  • 50
    • 0036523418 scopus 로고    scopus 로고
    • Combinatorial biosynthesis of antibiotics: Challenges and opportunities
    • Walsh, C. T. 2002. Combinatorial biosynthesis of antibiotics: challenges and opportunities. Chembiochem 3:125-134.
    • (2002) Chembiochem , vol.3 , pp. 125-134
    • Walsh, C.T.1
  • 51
    • 0033743319 scopus 로고    scopus 로고
    • Identification of the coumermycin A(1) biosynthetic gene cluster of Streptomyces nshiriensia DSM 40489
    • Wang, Z. X., S. M. Li, and L. Heide. 2000. Identification of the coumermycin A(1) biosynthetic gene cluster of Streptomyces nshiriensia DSM 40489. Antimicrob. Agents Chemother. 44:3040-3048.
    • (2000) Antimicrob. Agents Chemother , vol.44 , pp. 3040-3048
    • Wang, Z.X.1    Li, S.M.2    Heide, L.3
  • 52
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 53
    • 0347298786 scopus 로고    scopus 로고
    • Zerbe, K., O. Pylypenko, F. Vitali, W. Zhang, S. Rouset, M. Heck, J. W. Vrijbloed, D. Bischoff, B. Bister, R. D. Sussmuth, S. Pelzer, W. Wohlleben, J. A. Robinson, and I. Schlichting. 30 August 2002. Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis. J. Biol. Chem. 277:47476-47485. [Epub ahead of print.]
    • Zerbe, K., O. Pylypenko, F. Vitali, W. Zhang, S. Rouset, M. Heck, J. W. Vrijbloed, D. Bischoff, B. Bister, R. D. Sussmuth, S. Pelzer, W. Wohlleben, J. A. Robinson, and I. Schlichting. 30 August 2002. Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis. J. Biol. Chem. 277:47476-47485. [Epub ahead of print.]
  • 54
    • 0030796661 scopus 로고    scopus 로고
    • Analysis of the syrP gene, which regulates syringomycin synthesis by Pseudomonas syringae pv. syringae
    • Zhang, J. H., N. B. Quigley, and D. C. Gross. 1997. Analysis of the syrP gene, which regulates syringomycin synthesis by Pseudomonas syringae pv. syringae. Appl. Environ. Microbiol. 63:2771-2778.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 2771-2778
    • Zhang, J.H.1    Quigley, N.B.2    Gross, D.C.3


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