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Volumn 17, Issue 10, 2010, Pages 1077-1083

N-Acylation during glidobactin biosynthesis by the tridomain nonribosomal peptide synthetase module GlbF

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A; BACTERIAL PROTEIN; CYCLOPEPTIDE; GLIDOBACTIN A; NON RIBOSOMAL PEPTIDE SYNTHASE; NON-RIBOSOMAL PEPTIDE SYNTHASE; PEPTIDE SYNTHASE;

EID: 78049413334     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2010.08.007     Document Type: Article
Times cited : (77)

References (28)
  • 1
    • 1642567934 scopus 로고    scopus 로고
    • Functional analysis of genes involved in the synthesis of syringolin A by Pseudomonas syringae pv. syringae B301D-R
    • H. Amrein, S. Makart, J. Granado, R. Shakya, J. Schneider-Pokorny, and R. Dudler Functional analysis of genes involved in the synthesis of syringolin A by Pseudomonas syringae pv. syringae B301D-R Mol. Plant Microbe Interact. 17 2004 90 97
    • (2004) Mol. Plant Microbe Interact. , vol.17 , pp. 90-97
    • Amrein, H.1    Makart, S.2    Granado, J.3    Shakya, R.4    Schneider-Pokorny, J.5    Dudler, R.6
  • 2
    • 29244459093 scopus 로고    scopus 로고
    • Natural products to drugs: Daptomycin and related lipopeptide antibiotics
    • R.H. Baltz, V. Miao, and S.K. Wrigley Natural products to drugs: daptomycin and related lipopeptide antibiotics Nat. Prod. Rep. 22 2005 717 741
    • (2005) Nat. Prod. Rep. , vol.22 , pp. 717-741
    • Baltz, R.H.1    Miao, V.2    Wrigley, S.K.3
  • 4
    • 66149090781 scopus 로고    scopus 로고
    • Synthetic and structural studies on syringolin A and B reveal critical determinants of selectivity and potency of proteasome inhibition
    • J. Clerc, M. Groll, D.J. Illich, A.S. Bachmann, R. Huber, B. Schellenberg, R. Dudler, and M. Kaiser Synthetic and structural studies on syringolin A and B reveal critical determinants of selectivity and potency of proteasome inhibition Proc. Natl. Acad. Sci. USA 106 2009 6507 6512
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6507-6512
    • Clerc, J.1    Groll, M.2    Illich, D.J.3    Bachmann, A.S.4    Huber, R.5    Schellenberg, B.6    Dudler, R.7    Kaiser, M.8
  • 5
    • 34547116228 scopus 로고    scopus 로고
    • The 1.8 A crystal structure of PA2412, an MbtH-like protein from the pyoverdine cluster of Pseudomonas aeruginosa
    • E.J. Drake, J. Cao, J. Qu, M.B. Shah, R.M. Straubinger, and A.M. Gulick The 1.8 A crystal structure of PA2412, an MbtH-like protein from the pyoverdine cluster of Pseudomonas aeruginosa J. Biol. Chem. 282 2007 20425 20434
    • (2007) J. Biol. Chem. , vol.282 , pp. 20425-20434
    • Drake, E.J.1    Cao, J.2    Qu, J.3    Shah, M.B.4    Straubinger, R.M.5    Gulick, A.M.6
  • 6
    • 78049413985 scopus 로고    scopus 로고
    • Farnet, C.M., Staffa, A., and Zazopoulos, E. (2007). US Patent 7,235,651
    • Farnet, C.M., Staffa, A., and Zazopoulos, E. (2007). US Patent 7,235,651.
  • 7
    • 0032562142 scopus 로고    scopus 로고
    • Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF
    • A.M. Gehring, I. Mori, and C.T. Walsh Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF Biochemistry 37 1998 2648 2659
    • (1998) Biochemistry , vol.37 , pp. 2648-2659
    • Gehring, A.M.1    Mori, I.2    Walsh, C.T.3
  • 9
    • 70350326295 scopus 로고    scopus 로고
    • Enzymatic tailoring of ornithine in the biosynthesis of the Rhizobium cyclic trihydroxamate siderophore vicibactin
    • J.R. Heemstra, C.T. Walsh, and E.S. Sattely Enzymatic tailoring of ornithine in the biosynthesis of the Rhizobium cyclic trihydroxamate siderophore vicibactin J. Am. Chem. Soc. 131 2009 15317 15329
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15317-15329
    • Heemstra, J.R.1    Walsh, C.T.2    Sattely, E.S.3
  • 10
    • 0023939492 scopus 로고
    • The formation of daptomycin by supplying decanoic acid to Streptomyces roseosporus cultures producing the antibiotic complex A21978C
    • F.M. Huber, R.L. Pieper, and A.J. Tietz The formation of daptomycin by supplying decanoic acid to Streptomyces roseosporus cultures producing the antibiotic complex A21978C J. Biotechnol. 7 1988 283 292
    • (1988) J. Biotechnol. , vol.7 , pp. 283-292
    • Huber, F.M.1    Pieper, R.L.2    Tietz, A.J.3
  • 11
    • 73249136918 scopus 로고    scopus 로고
    • SylC catalyzes ureido-bond formation during biosynthesis of the proteasome inhibitor syringolin A
    • H.J. Imker, C.T. Walsh, and W.M. Weust SylC catalyzes ureido-bond formation during biosynthesis of the proteasome inhibitor syringolin A J. Am. Chem. Soc. 131 2009 18263 18265
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 18263-18265
    • Imker, H.J.1    Walsh, C.T.2    Weust, W.M.3
  • 13
    • 39749169353 scopus 로고    scopus 로고
    • Harnessing the chemical activation inherent to carrier protein-bound thioesters for the characterization of lipopeptide fatty acid tailoring enzymes
    • F. Kopp, U. Linne, M. Oberthur, and M.A. Marahiel Harnessing the chemical activation inherent to carrier protein-bound thioesters for the characterization of lipopeptide fatty acid tailoring enzymes J. Am. Chem. Soc. 130 2008 2656 2666
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2656-2666
    • Kopp, F.1    Linne, U.2    Oberthur, M.3    Marahiel, M.A.4
  • 14
    • 34249053161 scopus 로고    scopus 로고
    • MbtH-like protein-mediated cross-talk between non-ribosomal peptide antibiotic and siderophore biosynthetic pathways in Streptomyces coelicolor M145
    • S. Lautru, D. Oves-Costales, J.L. Pernodet, and G.L. Challis MbtH-like protein-mediated cross-talk between non-ribosomal peptide antibiotic and siderophore biosynthetic pathways in Streptomyces coelicolor M145 Microbiology 153 2007 1405 1412
    • (2007) Microbiology , vol.153 , pp. 1405-1412
    • Lautru, S.1    Oves-Costales, D.2    Pernodet, J.L.3    Challis, G.L.4
  • 15
    • 78049383224 scopus 로고    scopus 로고
    • Numata, K., and Oka, M. (1992). Glidobactin PF-1 Peptide Antibioitics. U.S. Patent 5,096,884
    • Numata, K., and Oka, M. (1992). Glidobactin PF-1 Peptide Antibioitics. U.S. Patent 5,096,884.
  • 17
    • 0023798582 scopus 로고
    • Glidobactins A, B and C, new antitumor antibiotics. I. Production, isolation, chemical properties and biological activity
    • M. Oka, Y. Nishiyama, S. Ohta, H. Kamei, M. Konishi, T. Miyaki, T. Oki, and H. Kawaguchi Glidobactins A, B and C, new antitumor antibiotics. I. Production, isolation, chemical properties and biological activity J. Antibiot. (Tokyo) 41 1988 1331 1337
    • (1988) J. Antibiot. (Tokyo) , vol.41 , pp. 1331-1337
    • Oka, M.1    Nishiyama, Y.2    Ohta, S.3    Kamei, H.4    Konishi, M.5    Miyaki, T.6    Oki, T.7    Kawaguchi, H.8
  • 19
    • 0032501971 scopus 로고    scopus 로고
    • Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases
    • L.E.N. Quadri, P.H. Weinreb, M. Lei, M.M. Nakano, P. Zuber, and C.T. Walsh Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases Biochemistry 37 1998 1585 1595
    • (1998) Biochemistry , vol.37 , pp. 1585-1595
    • Quadri, L.E.N.1    Weinreb, P.H.2    Lei, M.3    Nakano, M.M.4    Zuber, P.5    Walsh, C.T.6
  • 20
    • 26944502019 scopus 로고    scopus 로고
    • Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs)
    • C. Rausch, T. Weber, O. Kohlbacher, W. Wohlleben, and D.H. Huson Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs) Nucleic Acids Res. 33 2005 5799 5808
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5799-5808
    • Rausch, C.1    Weber, T.2    Kohlbacher, O.3    Wohlleben, W.4    Huson, D.H.5
  • 21
    • 34250710858 scopus 로고    scopus 로고
    • Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution
    • C. Rausch, I. Hoof, T. Weber, W. Wohlleben, and D.H. Huson Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution BMC Evol. Biol. 7 2007 78
    • (2007) BMC Evol. Biol. , vol.7 , pp. 78
    • Rausch, C.1    Hoof, I.2    Weber, T.3    Wohlleben, W.4    Huson, D.H.5
  • 22
    • 34250212125 scopus 로고    scopus 로고
    • Identification of genes involved in the biosynthesis of the cytotoxic compound glidobactin from a soil bacterium
    • B. Schellenberg, L. Bigler, and R. Dudler Identification of genes involved in the biosynthesis of the cytotoxic compound glidobactin from a soil bacterium Environ. Microbiol. 9 2007 1640 1650
    • (2007) Environ. Microbiol. , vol.9 , pp. 1640-1650
    • Schellenberg, B.1    Bigler, L.2    Dudler, R.3
  • 23
    • 0032575648 scopus 로고    scopus 로고
    • Peptide bond formation in nonribosomal peptide biosynthesis - Catalytic role of the condensation domain
    • T. Stachelhaus, H.D. Mootz, V. Bergendahl, and M.A. Marahiel Peptide bond formation in nonribosomal peptide biosynthesis - catalytic role of the condensation domain J. Biol. Chem. 273 1998 22773 22781
    • (1998) J. Biol. Chem. , vol.273 , pp. 22773-22781
    • Stachelhaus, T.1    Mootz, H.D.2    Bergendahl, V.3    Marahiel, M.A.4
  • 24
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • T. Stachelhaus, H.D. Mootz, and M.A. Marahiel The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases Chem. Biol. 6 1999 493 505
    • (1999) Chem. Biol. , vol.6 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 25
    • 4444252771 scopus 로고    scopus 로고
    • Initiation of surfactin biosynthesis and the role of the SrfD-thioesterase protein
    • S. Steller, A. Sokoll, C. Wilde, F. Bernhard, P. Franke, and J. Vater Initiation of surfactin biosynthesis and the role of the SrfD-thioesterase protein Biochemistry 43 2004 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
  • 26
    • 2642616988 scopus 로고    scopus 로고
    • Syringolin, a novel peptide elicitor from Pseudomonas syringae pv. syringae that induces resistance to Pyricularia oryzae in rice
    • U. Waspi, D. Blanc, T. Winkler, P. Ruedi, and R. Dudler Syringolin, a novel peptide elicitor from Pseudomonas syringae pv. syringae that induces resistance to Pyricularia oryzae in rice Mol. Plant Microbe Interact. 11 1998 727 733
    • (1998) Mol. Plant Microbe Interact. , vol.11 , pp. 727-733
    • Waspi, U.1    Blanc, D.2    Winkler, T.3    Ruedi, P.4    Dudler, R.5
  • 27
    • 34249004256 scopus 로고    scopus 로고
    • Effects of deletions of mbtH-like genes on clorobiocin biosynthesis in Streptomyces coelicolor
    • M. Wolpert, B. Gust, B. Kammerer, and L. Heide Effects of deletions of mbtH-like genes on clorobiocin biosynthesis in Streptomyces coelicolor Microbiology 153 2007 1413 1423
    • (2007) Microbiology , vol.153 , pp. 1413-1423
    • Wolpert, M.1    Gust, B.2    Kammerer, B.3    Heide, L.4
  • 28
    • 0027096070 scopus 로고
    • Proposal of Burkholderia gen. nov. and transfer of seven species of the genus Pseudomonas homology group II to the new genus, with the type species Burkholderia cepacia (Palleroni and Holmes 1981) comb. nov
    • E. Yabuuchi, Y. Kosako, H. Oyaizu, I. Yano, H. Hotta, Y. Hashimoto, T. Ezaki, and M. Arakawa Proposal of Burkholderia gen. nov. and transfer of seven species of the genus Pseudomonas homology group II to the new genus, with the type species Burkholderia cepacia (Palleroni And Holmes 1981) comb. nov Microbiol. Immunol. 36 1992 1251 1275
    • (1992) Microbiol. Immunol. , vol.36 , pp. 1251-1275
    • Yabuuchi, E.1    Kosako, Y.2    Oyaizu, H.3    Yano, I.4    Hotta, H.5    Hashimoto, Y.6    Ezaki, T.7    Arakawa, M.8


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