메뉴 건너뛰기




Volumn 14, Issue 14, 2010, Pages 1433-1446

Biosynthetic pathways and engineering for bioactive natural products

Author keywords

Bioactive compound; Biosynthetic pathway; Gene cluster; Natural product; NRPS; PKS; Secondary metabolism

Indexed keywords

BIOSYNTHESIS; GENES; KETONES; PHYSIOLOGY;

EID: 77954915996     PISSN: 13852728     EISSN: None     Source Type: Journal    
DOI: 10.2174/138527210791616759     Document Type: Article
Times cited : (7)

References (95)
  • 1
    • 34247109045 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the last 25 years
    • Newman, D.J.; Cragg, G.M. Natural products as sources of new drugs over the last 25 years. J. Nat. Prod., 2007, 70, 461-477.
    • (2007) J. Nat. Prod , vol.70 , pp. 461-477
    • Newman, D.J.1    Cragg, G.M.2
  • 2
    • 44249098800 scopus 로고    scopus 로고
    • Natural products to drugs: Natural product-derived compounds in clinical trials
    • Butler, M.S. Natural products to drugs: natural product-derived compounds in clinical trials. Nat. Prod. Rep., 2008, 25, 475-516.
    • (2008) Nat. Prod. Rep , vol.25 , pp. 475-516
    • Butler, M.S.1
  • 3
    • 64049088221 scopus 로고    scopus 로고
    • The DEBS paradigm for type I modular polyketide synthases and beyond
    • Katz, L. The DEBS paradigm for type I modular polyketide synthases and beyond. Methods. Enzymol., 2009, 459, 113-142.
    • (2009) Methods. Enzymol , vol.459 , pp. 113-142
    • Katz, L.1
  • 4
    • 39549092885 scopus 로고    scopus 로고
    • Advances in polyketide synthase structure and function
    • Van Lanen, S.G.; Shen, B. Advances in polyketide synthase structure and function. Curr. Opin. Drug. Discov. Devel., 2008, 11, 186-195.
    • (2008) Curr. Opin. Drug. Discov. Devel , vol.11 , pp. 186-195
    • van Lanen, S.G.1    Shen, B.2
  • 5
    • 44049083124 scopus 로고    scopus 로고
    • Protein-protein interactions in multienzyme megasynthetases
    • Weissman, K.J.; Muller, R. Protein-protein interactions in multienzyme megasynthetases. Chembiochemistry, 2008, 9, 826-848.
    • (2008) Chembiochemistry , vol.9 , pp. 826-848
    • Weissman, K.J.1    Muller, R.2
  • 6
    • 4043136597 scopus 로고    scopus 로고
    • Reactions catalyzed by mature and recombinant nonribosomal peptide synthetases
    • Linne, U.; Marahiel, M.A. Reactions catalyzed by mature and recombinant nonribosomal peptide synthetases. Methods. Enzymol., 2004, 388, 293-315.
    • (2004) Methods. Enzymol , vol.388 , pp. 293-315
    • Linne, U.1    Marahiel, M.A.2
  • 7
    • 0032475992 scopus 로고    scopus 로고
    • Harnessing the biosynthetic code: Combinations, permutations, and mutations
    • Cane, D.E.; Walsh, C.T.; Khosla, C. Harnessing the biosynthetic code: combinations, permutations, and mutations. Science, 1998, 282, 63-68.
    • (1998) Science , vol.282 , pp. 63-68
    • Cane, D.E.1    Walsh, C.T.2    Khosla, C.3
  • 9
    • 0026415106 scopus 로고
    • Modular organization of genes required for complex polyketide biosynthesis
    • Donadio, S.; Staver, M.J.; McAlpine, J.B.; Swanson, S.J.; Katz, L. Modular organization of genes required for complex polyketide biosynthesis. Science, 1991, 252, 675-679.
    • (1991) Science , vol.252 , pp. 675-679
    • Donadio, S.1    Staver, M.J.2    McAlpine, J.B.3    Swanson, S.J.4    Katz, L.5
  • 10
    • 0025081416 scopus 로고
    • An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea
    • Cortes, J.; Haydock, S.F.; Roberts, G.A.; Bevitt, D.J.; Leadlay, P.F. An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea. Nature, 1990, 348, 176-178.
    • (1990) Nature , vol.348 , pp. 176-178
    • Cortes, J.1    Haydock, S.F.2    Roberts, G.A.3    Bevitt, D.J.4    Leadlay, P.F.5
  • 12
    • 58549095504 scopus 로고    scopus 로고
    • Unusual chemistry in the biosynthesis of the antibiotic chondrochlorens
    • Rachid, S.; Scharfe, M.; Blocker, H.; Weissman, K.J.; Muller, R. Unusual chemistry in the biosynthesis of the antibiotic chondrochlorens. Chem. Biol., 2009, 16, 70-81.
    • (2009) Chem. Biol , vol.16 , pp. 70-81
    • Rachid, S.1    Scharfe, M.2    Blocker, H.3    Weissman, K.J.4    Muller, R.5
  • 13
    • 0034723333 scopus 로고    scopus 로고
    • Cloning and heterologous expression of the epothilone gene cluster
    • Tang, L.; Shah, S.; Chung, L.; Carney, J.; Katz, L.; Khosla, C.; Julien, B. Cloning and heterologous expression of the epothilone gene cluster. Science, 2000, 287, 640-642.
    • (2000) Science , vol.287 , pp. 640-642
    • Tang, L.1    Shah, S.2    Chung, L.3    Carney, J.4    Katz, L.5    Khosla, C.6    Julien, B.7
  • 14
    • 56749157843 scopus 로고    scopus 로고
    • Unprecedented biological cyclopropanation in the biosynthesis of FR-900848
    • Tokiwano, T.; Watanabe, H.; Seo, T.; Oikawa, H. Unprecedented biological cyclopropanation in the biosynthesis of FR-900848. Chem. Commun., 2008, 6016-6018.
    • (2008) Chem. Commun , pp. 6016-6018
    • Tokiwano, T.1    Watanabe, H.2    Seo, T.3    Oikawa, H.4
  • 15
    • 63449092823 scopus 로고    scopus 로고
    • A free-standing condensation enzyme catalyzing ester bond formation in C-1027 biosynthesis
    • Lin, S.; Van Lanen, S.G.; Shen, B. A free-standing condensation enzyme catalyzing ester bond formation in C-1027 biosynthesis. Proc. Natl. Acad. Sci. USA, 2009, 106, 4183-4188.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4183-4188
    • Lin, S.1    van Lanen, S.G.2    Shen, B.3
  • 17
    • 65249139526 scopus 로고    scopus 로고
    • An iterative nonribosomal peptide synthetase assembles the pyrrole-amide antibiotic congocidine in Streptomyces ambofaciens
    • Juguet, M.; Lautru, S.; Francou, F.X.; Nezbedova, S.; Leblond, P.; Gondry, M.; Pernodet, J.L. An iterative nonribosomal peptide synthetase assembles the pyrrole-amide antibiotic congocidine in Streptomyces ambofaciens. Chem. Biol., 2009, 16, 421-431.
    • (2009) Chem. Biol , vol.16 , pp. 421-431
    • Juguet, M.1    Lautru, S.2    Francou, F.X.3    Nezbedova, S.4    Leblond, P.5    Gondry, M.6    Pernodet, J.L.7
  • 18
    • 58149310896 scopus 로고    scopus 로고
    • Cloning and molecular characterization of the gene encoding the Aureobasidin A biosynthesis complex in Aureobasidium pullulans BP-1938
    • Slightom, J.L.; Metzger, B.P.; Luu, H.T.; Elhammer, A.P. Cloning and molecular characterization of the gene encoding the Aureobasidin A biosynthesis complex in Aureobasidium pullulans BP-1938. Gene, 2009, 431, 67-79.
    • (2009) Gene , vol.431 , pp. 67-79
    • Slightom, J.L.1    Metzger, B.P.2    Luu, H.T.3    Elhammer, A.P.4
  • 19
    • 0036905773 scopus 로고    scopus 로고
    • Ways of assembling complex natural products on modular nonribosomal peptide synthetases
    • Mootz, H.D.; Schwarzer, D.; Marahiel, M.A. Ways of assembling complex natural products on modular nonribosomal peptide synthetases. Chembiochemistry, 2002, 3, 490-504.
    • (2002) Chembiochemistry , vol.3 , pp. 490-504
    • Mootz, H.D.1    Schwarzer, D.2    Marahiel, M.A.3
  • 20
    • 9244234513 scopus 로고    scopus 로고
    • Biosynthesis of nonribosomal peptides1
    • Finking, R.; Marahiel, M.A. Biosynthesis of nonribosomal peptides1. Annu. Rev. Microbiol., 2004, 58, 453-488.
    • (2004) Annu. Rev. Microbiol , vol.58 , pp. 453-488
    • Finking, R.1    Marahiel, M.A.2
  • 21
    • 33847112437 scopus 로고    scopus 로고
    • Aminoacyl-Coenzyme A synthesis catalyzed by adenylation domains
    • Linne, U.; Schafer, A.; Stubbs, M.T.; Marahiel, M.A. Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains. FEBS. Lett., 2007, 581, 905-910.
    • (2007) FEBS. Lett , vol.581 , pp. 905-910
    • Linne, U.1    Schafer, A.2    Stubbs, M.T.3    Marahiel, M.A.4
  • 22
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • Stachelhaus, T.; Mootz, H.D.; Marahiel, M.A. The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases. Chem. Biol., 1999, 6, 493-505.
    • (1999) Chem. Biol , vol.6 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 23
    • 0030756031 scopus 로고    scopus 로고
    • Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S
    • Conti, E.; Stachelhaus, T.; Marahiel, M.A.; Brick, P. Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S. EMBO. J., 1997, 16, 4174-4183.
    • (1997) EMBO. J , vol.16 , pp. 4174-4183
    • Conti, E.1    Stachelhaus, T.2    Marahiel, M.A.3    Brick, P.4
  • 24
    • 33747799012 scopus 로고    scopus 로고
    • Characterization of the cereulide NRPS alpha-hydroxy acid specifying modules: Activation of alpha-keto acids and chiral reduction on the assembly line
    • Magarvey, N.A.; Ehling-Schulz, M.; Walsh, C.T., Characterization of the cereulide NRPS alpha-hydroxy acid specifying modules: activation of alpha-keto acids and chiral reduction on the assembly line. J. Am. Chem. Soc., 2006, 128, 10698-10699.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10698-10699
    • Magarvey, N.A.1    Ehling-Schulz, M.2    Walsh, C.T.3
  • 26
    • 34548496029 scopus 로고    scopus 로고
    • Identification of a biosynthetic gene cluster and the six associated lipopeptides involved in swarming motility of Pseudomonas syringae pv. tomato DC3000
    • Berti, A.D.; Greve, N.J.; Christensen, Q.H.; Thomas, M.G. Identification of a biosynthetic gene cluster and the six associated lipopeptides involved in swarming motility of Pseudomonas syringae pv. tomato DC3000. J. Bacteriol., 2007, 189, 6312-6323.
    • (2007) J. Bacteriol , vol.189 , pp. 6312-6323
    • Berti, A.D.1    Greve, N.J.2    Christensen, Q.H.3    Thomas, M.G.4
  • 27
    • 55149116296 scopus 로고    scopus 로고
    • Tandem heterocyclization domains in a nonribosomal peptide synthetase essential for siderophore biosynthesis in Vibrio anguillarum
    • Di Lorenzo, M.; Stork, M.; Naka, H.; Tolmasky, M.E.; Crosa, J.H. Tandem heterocyclization domains in a nonribosomal peptide synthetase essential for siderophore biosynthesis in Vibrio anguillarum. Biometals, 2008, 21, 635-648.
    • (2008) Biometals , vol.21 , pp. 635-648
    • Di Lorenzo, M.1    Stork, M.2    Naka, H.3    Tolmasky, M.E.4    Crosa, J.H.5
  • 28
    • 0033574774 scopus 로고    scopus 로고
    • Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis
    • Belshaw, P.J.; Walsh, C.T.; Stachelhaus, T. Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis. Science, 1999, 284, 486-489.
    • (1999) Science , vol.284 , pp. 486-489
    • Belshaw, P.J.1    Walsh, C.T.2    Stachelhaus, T.3
  • 29
    • 0033118907 scopus 로고    scopus 로고
    • Thiazole and oxazole peptides: Biosynthesis and molecular machinery
    • Roy, R.S.; Gehring, A.M.; Milne, J.C.; Belshaw, P.J.; Walsh, C.T., Thiazole and oxazole peptides: biosynthesis and molecular machinery. Nat. Prod. Rep., 1999, 16, 249-263.
    • (1999) Nat. Prod. Rep , vol.16 , pp. 249-263
    • Roy, R.S.1    Gehring, A.M.2    Milne, J.C.3    Belshaw, P.J.4    Walsh, C.T.5
  • 30
    • 64149117037 scopus 로고    scopus 로고
    • Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway
    • Claxton, H.B.; Akey, D.L.; Silver, M.K.; Admiraal, S.J.; Smith, J.L. Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway. J. Biol. Chem., 2009, 284, 5021-5029.
    • (2009) J. Biol. Chem , vol.284 , pp. 5021-5029
    • Claxton, H.B.1    Akey, D.L.2    Silver, M.K.3    Admiraal, S.J.4    Smith, J.L.5
  • 31
    • 33846296304 scopus 로고    scopus 로고
    • The iterative gramicidin s thioesterase catalyzes peptide ligation and cyclization
    • Hoyer, K.M.; Mahlert, C.; Marahiel, M.A. The iterative gramicidin s thioesterase catalyzes peptide ligation and cyclization. Chem. Biol., 2007, 14, 13-22.
    • (2007) Chem. Biol , vol.14 , pp. 13-22
    • Hoyer, K.M.1    Mahlert, C.2    Marahiel, M.A.3
  • 32
    • 0034648798 scopus 로고    scopus 로고
    • Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase
    • Trauger, J.W.; Kohli, R.M.; Mootz, H.D.; Marahiel, M.A.; Walsh, C.T. Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase. Nature, 2000, 407, 215-218.
    • (2000) Nature , vol.407 , pp. 215-218
    • Trauger, J.W.1    Kohli, R.M.2    Mootz, H.D.3    Marahiel, M.A.4    Walsh, C.T.5
  • 34
    • 21144439895 scopus 로고    scopus 로고
    • The biosynthesis of vancomycin-type glycopeptide antibiotics--a model for oxidative side-chain cross-linking by oxygenases coupled to the action of peptide synthetases
    • Bischoff, D.; Bister, B.; Bertazzo, M.; Pfeifer, V.; Stegmann, E.; Nicholson, G. J.; Keller, S.; Pelzer, S.; Wohlleben, W.; Sussmuth, R.D. The biosynthesis of vancomycin-type glycopeptide antibiotics--a model for oxidative side-chain cross-linking by oxygenases coupled to the action of peptide synthetases. Chembiochemistry, 2005, 6, 267-272.
    • (2005) Chembiochemistry , vol.6 , pp. 267-272
    • Bischoff, D.1    Bister, B.2    Bertazzo, M.3    Pfeifer, V.4    Stegmann, E.5    Nicholson, G.J.6    Keller, S.7    Pelzer, S.8    Wohlleben, W.9    Sussmuth, R.D.10
  • 36
    • 36448952357 scopus 로고    scopus 로고
    • Biosynthetic tailoring of microcin E492m: Post-translational modification affords an antibacterial siderophore-peptide conjugate
    • Nolan, E.M.; Fischbach, M.A.; Koglin, A.; Walsh, C.T. Biosynthetic tailoring of microcin E492m: post-translational modification affords an antibacterial siderophore-peptide conjugate. J. Am. Chem. Soc., 2007, 129, 14336-14347.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 14336-14347
    • Nolan, E.M.1    Fischbach, M.A.2    Koglin, A.3    Walsh, C.T.4
  • 37
    • 64249100988 scopus 로고    scopus 로고
    • Biosynthesis and genetic engineering of lipopeptides in Streptomyces roseosporus
    • Baltz, R.H. Biosynthesis and genetic engineering of lipopeptides in Streptomyces roseosporus. Methods. Enzymol., 2009, 458, 511-531.
    • (2009) Methods. Enzymol , vol.458 , pp. 511-531
    • Baltz, R.H.1
  • 38
    • 30844455997 scopus 로고    scopus 로고
    • Combinatorial biosynthesis of lipopeptide antibiotics in Streptomyces roseosporus
    • Baltz, R.H.; Brian, P.; Miao, V.; Wrigley, S.K. Combinatorial biosynthesis of lipopeptide antibiotics in Streptomyces roseosporus. J. Ind. Microbiol. Biotechnol., 2006, 33, 66-74.
    • (2006) J. Ind. Microbiol. Biotechnol , vol.33 , pp. 66-74
    • Baltz, R.H.1    Brian, P.2    Miao, V.3    Wrigley, S.K.4
  • 39
    • 67749113468 scopus 로고    scopus 로고
    • Li,C. Thiostrepton biosynthesis: Prototype for a new family of bacteriocins
    • Kelly, W.L.; Pan, L.; Li,C. Thiostrepton biosynthesis: prototype for a new family of bacteriocins. J. Am. Chem. Soc., 2009, 131, 4327-4334.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 4327-4334
    • Kelly, W.L.1    Pan, L.2
  • 40
    • 60549109637 scopus 로고    scopus 로고
    • Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications
    • Liao, R.; Duan, L.; Lei, C.; Pan, H.; Ding, Y.; Zhang, Q.; Chen, D.; Shen, B.; Yu, Y.; Liu, W., Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications. Chem. Biol., 2009, 16, 141-147.
    • (2009) Chem. Biol , vol.16 , pp. 141-147
    • Liao, R.1    Duan, L.2    Lei, C.3    Pan, H.4    Ding, Y.5    Zhang, Q.6    Chen, D.7    Shen, B.8    Yu, Y.9    Liu, W.10
  • 41
    • 17344375809 scopus 로고    scopus 로고
    • Studies on the biosynthesis of thiostrepton: 4-(1-hydroxyethyl)quinoline-2-carboxylate as a free intermediate on the pathway to the quinaldic acid moiety
    • Priestley, N.D.; Smith, T.M.; Shipley, P.R.; Floss, H.G. Studies on the biosynthesis of thiostrepton: 4-(1-hydroxyethyl)quinoline-2-carboxylate as a free intermediate on the pathway to the quinaldic acid moiety. Bioorg. Med. Chem., 1996, 4, 1135-1147.
    • (1996) Bioorg. Med. Chem , vol.4 , pp. 1135-1147
    • Priestley, N.D.1    Smith, T.M.2    Shipley, P.R.3    Floss, H.G.4
  • 43
    • 0035673048 scopus 로고    scopus 로고
    • The biosynthetic gene cluster for the anticancer drug bleomycin from Streptomyces verticillus ATCC15003 as a model for hybrid peptide-polyketide natural product biosynthesis
    • Shen, B.; Du, L.; Sanchez, C.; Edwards, D.J.; Chen, M.; Murrell, J.M. The biosynthetic gene cluster for the anticancer drug bleomycin from Streptomyces verticillus ATCC15003 as a model for hybrid peptide-polyketide natural product biosynthesis. J. Ind. Microbiol. Biotechnol., 2001, 27, 378-385.
    • (2001) J. Ind. Microbiol. Biotechnol , vol.27 , pp. 378-385
    • Shen, B.1    Du, L.2    Sanchez, C.3    Edwards, D.J.4    Chen, M.5    Murrell, J.M.6
  • 44
    • 0033835373 scopus 로고    scopus 로고
    • The biosynthetic gene cluster for the antitumor drug bleomycin from Streptomyces verticillus ATCC15003 supporting functional interactions between nonribosomal peptide synthetases and a polyketide synthase
    • Du, L.; Sanchez, C.; Chen, M.; Edwards, D.J.; Shen, B. The biosynthetic gene cluster for the antitumor drug bleomycin from Streptomyces verticillus ATCC15003 supporting functional interactions between nonribosomal peptide synthetases and a polyketide synthase. Chem. Biol., 2000, 7, 623-642.
    • (2000) Chem. Biol , vol.7 , pp. 623-642
    • Du, L.1    Sanchez, C.2    Chen, M.3    Edwards, D.J.4    Shen, B.5
  • 46
    • 33745949592 scopus 로고    scopus 로고
    • Isolation and characterization of meridamycin biosynthetic gene cluster from Streptomyces sp. NRRL 30748
    • He, M.; Haltli, B.; Summers, M.; Feng, X.; Hucul, J. Isolation and characterization of meridamycin biosynthetic gene cluster from Streptomyces sp. NRRL 30748. Gene, 2006, 377, 109-118.
    • (2006) Gene , vol.377 , pp. 109-118
    • He, M.1    Haltli, B.2    Summers, M.3    Feng, X.4    Hucul, J.5
  • 47
    • 39149122159 scopus 로고    scopus 로고
    • Molecular analysis of the kirromycin biosynthetic gene cluster revealed beta-alanine as precursor of the pyridone moiety
    • Weber, T.; Laiple, K.J.; Pross, E.K.; Textor, A.; Grond, S.; Welzel, K.; Pelzer, S.; Vente, A.; Wohlleben, W. Molecular analysis of the kirromycin biosynthetic gene cluster revealed beta-alanine as precursor of the pyridone moiety. Chem. Biol., 2008, 15, 175-188.
    • (2008) Chem. Biol , vol.15 , 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
  • 48
    • 57449094594 scopus 로고    scopus 로고
    • The biosynthetic gene cluster of zorbamycin, a member of the bleomycin family of antitumor antibiotics, from Streptomyces flavoviridis ATCC 21892
    • Galm, U.; Wendt-Pienkowski, E.; Wang, L.; George, N.P.; Oh, T.J.; Yi, F.; Tao, M.; Coughlin, J.M.; Shen, B. The biosynthetic gene cluster of zorbamycin, a member of the bleomycin family of antitumor antibiotics, from Streptomyces flavoviridis ATCC 21892. Mol. Biosyst., 2009, 5, 77-90.
    • (2009) Mol. Biosyst , vol.5 , pp. 77-90
    • Galm, U.1    Wendt-Pienkowski, E.2    Wang, L.3    George, N.P.4    Oh, T.J.5    Yi, F.6    Tao, M.7    Coughlin, J.M.8    Shen, B.9
  • 49
    • 33845708150 scopus 로고    scopus 로고
    • New antibiotics from bacterial natural products
    • Clardy, J.; Fischbach, M.A.; Walsh, C.T. New antibiotics from bacterial natural products. Nat. Biotechnol., 2006, 24, 1541-1550.
    • (2006) Nat. Biotechnol , vol.24 , pp. 1541-1550
    • Clardy, J.1    Fischbach, M.A.2    Walsh, C.T.3
  • 50
    • 10044241785 scopus 로고    scopus 로고
    • Engineered biosynthesis of polyketides in heterologous hosts
    • Rude, M.A., Khosla, C. Engineered biosynthesis of polyketides in heterologous hosts. Chem. Eng. Sci., 2004, 59, 4693-4701.
    • (2004) Chem. Eng. Sci , vol.59 , pp. 4693-4701
    • Rude, M.A.1    Khosla, C.2
  • 51
    • 0035102454 scopus 로고    scopus 로고
    • Biosynthesis of polyketides in heterologous hosts
    • Pfeifer, B.A.; Khosla, C. Biosynthesis of polyketides in heterologous hosts. Microbiol. Mol. Biol. Rev., 2001, 65, 106-118.
    • (2001) Microbiol. Mol. Biol. Rev , vol.65 , pp. 106-118
    • Pfeifer, B.A.1    Khosla, C.2
  • 53
    • 15744370033 scopus 로고    scopus 로고
    • Heterologous expression of a myxobacterial natural products assembly line in pseudomonads via red/ET recombineering
    • Wenzel, S.C.; Gross, F.; Zhang, Y.; Fu, J.; Stewart, A. F.; Muller, R. Heterologous expression of a myxobacterial natural products assembly line in pseudomonads via red/ET recombineering. Chem. Biol., 2005, 12, 349-356.
    • (2005) Chem. Biol , vol.12 , pp. 349-356
    • Wenzel, S.C.1    Gross, F.2    Zhang, Y.3    Fu, J.4    Stewart, A.F.5    Muller, R.6
  • 54
    • 59849119654 scopus 로고    scopus 로고
    • Recombineering: A homologous recombination-based method of genetic engineering
    • Sharan, S.K.; Thomason, L.C.; Kuznetsov, S.G.; Court, D.L. Recombineering: a homologous recombination-based method of genetic engineering. Nat. Protoc., 2009, 4, 206-223.
    • (2009) Nat. Protoc , vol.4 , pp. 206-223
    • Sharan, S.K.1    Thomason, L.C.2    Kuznetsov, S.G.3    Court, D.L.4
  • 55
    • 0031664853 scopus 로고    scopus 로고
    • A new logic for DNA engineering using recombination in Escherichia coli
    • Zhang, Y.; Buchholz, F.; Muyrers, J.P.; Stewart, A.F. A new logic for DNA engineering using recombination in Escherichia coli. Nat. Genet., 1998, 20, 123-128.
    • (1998) Nat. Genet , vol.20 , pp. 123-128
    • Zhang, Y.1    Buchholz, F.2    Muyrers, J.P.3    Stewart, A.F.4
  • 56
    • 0037452723 scopus 로고    scopus 로고
    • PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin
    • Gust, B.; Challis, G.L.; Fowler, K.; Kieser, T.; Chater, K.F. PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin. Proc. Natl. Acad. Sci. USA, 2003, 100, 1541-1546.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1541-1546
    • Gust, B.1    Challis, G.L.2    Fowler, K.3    Kieser, T.4    Chater, K.F.5
  • 57
    • 0035793858 scopus 로고    scopus 로고
    • Biosynthesis of complex polyketides in a metabolically engineered strain of
    • Pfeifer, B.A.; Admiraal, S.J.; Gramajo, H.; Cane, D.E.; Khosla, C. Biosynthesis of complex polyketides in a metabolically engineered strain of E. coli. Science, 2001, 291, 1790-1792.
    • (2001) E. Coli. Science , vol.291 , pp. 1790-1792
    • Pfeifer, B.A.1    Admiraal, S.J.2    Gramajo, H.3    Cane, D.E.4    Khosla, C.5
  • 58
    • 0034724272 scopus 로고    scopus 로고
    • Heterologous expression in Escherichia coli of the first module of the nonribosomal peptide synthetase for chloroeremomycin, a vancomycin-type glycopeptide antibiotic
    • Trauger, J. W.; Walsh, C. T. Heterologous expression in Escherichia coli of the first module of the nonribosomal peptide synthetase for chloroeremomycin, a vancomycin-type glycopeptide antibiotic. Proc. Natl. Acad. Sci. USA, 2000, 97, 3112-3117.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3112-3117
    • Trauger, J.W.1    Walsh, C.T.2
  • 59
    • 64349117410 scopus 로고    scopus 로고
    • Plasmid-borne gene cluster assemblage and heterologous biosynthesis of nonribosomal peptides in Escherichia coli
    • Watanabe, K.; Praseuth, A.P.; Praseuth, M.B.; Hotta, K. Plasmid-borne gene cluster assemblage and heterologous biosynthesis of nonribosomal peptides in Escherichia coli. Methods Enzymol., 2009, 458, 379-399.
    • (2009) Methods Enzymol , vol.458 , pp. 379-399
    • Watanabe, K.1    Praseuth, A.P.2    Praseuth, M.B.3    Hotta, K.4
  • 62
    • 0033591447 scopus 로고    scopus 로고
    • Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis
    • Kennedy, J.; Auclair, K.; Kendrew, S.G.; Park, C.; Vederas, J.C.; Hutchinson, C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science, 1999, 284, 1368-1372.
    • (1999) Science , vol.284 , pp. 1368-1372
    • Kennedy, J.1    Auclair, K.2    Kendrew, S.G.3    Park, C.4    Vederas, J.C.5    Hutchinson, C.R.6
  • 63
    • 0041816073 scopus 로고    scopus 로고
    • Enhancement and selective production of phoslactomycin B, a protein phosphatase IIa inhibitor, through identification and engineering of the corresponding biosynthetic gene cluster
    • Palaniappan, N.; Kim, B.S.; Sekiyama, Y.; Osada, H.; Reynolds, K.A. Enhancement and selective production of phoslactomycin B, a protein phosphatase IIa inhibitor, through identification and engineering of the corresponding biosynthetic gene cluster. J. Biol. Chem., 2003, 278, 35552-35557.
    • (2003) J. Biol. Chem , vol.278 , pp. 35552-35557
    • Palaniappan, N.1    Kim, B.S.2    Sekiyama, Y.3    Osada, H.4    Reynolds, K.A.5
  • 64
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D.; Weinberg, R.A. The hallmarks of cancer. Cell., 2000, 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 65
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal, A.; Thao, L.; Sensintaffar, J.; Zhang, L.; Boehm, M.F.; Fritz, L.C.; Burrows, F.J. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature, 2003, 425, 407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3    Zhang, L.4    Boehm, M.F.5    Fritz, L.C.6    Burrows, F.J.7
  • 67
    • 33646376411 scopus 로고    scopus 로고
    • Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells
    • Yilmaz, O.H.; Valdez, R.; Theisen, B.K.; Guo, W.; Ferguson, D.O.; Wu, H.; Morrison, S.J. Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells. Nature, 2006, 441, 475-482.
    • (2006) Nature , vol.441 , pp. 475-482
    • Yilmaz, O.H.1    Valdez, R.2    Theisen, B.K.3    Guo, W.4    Ferguson, D.O.5    Wu, H.6    Morrison, S.J.7
  • 69
    • 37549071045 scopus 로고    scopus 로고
    • Drug discovery beyond the 'rule-of-five'
    • Zhang, M.Q.; Wilkinson, B. Drug discovery beyond the 'rule-of-five'. Curr. Opin. Biotechnol., 2007, 18, 478-488.
    • (2007) Curr. Opin. Biotechnol , vol.18 , pp. 478-488
    • Zhang, M.Q.1    Wilkinson, B.2
  • 70
    • 31044442400 scopus 로고    scopus 로고
    • Harnessing the potential of communication-mediating domains for the biocombinatorial synthesis of nonribosomal peptides
    • Hahn, M.; Stachelhaus, T. Harnessing the potential of communication-mediating domains for the biocombinatorial synthesis of nonribosomal peptides. Proc. Natl. Acad. Sci. USA, 2006, 103, 275-280.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 275-280
    • Hahn, M.1    Stachelhaus, T.2
  • 71
    • 8144230760 scopus 로고    scopus 로고
    • Selective interaction between nonribosomal peptide synthetases is facilitated by short communication-mediating domains
    • Hahn, M.; Stachelhaus, T. Selective interaction between nonribosomal peptide synthetases is facilitated by short communication-mediating domains. Proc. Natl. Acad. Sci. USA, 2004, 101, 15585-15590.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15585-15590
    • Hahn, M.1    Stachelhaus, T.2
  • 72
    • 0033618459 scopus 로고    scopus 로고
    • Analysis of engineered multifunctional peptide synthetases. Enzymatic characterization of surfactin synthetase domains in hybrid bimodular systems
    • Symmank, H.; Saenger, W.; Bernhard, F. Analysis of engineered multifunctional peptide synthetases. Enzymatic characterization of surfactin synthetase domains in hybrid bimodular systems. J. Biol. Chem., 1999, 274, 21581-21588.
    • (1999) J. Biol. Chem , vol.274 , pp. 21581-21588
    • Symmank, H.1    Saenger, W.2    Bernhard, F.3
  • 74
    • 48749083335 scopus 로고    scopus 로고
    • Crystal structure of the termination module of a nonribosomal peptide synthetase
    • Tanovic, A.; Samel, S.A.; Essen, L.O.; Marahiel, M.A. Crystal structure of the termination module of a nonribosomal peptide synthetase. Science, 2008, 321, 659-663.
    • (2008) Science , vol.321 , pp. 659-663
    • Tanovic, A.1    Samel, S.A.2    Essen, L.O.3    Marahiel, M.A.4
  • 75
    • 0034705130 scopus 로고    scopus 로고
    • Construction of hybrid peptide synthetases by module and domain fusions
    • Mootz, H. D.; Schwarzer, D.; Marahiel, M. A. Construction of hybrid peptide synthetases by module and domain fusions. Proc. Natl. Acad. Sci. USA, 2000, 97, 5848-5853.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5848-5853
    • Mootz, H.D.1    Schwarzer, D.2    Marahiel, M.A.3
  • 76
    • 34547547069 scopus 로고    scopus 로고
    • Directed evolution can rapidly improve the activity of chimeric assembly-line enzymes
    • Fischbach, M. A.; Lai, J. R.; Roche, E. D.; Walsh, C. T.; Liu, D. R. Directed evolution can rapidly improve the activity of chimeric assembly-line enzymes. Proc. Natl. Acad. Sci. USA, 2007, 104, 11951-11956.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11951-11956
    • Fischbach, M.A.1    Lai, J.R.2    Roche, E.D.3    Walsh, C.T.4    Liu, D.R.5
  • 77
    • 34547409782 scopus 로고    scopus 로고
    • Directed evolution of aryl carrier proteins in the enterobactin synthetase
    • Zhou, Z.; Lai, J.R.; Walsh, C.T. Directed evolution of aryl carrier proteins in the enterobactin synthetase. Proc. Natl. Acad. Sci. USA, 2007, 104, 11621-11626.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11621-11626
    • Zhou, Z.1    Lai, J.R.2    Walsh, C.T.3
  • 79
    • 0034659816 scopus 로고    scopus 로고
    • Coelichelin, a new peptide siderophore encoded by the Streptomyces coelicolor genome: Structure prediction from the sequence of its non-ribosomal peptide synthetase
    • Challis, G.L.; Ravel, J. Coelichelin, a new peptide siderophore encoded by the Streptomyces coelicolor genome: structure prediction from the sequence of its non-ribosomal peptide synthetase. FEMS. Microbiol. Lett., 2000, 187, 111-114.
    • (2000) FEMS. Microbiol. Lett , vol.187 , pp. 111-114
    • Challis, G.L.1    Ravel, J.2
  • 80
    • 27544477567 scopus 로고    scopus 로고
    • Discovery of a new peptide natural product by Streptomyces coelicolor genome mining
    • Lautru, S.; Deeth, R.J.; Bailey, L.M.; Challis, G.L. Discovery of a new peptide natural product by Streptomyces coelicolor genome mining. Nat. Chem. Biol., 2005, 1, 265-269.
    • (2005) Nat. Chem. Biol , vol.1 , pp. 265-269
    • Lautru, S.1    Deeth, R.J.2    Bailey, L.M.3    Challis, G.L.4
  • 83
    • 17844407663 scopus 로고    scopus 로고
    • Microbial genomics as a guide to drug discovery and structural elucidation: ECO-02301, a novel antifungal agent, as an example
    • McAlpine, J.B.; Bachmann, B.O.; Piraee, M.; Tremblay, S.; Alarco, A.M.; Zazopoulos, E.; Farnet, C.M. Microbial genomics as a guide to drug discovery and structural elucidation: ECO-02301, a novel antifungal agent, as an example. J. Nat. Prod., 2005, 68, 493-496.
    • (2005) J. Nat. Prod , vol.68 , pp. 493-496
    • McAlpine, J.B.1    Bachmann, B.O.2    Piraee, M.3    Tremblay, S.4    Alarco, A.M.5    Zazopoulos, E.6    Farnet, C.M.7
  • 85
    • 33646397902 scopus 로고    scopus 로고
    • Cloning and characterization of a bacterial iterative type I polyketide synthase gene encoding the 6-methylsalicyclic acid synthase
    • Shao, L.; Qu, X.D.; Jia, X.Y.; Zhao, Q.F.; Tian, Z.H.; Wang, M.; Tang, G.L.; Liu, W. Cloning and characterization of a bacterial iterative type I polyketide synthase gene encoding the 6-methylsalicyclic acid synthase. Biochem. Biophys. Res. Commun., 2006, 345, 133-139.
    • (2006) Biochem. Biophys. Res. Commun , vol.345 , pp. 133-139
    • Shao, L.1    Qu, X.D.2    Jia, X.Y.3    Zhao, Q.F.4    Tian, Z.H.5    Wang, M.6    Tang, G.L.7    Liu, W.8
  • 86
    • 0034598743 scopus 로고    scopus 로고
    • Alternative modular polyketide synthase expression controls macrolactone structure
    • Xue, Y.; Sherman, D. H. Alternative modular polyketide synthase expression controls macrolactone structure. Nature, 2000, 403, 571-575.
    • (2000) Nature , vol.403 , pp. 571-575
    • Xue, Y.1    Sherman, D.H.2
  • 87
    • 35348982402 scopus 로고    scopus 로고
    • Non-colinear polyketide biosynthesis in the aureothin and neoaureothin pathways: An evolutionary perspective
    • Traitcheva, N.; Jenke-Kodama, H.; He, J.; Dittmann, E.; Hertweck, C. Non-colinear polyketide biosynthesis in the aureothin and neoaureothin pathways: an evolutionary perspective. Chembiochemistry, 2007, 8, 1841-1849.
    • (2007) Chembiochemistry , vol.8 , pp. 1841-1849
    • Traitcheva, N.1    Jenke-Kodama, H.2    He, J.3    Dittmann, E.4    Hertweck, C.5
  • 88
    • 67849110452 scopus 로고    scopus 로고
    • Timing of the Delta(10,12)-Delta(11,13) double bond migration during ansamitocin biosynthesis in Actinosynnema pretiosum
    • Taft, F.; Brunjes, M.; Knobloch, T.; Floss, H.G.; Kirschning, A. Timing of the Delta(10,12)-Delta(11,13) double bond migration during ansamitocin biosynthesis in Actinosynnema pretiosum. J. Am. Chem. Soc., 2009, 131, 3812-3813.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 3812-3813
    • Taft, F.1    Brunjes, M.2    Knobloch, T.3    Floss, H.G.4    Kirschning, A.5
  • 89
    • 3442896886 scopus 로고    scopus 로고
    • NRPS-PKS: A knowledge-based resource for analysis of NRPS/PKS megasynthases
    • Ansari, M.Z.; Yadav, G.; Gokhale, R.S.; Mohanty, D. NRPS-PKS: a knowledge-based resource for analysis of NRPS/PKS megasynthases. Nucleic Acids Res., 2004, 32, (Web Server issue), W405-413.
    • (2004) Nucleic Acids Res , vol.32 , Issue.Web Server issue
    • Ansari, M.Z.1    Yadav, G.2    Gokhale, R.S.3    Mohanty, D.4
  • 90
    • 26944502019 scopus 로고    scopus 로고
    • Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs)
    • Rausch, C.; Weber, T.; Kohlbacher, O.; Wohlleben, W.; Huson, D.H. Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs). Nucleic Acids Res., 2005, 33, 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
  • 91
    • 57149112966 scopus 로고    scopus 로고
    • ClustScan: An integrated program package for the semi-automatic annotation of modular biosynthetic gene clusters and in silico prediction of novel chemical structures
    • Starcevic, A.; Zucko, J.; Simunkovic, J.; Long, P.F.; Cullum, J.; Hranueli, D. ClustScan: an integrated program package for the semi-automatic annotation of modular biosynthetic gene clusters and in silico prediction of novel chemical structures. Nucleic Acids Res., 2008, 36, 6882-6892.
    • (2008) Nucleic Acids Res , vol.36 , pp. 6882-6892
    • Starcevic, A.1    Zucko, J.2    Simunkovic, J.3    Long, P.F.4    Cullum, J.5    Hranueli, D.6
  • 92
    • 61649111711 scopus 로고    scopus 로고
    • CLUSEAN: A computer-based framework for the automated analysis of bacterial secondary metabolite biosynthetic gene clusters
    • Weber, T.; Rausch, C.; Lopez, P.; Hoof, I.; Gaykova, V.; Huson, D.H.; Wohlleben, W., CLUSEAN: a computer-based framework for the automated analysis of bacterial secondary metabolite biosynthetic gene clusters. J. Biotechnol., 2009, 140, 13-17.
    • (2009) J. Biotechnol , vol.140 , pp. 13-17
    • Weber, T.1    Rausch, C.2    Lopez, P.3    Hoof, I.4    Gaykova, V.5    Huson, D.H.6    Wohlleben, W.7
  • 93
    • 2542536213 scopus 로고    scopus 로고
    • Synthesis of aminoshikimic acid
    • Guo, J.; Frost, J.W., Synthesis of aminoshikimic acid. Org. Lett., 2004, 6, 1585-1588.
    • (2004) Org. Lett , vol.6 , pp. 1585-1588
    • Guo, J.1    Frost, J.W.2
  • 94
    • 33751092257 scopus 로고    scopus 로고
    • Biosynthesis of lovastatin analogs with a broadly specific acyltransferase
    • Xie, X.; Watanabe, K.; Wojcicki, W.A.; Wang, C.C.; Tang, Y. Biosynthesis of lovastatin analogs with a broadly specific acyltransferase. Chem. Biol., 2006, 13, 1161-1169.
    • (2006) Chem. Biol , vol.13 , pp. 1161-1169
    • Xie, X.1    Watanabe, K.2    Wojcicki, W.A.3    Wang, C.C.4    Tang, Y.5
  • 95
    • 34247474300 scopus 로고    scopus 로고
    • Efficient synthesis of simvastatin by use of whole-cell biocatalysis
    • Xie, X.; Tang, Y. Efficient synthesis of simvastatin by use of whole-cell biocatalysis. Appl. Environ. Microbiol., 2007, 73, 2054-2060.
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 2054-2060
    • Xie, X.1    Tang, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.