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Volumn 48, Issue 1, 2011, Pages 49-61

Surveys of non-ribosomal peptide and polyketide assembly lines in fungi and prospects for their analysis in vitro and in vivo

Author keywords

Fourier Transform mass spectrometry; Fungal metabolism; Mass spectrometry; Non ribosomal peptide synthetases; Polyketide synthases; Proteomics; Secondary metabolism; Thiotemplate biosynthesis

Indexed keywords

AFLATOXIN; CEPHALOSPORIN DERIVATIVE; COMPACTIN; CYCLOSPORIN A; GLIOTOXIN; MEVINOLIN; MYCOSUBTILIN; NATURAL PRODUCT; NON RIBOSOMAL PEPTIDE; PENICILLIN DERIVATIVE; PEPTIDE DERIVATIVE; PIKROMYCIN; POLYKETIDE; SURFACTIN; TYROCIDINE; UNCLASSIFIED DRUG;

EID: 78650200742     PISSN: 10871845     EISSN: 10960937     Source Type: Journal    
DOI: 10.1016/j.fgb.2010.06.012     Document Type: Review
Times cited : (48)

References (89)
  • 1
    • 0026800606 scopus 로고
    • Penicillin and cephalosporin biosynthetic genes: structure, organization, regulation, and evolution
    • Aharonowitz Y., Cohen G., Martin J.F. Penicillin and cephalosporin biosynthetic genes: structure, organization, regulation, and evolution. Annu. Rev. Microbiol. 1992, 46:461-495.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 461-495
    • Aharonowitz, Y.1    Cohen, G.2    Martin, J.F.3
  • 2
    • 31644438873 scopus 로고    scopus 로고
    • Two polyketide synthase-encoding genes are required for biosynthesis of the polyketide virulence factor, T-toxin, by Cochliobolus heterostrophus
    • Baker S.E., Kroken S., Inderbitzin P., Asvarak T., Li B.Y., Shi L., Yoder O.C., Turgeon B.G. Two polyketide synthase-encoding genes are required for biosynthesis of the polyketide virulence factor, T-toxin, by Cochliobolus heterostrophus. Mol. Plant Microbe Interact. 2006, 19:139-149.
    • (2006) Mol. Plant Microbe Interact. , vol.19 , pp. 139-149
    • Baker, S.E.1    Kroken, S.2    Inderbitzin, P.3    Asvarak, T.4    Li, B.Y.5    Shi, L.6    Yoder, O.C.7    Turgeon, B.G.8
  • 3
    • 34548069725 scopus 로고    scopus 로고
    • Terrequinone A biosynthesis through l-tryptophan oxidation, dimerization and bisprenylation
    • Balibar C.J., Howard-Jones A.R., Walsh C.T. Terrequinone A biosynthesis through l-tryptophan oxidation, dimerization and bisprenylation. Nat. Chem. Biol. 2007, 3:584-592.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 584-592
    • Balibar, C.J.1    Howard-Jones, A.R.2    Walsh, C.T.3
  • 6
    • 33748362233 scopus 로고    scopus 로고
    • Biosynthesis of dothistromin
    • Bradshaw R.E., Zhang S. Biosynthesis of dothistromin. Mycopathologia 2006, 162:201-213.
    • (2006) Mycopathologia , vol.162 , pp. 201-213
    • Bradshaw, R.E.1    Zhang, S.2
  • 7
    • 70349959824 scopus 로고    scopus 로고
    • A proteomics approach to discovering natural products and their biosynthetic pathways
    • Bumpus S.B., Evans B.S., Thomas P.M., Ntai I., Kelleher N.L. A proteomics approach to discovering natural products and their biosynthetic pathways. Nat. Biotechnol. 2009, 27:951-956.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 951-956
    • Bumpus, S.B.1    Evans, B.S.2    Thomas, P.M.3    Ntai, I.4    Kelleher, N.L.5
  • 8
    • 51349154318 scopus 로고    scopus 로고
    • A ketoreductase domain in the PksJ protein of the bacillaene assembly line carries out both alpha- and beta-ketone reduction during chain growth
    • Calderone C.T., Bumpus S.B., Kelleher N.L., Walsh C.T., Magarvey N.A. A ketoreductase domain in the PksJ protein of the bacillaene assembly line carries out both alpha- and beta-ketone reduction during chain growth. Proc. Natl. Acad. Sci. USA 2008, 105:12809-12814.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12809-12814
    • Calderone, C.T.1    Bumpus, S.B.2    Kelleher, N.L.3    Walsh, C.T.4    Magarvey, N.A.5
  • 9
    • 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
  • 11
    • 0034013269 scopus 로고    scopus 로고
    • Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains
    • Challis G.L., Ravel J., Townsend C.A. Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains. Chem. Biol. 2000, 7:211-224.
    • (2000) Chem. Biol. , vol.7 , pp. 211-224
    • Challis, G.L.1    Ravel, J.2    Townsend, C.A.3
  • 15
    • 68049088909 scopus 로고    scopus 로고
    • A gene cluster containing two fungal polyketide synthases encodes the biosynthetic pathway for a polyketide, asperfuranone, in Aspergillus nidulans
    • Chiang Y.M., Szewczyk E., Davidson A.D., Keller N., Oakley B.R., Wang C.C. A gene cluster containing two fungal polyketide synthases encodes the biosynthetic pathway for a polyketide, asperfuranone, in Aspergillus nidulans. J. Am. Chem. Soc. 2009, 131:2965-2970.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2965-2970
    • Chiang, Y.M.1    Szewczyk, E.2    Davidson, A.D.3    Keller, N.4    Oakley, B.R.5    Wang, C.C.6
  • 17
    • 64049094079 scopus 로고    scopus 로고
    • Complex enzymes in microbial natural product biosynthesis, part B: polyketides, aminocoumarins and carbohydrates. Chapter 3 fungal type I polyketide synthases
    • Cox R.J., Simpson T.J. Complex enzymes in microbial natural product biosynthesis, part B: polyketides, aminocoumarins and carbohydrates. Chapter 3 fungal type I polyketide synthases. Methods Enzymol. 2009, 459:49-98.
    • (2009) Methods Enzymol. , vol.459 , pp. 49-98
    • Cox, R.J.1    Simpson, T.J.2
  • 21
    • 0029949095 scopus 로고    scopus 로고
    • Linkage among genes responsible for fumonisin biosynthesis in Gibberella fujikuroi mating population A
    • Desjardins A., Plattner R., Proctor R. Linkage among genes responsible for fumonisin biosynthesis in Gibberella fujikuroi mating population A. Appl. Environ. Microbiol. 1996, 62:2571-2576.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2571-2576
    • Desjardins, A.1    Plattner, R.2    Proctor, R.3
  • 22
    • 0015498994 scopus 로고
    • Isolation of averufin from a mutant of Aspergillus parasiticus impaired in aflatoxin biosynthesis
    • Donkersloot J.A., Mateles R.I., Yang S.S. Isolation of averufin from a mutant of Aspergillus parasiticus impaired in aflatoxin biosynthesis. Biochem. Biophys. Res. Commun. 1972, 47:1051-1055.
    • (1972) Biochem. Biophys. Res. Commun. , vol.47 , pp. 1051-1055
    • Donkersloot, J.A.1    Mateles, R.I.2    Yang, S.S.3
  • 24
    • 33750360806 scopus 로고    scopus 로고
    • Facile detection of acyl and peptidyl intermediates on thiotemplate carrier domains via phosphopantetheinyl elimination reactions during tandem mass spectrometry
    • Dorrestein P.C., Bumpus S.B., Calderone C.T., Garneau-Tsodikova S., Aron Z.D., Straight P.D., Kolter R., Walsh C.T., Kelleher N.L. Facile detection of acyl and peptidyl intermediates on thiotemplate carrier domains via phosphopantetheinyl elimination reactions during tandem mass spectrometry. Biochemistry 2006, 45:12756-12766.
    • (2006) Biochemistry , vol.45 , pp. 12756-12766
    • Dorrestein, P.C.1    Bumpus, S.B.2    Calderone, C.T.3    Garneau-Tsodikova, S.4    Aron, Z.D.5    Straight, P.D.6    Kolter, R.7    Walsh, C.T.8    Kelleher, N.L.9
  • 25
    • 77950949876 scopus 로고    scopus 로고
    • Non-ribosomal peptide synthetases of fungi
    • Springer, Heidelberg, T. Anke, D. Weber (Eds.)
    • Eisfeld K. Non-ribosomal peptide synthetases of fungi. Physiology and Genetics: Selected Basic and Applied Aspects 2009, 305-330. Springer, Heidelberg. T. Anke, D. Weber (Eds.).
    • (2009) Physiology and Genetics: Selected Basic and Applied Aspects , pp. 305-330
    • Eisfeld, K.1
  • 26
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: logic, machinery, and mechanisms
    • Fischbach M.A., Walsh C.T. Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: logic, machinery, and mechanisms. Chem. Rev. 2006, 106:3468-3496.
    • (2006) Chem. Rev. , vol.106 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 27
    • 33746523463 scopus 로고    scopus 로고
    • The biosynthetic pathway for aurofusarin in Fusarium graminearum reveals a close link between the naphthoquinones and naphthopyrones
    • Frandsen R.J., Nielsen N.J., Maolanon N., Sorensen J.C., Olsson S., Nielsen J., Giese H. The biosynthetic pathway for aurofusarin in Fusarium graminearum reveals a close link between the naphthoquinones and naphthopyrones. Mol. Microbiol. 2006, 61:1069-1080.
    • (2006) Mol. Microbiol. , vol.61 , pp. 1069-1080
    • Frandsen, R.J.1    Nielsen, N.J.2    Maolanon, N.3    Sorensen, J.C.4    Olsson, S.5    Nielsen, J.6    Giese, H.7
  • 28
    • 0032544193 scopus 로고    scopus 로고
    • The nonribosomal peptide synthetase HMWP2 forms a thiazoline ring during biogenesis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis
    • Gehring A.M., Mori I., Perry R.D., Walsh C.T. The nonribosomal peptide synthetase HMWP2 forms a thiazoline ring during biogenesis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis. Biochemistry 1998, 37:11637-11650.
    • (1998) Biochemistry , vol.37 , pp. 11637-11650
    • Gehring, A.M.1    Mori, I.2    Perry, R.D.3    Walsh, C.T.4
  • 29
    • 67749135577 scopus 로고    scopus 로고
    • A PLP-dependent polyketide chain releasing mechanism in the biosynthesis of mycotoxin fumonisins in Fusarium verticillioides
    • Gerber R., Lou L., Du L. A PLP-dependent polyketide chain releasing mechanism in the biosynthesis of mycotoxin fumonisins in Fusarium verticillioides. J. Am. Chem. Soc. 2009.
    • (2009) J. Am. Chem. Soc.
    • Gerber, R.1    Lou, L.2    Du, L.3
  • 30
    • 0036037587 scopus 로고    scopus 로고
    • Enniatin synthetase is a monomer with extended structure: evidence for an intramolecular reaction mechanism
    • Glinski M., Urbanke C., Hornbogen T., Zocher R. Enniatin synthetase is a monomer with extended structure: evidence for an intramolecular reaction mechanism. Arch. Microbiol. 2002, 178:267-273.
    • (2002) Arch. Microbiol. , vol.178 , pp. 267-273
    • Glinski, M.1    Urbanke, C.2    Hornbogen, T.3    Zocher, R.4
  • 31
    • 33644552441 scopus 로고    scopus 로고
    • Bacterial type III polyketide synthases: phylogenetic analysis and potential for the production of novel secondary metabolites by heterologous expression in pseudomonads
    • Gross F., Luniak N., Perlova O., Gaitatzis N., Jenke-Kodama H., Gerth K., Gottschalk D., Dittmann E., Muller R. Bacterial type III polyketide synthases: phylogenetic analysis and potential for the production of novel secondary metabolites by heterologous expression in pseudomonads. Arch. Microbiol. 2006, 185:28-38.
    • (2006) Arch. Microbiol. , vol.185 , pp. 28-38
    • Gross, F.1    Luniak, N.2    Perlova, O.3    Gaitatzis, N.4    Jenke-Kodama, H.5    Gerth, K.6    Gottschalk, D.7    Dittmann, E.8    Muller, R.9
  • 33
    • 0027466435 scopus 로고
    • Molecular characterization of the enniatin synthetase gene encoding a multifunctional enzyme catalysing N-methyldepsipeptide formation in Fusarium scirpi
    • Haese A., Schubert M., Herrmann M., Zocher R. Molecular characterization of the enniatin synthetase gene encoding a multifunctional enzyme catalysing N-methyldepsipeptide formation in Fusarium scirpi. Mol. Microbiol. 1993, 7:905-914.
    • (1993) Mol. Microbiol. , vol.7 , pp. 905-914
    • Haese, A.1    Schubert, M.2    Herrmann, M.3    Zocher, R.4
  • 35
    • 34249002570 scopus 로고    scopus 로고
    • The loading module of mycosubtilin: an adenylation domain with fatty acid selectivity
    • Hansen D.B., Bumpus S.B., Aron Z.D., Kelleher N.L., Walsh C.T. The loading module of mycosubtilin: an adenylation domain with fatty acid selectivity. J. Am. Chem. Soc. 2007, 129:6366-6367.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6366-6367
    • Hansen, D.B.1    Bumpus, S.B.2    Aron, Z.D.3    Kelleher, N.L.4    Walsh, C.T.5
  • 36
    • 0035900432 scopus 로고    scopus 로고
    • Biosynthesis of ochratoxins by Aspergillus ochraceus
    • Harris J.P., Mantle P.G. Biosynthesis of ochratoxins by Aspergillus ochraceus. Phytochemistry 2001, 58:709-716.
    • (2001) Phytochemistry , vol.58 , pp. 709-716
    • Harris, J.P.1    Mantle, P.G.2
  • 37
    • 0035712954 scopus 로고    scopus 로고
    • The magnitude of fungal diversity: the 1.5 million species estimate revisited
    • Hawksworth D.L. The magnitude of fungal diversity: the 1.5 million species estimate revisited. Mycological Res. 2001, 105:1422-1432.
    • (2001) Mycological Res. , vol.105 , pp. 1422-1432
    • Hawksworth, D.L.1
  • 38
    • 33947694781 scopus 로고    scopus 로고
    • Natural products of filamentous fungi: enzymes, genes, and their regulation
    • Hoffmeister D., Keller N.P. Natural products of filamentous fungi: enzymes, genes, and their regulation. Nat. Prod. Rep. 2007, 24:393-416.
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 393-416
    • Hoffmeister, D.1    Keller, N.P.2
  • 39
    • 0025606149 scopus 로고
    • Molecular genetics of polyketides and its comparison to fatty acid biosynthesis
    • Hopwood D.A., Sherman D.H. Molecular genetics of polyketides and its comparison to fatty acid biosynthesis. Annu. Rev. Genet. 1990, 24:37-66.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 37-66
    • Hopwood, D.A.1    Sherman, D.H.2
  • 41
    • 34547945950 scopus 로고    scopus 로고
    • A tylosin ketoreductase reveals how chirality is determined in polyketides
    • Keatinge-Clay A.T. A tylosin ketoreductase reveals how chirality is determined in polyketides. Chem. Biol. 2007, 14:898-908.
    • (2007) Chem. Biol. , vol.14 , pp. 898-908
    • Keatinge-Clay, A.T.1
  • 42
    • 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
  • 44
    • 0014646163 scopus 로고
    • Nonribosomal polypeptide synthesis: the biosynthesis of a cyclic peptide antibiotic, gramicidin S
    • Kleinkauf H., Gevers W. Nonribosomal polypeptide synthesis: the biosynthesis of a cyclic peptide antibiotic, gramicidin S. Cold Spring Harb. Symp. Quant. Biol. 1969, 34:805-813.
    • (1969) Cold Spring Harb. Symp. Quant. Biol. , vol.34 , pp. 805-813
    • Kleinkauf, H.1    Gevers, W.2
  • 45
    • 0035912883 scopus 로고    scopus 로고
    • Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases
    • Kohli R.M., Trauger J.W., Schwarzer D., Marahiel M.A., Walsh C.T. Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases. Biochemistry 2001, 40:7099-7108.
    • (2001) Biochemistry , vol.40 , pp. 7099-7108
    • Kohli, R.M.1    Trauger, J.W.2    Schwarzer, D.3    Marahiel, M.A.4    Walsh, C.T.5
  • 46
    • 39749169353 scopus 로고    scopus 로고
    • Harnessing the chemical activation inherent to carrier protein-bound thioesters for the characterization of lipopeptide fatty acid tailoring enzymes
    • Kopp F., Linne U., Oberthur M., Marahiel M.A. Harnessing the chemical activation inherent to carrier protein-bound thioesters for the characterization of lipopeptide fatty acid tailoring enzymes. J. Am. Chem. Soc. 2008, 130:2656-2666.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2656-2666
    • Kopp, F.1    Linne, U.2    Oberthur, M.3    Marahiel, M.A.4
  • 48
    • 67049115710 scopus 로고    scopus 로고
    • In vitro characterization of a heterologously expressed nonribosomal Peptide synthetase involved in phosphinothricin tripeptide biosynthesis
    • Lee J.H., Evans B.S., Li G., Kelleher N.L., van der Donk W.A. In vitro characterization of a heterologously expressed nonribosomal Peptide synthetase involved in phosphinothricin tripeptide biosynthesis. Biochemistry 2009, 48:5054-5056.
    • (2009) Biochemistry , vol.48 , pp. 5054-5056
    • Lee, J.H.1    Evans, B.S.2    Li, G.3    Kelleher, N.L.4    van der Donk, W.A.5
  • 49
    • 0037397957 scopus 로고    scopus 로고
    • Building-block selectivity of polyketide synthases
    • Liou G.F., Khosla C. Building-block selectivity of polyketide synthases. Curr. Opin. Chem. Biol. 2003, 7:279-284.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 279-284
    • Liou, G.F.1    Khosla, C.2
  • 52
    • 33748776033 scopus 로고    scopus 로고
    • Synthesis and evaluation of bioorthogonal pantetheine analogues for in vivo protein modification
    • Meier J.L., Mercer A.C., Rivera H., Burkart M.D. Synthesis and evaluation of bioorthogonal pantetheine analogues for in vivo protein modification. J. Am. Chem. Soc. 2006, 128:12174-12184.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12174-12184
    • Meier, J.L.1    Mercer, A.C.2    Rivera, H.3    Burkart, M.D.4
  • 53
    • 42949128785 scopus 로고    scopus 로고
    • Fluorescent profiling of modular biosynthetic enzymes by complementary metabolic and activity based probes
    • Meier J.L., Mercer A.C., Burkart M.D. Fluorescent profiling of modular biosynthetic enzymes by complementary metabolic and activity based probes. J. Am. Chem. Soc. 2008, 130:5443-5445.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 5443-5445
    • Meier, J.L.1    Mercer, A.C.2    Burkart, M.D.3
  • 54
    • 73449131845 scopus 로고    scopus 로고
    • An orthogonal active site identification system (OASIS) for proteomic profiling of natural product biosynthesis
    • Meier J.L., Niessen S., Hoover H.S., Foley T.L., Cravatt B.F., Burkart M.D. An orthogonal active site identification system (OASIS) for proteomic profiling of natural product biosynthesis. ACS Chem. Biol. 2009, 4:948-957.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 948-957
    • Meier, J.L.1    Niessen, S.2    Hoover, H.S.3    Foley, T.L.4    Cravatt, B.F.5    Burkart, M.D.6
  • 55
    • 43549120227 scopus 로고    scopus 로고
    • Top-down mass spectrometry on low-resolution instruments: characterization of phosphopantetheinylated carrier domains in polyketide and non-ribosomal biosynthetic pathways
    • Meluzzi D., Zheng W.H., Hensler M., Nizet V., Dorrestein P.C. Top-down mass spectrometry on low-resolution instruments: characterization of phosphopantetheinylated carrier domains in polyketide and non-ribosomal biosynthetic pathways. Bioorg. Med. Chem. Lett. 2008, 18:3107-3111.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 3107-3111
    • Meluzzi, D.1    Zheng, W.H.2    Hensler, M.3    Nizet, V.4    Dorrestein, P.C.5
  • 56
    • 0027458001 scopus 로고
    • Structural and functional organization of the surfactin synthetase multienzyme system
    • Menkhaus M., Ullrich C., Kluge B., Vater J., Vollenbroich D., Kamp R.M. Structural and functional organization of the surfactin synthetase multienzyme system. J. Biol. Chem. 1993, 268:7678-7684.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7678-7684
    • Menkhaus, M.1    Ullrich, C.2    Kluge, B.3    Vater, J.4    Vollenbroich, D.5    Kamp, R.M.6
  • 58
    • 78650213047 scopus 로고    scopus 로고
    • Biosynthesis and toxicological effects of patulin
    • Puel O., Galtier P., Oswald I. Biosynthesis and toxicological effects of patulin. Toxins 2010, 2:613-631.
    • (2010) Toxins , vol.2 , pp. 613-631
    • Puel, O.1    Galtier, P.2    Oswald, I.3
  • 59
    • 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
  • 60
    • 0036774667 scopus 로고    scopus 로고
    • Modification of post-PKS tailoring steps through combinatorial biosynthesis
    • Rix U., Fischer C., Remsing L.L., Rohr J. Modification of post-PKS tailoring steps through combinatorial biosynthesis. Nat. Prod. Rep. 2002, 19:542-580.
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 542-580
    • Rix, U.1    Fischer, C.2    Remsing, L.L.3    Rohr, J.4
  • 61
    • 0030947388 scopus 로고    scopus 로고
    • Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
    • Roach P.L., Clifton I.J., Hensgens C.M., Shibata N., Schofield C.J., Hajdu J., Baldwin J.E. Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature 1997, 387:827-830.
    • (1997) Nature , vol.387 , pp. 827-830
    • Roach, P.L.1    Clifton, I.J.2    Hensgens, C.M.3    Shibata, N.4    Schofield, C.J.5    Hajdu, J.6    Baldwin, J.E.7
  • 63
    • 33745969462 scopus 로고    scopus 로고
    • Advances in cloning, functional analysis and heterologous expression of fungal polyketide synthase genes
    • Schumann J., Hertweck C. Advances in cloning, functional analysis and heterologous expression of fungal polyketide synthase genes. J. Biotechnol. 2006, 124:690-703.
    • (2006) J. Biotechnol. , vol.124 , pp. 690-703
    • Schumann, J.1    Hertweck, C.2
  • 66
    • 17444429231 scopus 로고    scopus 로고
    • Discovery of a novel superfamily of type III polyketide synthases in Aspergillus oryzae
    • Seshime Y., Juvvadi P.R., Fujii I., Kitamoto K. Discovery of a novel superfamily of type III polyketide synthases in Aspergillus oryzae. Biochem. Biophys. Res. Commun. 2005, 331:253-260.
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 253-260
    • Seshime, Y.1    Juvvadi, P.R.2    Fujii, I.3    Kitamoto, K.4
  • 67
    • 0037398774 scopus 로고    scopus 로고
    • Polyketide biosynthesis beyond the type I, II and III polyketide synthase paradigms
    • Shen B. Polyketide biosynthesis beyond the type I, II and III polyketide synthase paradigms. Curr. Opin. Chem. Biol. 2003, 7:285-295.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 285-295
    • Shen, B.1
  • 68
    • 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
  • 69
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosynthesis: a millennium review
    • Staunton J., Weissman K.J. Polyketide biosynthesis: a millennium review. Nat. Prod. Rep. 2001, 18:380-416.
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 380-416
    • Staunton, J.1    Weissman, K.J.2
  • 72
    • 0142135988 scopus 로고    scopus 로고
    • Polyketide chain length control by chain length factor
    • Tang Y., Tsai S.C., Khosla C. Polyketide chain length control by chain length factor. J. Am. Chem. Soc. 2003, 125:12708-12709.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12708-12709
    • Tang, Y.1    Tsai, S.C.2    Khosla, C.3
  • 73
    • 33746776204 scopus 로고    scopus 로고
    • The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase
    • Tang Y., Kim C.Y., Mathews I.I., Cane D.E., Khosla C. The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase. Proc. Natl. Acad. Sci. USA 2006, 103:11124-11129.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11124-11129
    • Tang, Y.1    Kim, C.Y.2    Mathews, I.I.3    Cane, D.E.4    Khosla, C.5
  • 74
    • 0024590380 scopus 로고
    • B-(l-a-Aminoadipyl)-l-cysteinyl-d-valine synthetase from Aspergillus nidulans
    • van Liemt H., von Doren H., Klienkauf H. B-(l-a-Aminoadipyl)-l-cysteinyl-d-valine synthetase from Aspergillus nidulans. J Biol. Chem. 1989, 264:3680-3684.
    • (1989) J Biol. Chem. , vol.264 , pp. 3680-3684
    • van Liemt, H.1    von Doren, H.2    Klienkauf, H.3
  • 75
    • 1842833444 scopus 로고    scopus 로고
    • Gliotoxin is a dual inhibitor of farnesyltransferase and geranylgeranyltransferase I with antitumor activity against breast cancer in vivo
    • Vigushin D.M., Mirsaidi N., Brooke G., Sun C., Pace P., Inman L., Moody C.J., Coombes R.C. Gliotoxin is a dual inhibitor of farnesyltransferase and geranylgeranyltransferase I with antitumor activity against breast cancer in vivo. Med. Oncol. 2004, 21:21-30.
    • (2004) Med. Oncol. , vol.21 , pp. 21-30
    • Vigushin, D.M.1    Mirsaidi, N.2    Brooke, G.3    Sun, C.4    Pace, P.5    Inman, L.6    Moody, C.J.7    Coombes, R.C.8
  • 76
    • 14744277927 scopus 로고    scopus 로고
    • Biochemistry and general genetics of nonribosomal peptide synthetases in fungi
    • von Dohren H. Biochemistry and general genetics of nonribosomal peptide synthetases in fungi. Adv. Biochem. Eng. Biotechnol. 2004, 88:217-264.
    • (2004) Adv. Biochem. Eng. Biotechnol. , vol.88 , pp. 217-264
    • von Dohren, H.1
  • 77
    • 63849314526 scopus 로고    scopus 로고
    • A survey of nonribosomal peptide synthetase (NRPS) genes in Aspergillus nidulans
    • von Dohren H. A survey of nonribosomal peptide synthetase (NRPS) genes in Aspergillus nidulans. Fungal Genet. Biol. 2009, 46(Suppl. 1):S45-S52.
    • (2009) Fungal Genet. Biol. , vol.46 , Issue.SUPPL. 1
    • von Dohren, H.1
  • 78
    • 33746208944 scopus 로고    scopus 로고
    • HC-toxin
    • Walton J.D. HC-toxin. Phytochemistry 2006, 67:1406-1413.
    • (2006) Phytochemistry , vol.67 , pp. 1406-1413
    • Walton, J.D.1
  • 79
    • 0032890191 scopus 로고    scopus 로고
    • Re-identification of Aspergillus nidulans wA gene to code for a polyketide synthase of naphthopyrone
    • Watanabe A., Fujii I., Sankawa U., Mayorga M., Timberlake W., Ebizuka Y. Re-identification of Aspergillus nidulans wA gene to code for a polyketide synthase of naphthopyrone. Tetrahedron Lett. 1999, 40:91-94.
    • (1999) Tetrahedron Lett. , vol.40 , pp. 91-94
    • Watanabe, A.1    Fujii, I.2    Sankawa, U.3    Mayorga, M.4    Timberlake, W.5    Ebizuka, Y.6
  • 80
    • 0028284699 scopus 로고
    • The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame
    • Weber G., Schorgendorfer K., Schneider-Scherzer E., Leitner E. The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame. Curr. Genet. 1994, 26:120-125.
    • (1994) Curr. Genet. , vol.26 , pp. 120-125
    • Weber, G.1    Schorgendorfer, K.2    Schneider-Scherzer, E.3    Leitner, E.4
  • 81
    • 0032521312 scopus 로고    scopus 로고
    • Genetic organization and function of the aflatoxin B1 biosynthetic genes
    • Woloshuk C.P., Prieto R. Genetic organization and function of the aflatoxin B1 biosynthetic genes. FEMS Microbiol. Lett. 1998, 160:169-176.
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 169-176
    • Woloshuk, C.P.1    Prieto, R.2
  • 82
    • 67650537065 scopus 로고    scopus 로고
    • Acyltransferase mediated polyketide release from a fungal megasynthase
    • Xie X., Meehan M.J., Xu W., Dorrestein P.C., Tang Y. Acyltransferase mediated polyketide release from a fungal megasynthase. J. Am. Chem. Soc. 2009, 131:8388-8389.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8388-8389
    • Xie, X.1    Meehan, M.J.2    Xu, W.3    Dorrestein, P.C.4    Tang, Y.5
  • 83
    • 3142682353 scopus 로고    scopus 로고
    • Enzyme reactions and genes in aflatoxin biosynthesis
    • Yabe K., Nakajima H. Enzyme reactions and genes in aflatoxin biosynthesis. Appl. Microbiol. Biotechnol. 2004, 64:745-755.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 745-755
    • Yabe, K.1    Nakajima, H.2
  • 84
    • 0029143685 scopus 로고
    • Sterigmatocystin biosynthesis in Aspergillus nidulans requires a novel type I polyketide synthase
    • Yu J.H., Leonard T.J. Sterigmatocystin biosynthesis in Aspergillus nidulans requires a novel type I polyketide synthase. J. Bacteriol. 1995, 177:4792-4800.
    • (1995) J. Bacteriol. , vol.177 , pp. 4792-4800
    • Yu, J.H.1    Leonard, T.J.2
  • 86
    • 39549096803 scopus 로고    scopus 로고
    • A phosphopantetheinylating polyketide synthase producing a linear polyene to initiate enediyne antitumor antibiotic biosynthesis
    • Zhang J., Van Lanen S.G., Ju J., Liu W., Dorrestein P.C., Li W., Kelleher N.L., Shen B. A phosphopantetheinylating polyketide synthase producing a linear polyene to initiate enediyne antitumor antibiotic biosynthesis. Proc. Natl. Acad. Sci. USA 2008, 105:1460-1465.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1460-1465
    • Zhang, J.1    Van Lanen, S.G.2    Ju, J.3    Liu, W.4    Dorrestein, P.C.5    Li, W.6    Kelleher, N.L.7    Shen, B.8
  • 87
    • 0032736469 scopus 로고    scopus 로고
    • Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in Aspergillus parasiticus
    • Zhou R., Linz J.E. Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in Aspergillus parasiticus. Appl. Environ. Microbiol. 1999, 65:5639-5641.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5639-5641
    • Zhou, R.1    Linz, J.E.2
  • 88
    • 0031060707 scopus 로고    scopus 로고
    • Thiol template peptide synthesis systems in bacteria and fungi
    • Zocher R., Keller U. Thiol template peptide synthesis systems in bacteria and fungi. Adv. Microb. Physiol. 1997, 38:85-131.
    • (1997) Adv. Microb. Physiol. , vol.38 , pp. 85-131
    • Zocher, R.1    Keller, U.2
  • 89
    • 0020475126 scopus 로고
    • Enniatin synthetase, a novel type of multifunctional enzyme catalyzing depsipeptide synthesis in Fusarium oxysporum
    • Zocher R., Keller U., Kleinkauf H. Enniatin synthetase, a novel type of multifunctional enzyme catalyzing depsipeptide synthesis in Fusarium oxysporum. Biochemistry 1982, 21:43-48.
    • (1982) Biochemistry , vol.21 , pp. 43-48
    • Zocher, R.1    Keller, U.2    Kleinkauf, H.3


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