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Volumn 27, Issue 2, 2013, Pages 43-50

Fungal peptide synthetases: An update on functions and specificity signatures

Author keywords

Natural product; Nonribosomal peptide synthetase; Secondary metabolism; Substrate specificity

Indexed keywords

BASIDIOMYCOTA;

EID: 84881089982     PISSN: 17494613     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fbr.2013.05.002     Document Type: Review
Times cited : (23)

References (49)
  • 2
    • 77950929561 scopus 로고    scopus 로고
    • Anthranilate-activating modules from fungal nonribosomal peptide assembly lines
    • Ames B.D., Walsh C.T. Anthranilate-activating modules from fungal nonribosomal peptide assembly lines. Biochemistry 2010, 49:3351-3365.
    • (2010) Biochemistry , vol.49 , pp. 3351-3365
    • Ames, B.D.1    Walsh, C.T.2
  • 3
    • 33845592512 scopus 로고    scopus 로고
    • GliP, a multimodular nonribosomal peptide synthetase in Aspergillus fumigatus, makes the diketopiperazine scaffold of gliotoxin
    • Balibar C.J., Walsh C.T. GliP, a multimodular nonribosomal peptide synthetase in Aspergillus fumigatus, makes the diketopiperazine scaffold of gliotoxin. Biochemistry 2006, 45:15029-15038.
    • (2006) Biochemistry , vol.45 , pp. 15029-15038
    • Balibar, C.J.1    Walsh, C.T.2
  • 4
    • 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
    • 0021906426 scopus 로고
    • Alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes
    • Bhattacharjee J.K. alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes. Crit. Rev. Microbiol. 1985, 12:131-151.
    • (1985) Crit. Rev. Microbiol. , vol.12 , pp. 131-151
    • Bhattacharjee, J.K.1
  • 7
    • 79951537655 scopus 로고    scopus 로고
    • Metabolites from the induced expression of cryptic single operons found in the genome of Burkholderia pseudomallei
    • Biggins J.B., Liu X., Feng Z., Brady S.F. Metabolites from the induced expression of cryptic single operons found in the genome of Burkholderia pseudomallei. J. Am. Chem. Soc. 2011, 133:1638-1641.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 1638-1641
    • Biggins, J.B.1    Liu, X.2    Feng, Z.3    Brady, S.F.4
  • 9
    • 60649096983 scopus 로고    scopus 로고
    • Module evolution and substrate specificity of fungal nonribosomal peptide synthetases involved in siderophore biosynthesis
    • Bushley K.E., Ripoll D.R., Turgeon B.G. Module evolution and substrate specificity of fungal nonribosomal peptide synthetases involved in siderophore biosynthesis. BMC Evol. Biol. 2008, 8:328.
    • (2008) BMC Evol. Biol. , vol.8 , pp. 328
    • Bushley, K.E.1    Ripoll, D.R.2    Turgeon, B.G.3
  • 10
    • 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
  • 12
    • 84871826475 scopus 로고    scopus 로고
    • Structure and noncanonical chemistry of nonribosomal peptide biosynthetic machinery
    • Condurso H.L., Bruner S.D. Structure and noncanonical chemistry of nonribosomal peptide biosynthetic machinery. Nat. Prod. Rep. 2012, 29:1099-1110.
    • (2012) Nat. Prod. Rep. , vol.29 , pp. 1099-1110
    • Condurso, H.L.1    Bruner, S.D.2
  • 13
    • 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
  • 14
    • 0346968186 scopus 로고    scopus 로고
    • Molecular cloning and analysis of the ergopeptine assembly system in the ergot fungus Claviceps purpurea
    • Correia T., Grammel N., Ortel I., Keller U., Tudzynski P. Molecular cloning and analysis of the ergopeptine assembly system in the ergot fungus Claviceps purpurea. Chem. Biol. 2003, 10:1281-1292.
    • (2003) Chem. Biol. , vol.10 , pp. 1281-1292
    • Correia, T.1    Grammel, N.2    Ortel, I.3    Keller, U.4    Tudzynski, P.5
  • 15
    • 78650200742 scopus 로고    scopus 로고
    • Surveys of non-ribosomal peptide and polyketide assembly lines in fungi and prospects for their analysis invitro and invivo
    • Evans B.S., Robinson S.J., Kelleher N.L. Surveys of non-ribosomal peptide and polyketide assembly lines in fungi and prospects for their analysis invitro and invivo. Fungal Genet. Biol. 2011, 48:49-61.
    • (2011) Fungal Genet. Biol. , vol.48 , pp. 49-61
    • Evans, B.S.1    Robinson, S.J.2    Kelleher, N.L.3
  • 17
    • 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
  • 20
    • 79952270689 scopus 로고    scopus 로고
    • Fungal indole alkaloid biosynthesis: genetic and biochemical investigation of the tryptoquialanine pathway in Penicillium aethiopicum
    • Gao X., Chooi Y.H., Ames B.D., Wang P., Walsh C.T., Tang Y. Fungal indole alkaloid biosynthesis: genetic and biochemical investigation of the tryptoquialanine pathway in Penicillium aethiopicum. J. Am. Chem. Soc. 2011, 133:2729-2741.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2729-2741
    • Gao, X.1    Chooi, Y.H.2    Ames, B.D.3    Wang, P.4    Walsh, C.T.5    Tang, Y.6
  • 23
    • 20444414907 scopus 로고    scopus 로고
    • The ergot alkaloid gene cluster in Claviceps purpurea: extension of the cluster sequence and intra species evolution
    • Haarmann T., Machado C., Lübbe Y., Correia T., Schardl C.L., Panaccione D.G., Tudzynski P. The ergot alkaloid gene cluster in Claviceps purpurea: extension of the cluster sequence and intra species evolution. Phytochemistry 2005, 66:1312-1320.
    • (2005) Phytochemistry , vol.66 , pp. 1312-1320
    • Haarmann, T.1    Machado, C.2    Lübbe, Y.3    Correia, T.4    Schardl, C.L.5    Panaccione, D.G.6    Tudzynski, P.7
  • 25
    • 84876518582 scopus 로고    scopus 로고
    • Complexity generation in fungal peptidyl alkaloid biosynthesis: a two enzyme pathway to the hexacyclic MDR export pump inhibitor ardeemin
    • Haynes S.W., Gao X., Tang Y., Walsh C.T. Complexity generation in fungal peptidyl alkaloid biosynthesis: a two enzyme pathway to the hexacyclic MDR export pump inhibitor ardeemin. ACS Chem. Biol. 2013, 8:741-748.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 741-748
    • Haynes, S.W.1    Gao, X.2    Tang, Y.3    Walsh, C.T.4
  • 26
    • 0035095042 scopus 로고    scopus 로고
    • Characterization of the lys2 gene of Acremonium chrysogenum encoding a functional α-aminoadipate activating and reducing enzyme
    • Hijarrubia M.J., Aparicio J.F., Casqueiro J., Martin J.F. Characterization of the lys2 gene of Acremonium chrysogenum encoding a functional α-aminoadipate activating and reducing enzyme. Mol. Gen. Genet. 2001, 264:755-762.
    • (2001) Mol. Gen. Genet. , vol.264 , pp. 755-762
    • Hijarrubia, M.J.1    Aparicio, J.F.2    Casqueiro, J.3    Martin, J.F.4
  • 27
    • 77449129446 scopus 로고    scopus 로고
    • Structure of a eukaryotic nonribosomal peptide synthetase adenylation domain that activates a large hydroxamate amino acid in siderophore biosynthesis
    • Lee T.V., Johnson L.J., Johnson R.D., Koulman A., Lane G.A., Lott J.S., Arcus V.L. Structure of a eukaryotic nonribosomal peptide synthetase adenylation domain that activates a large hydroxamate amino acid in siderophore biosynthesis. J. Biol. Chem. 2010, 285:2415-2427.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2415-2427
    • Lee, T.V.1    Johnson, L.J.2    Johnson, R.D.3    Koulman, A.4    Lane, G.A.5    Lott, J.S.6    Arcus, V.L.7
  • 28
    • 34948842874 scopus 로고    scopus 로고
    • Identification of a hybrid PKS/NRPS required for pseurotin A biosynthesis in the human pathogen Aspergillus fumigatus
    • Maiya S., Grundmann A., Li X., Li S.M., Turner G. Identification of a hybrid PKS/NRPS required for pseurotin A biosynthesis in the human pathogen Aspergillus fumigatus. Chembiochem 2007, 8:1736-1743.
    • (2007) Chembiochem , vol.8 , pp. 1736-1743
    • Maiya, S.1    Grundmann, A.2    Li, X.3    Li, S.M.4    Turner, G.5
  • 29
    • 0037126024 scopus 로고    scopus 로고
    • Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases
    • May J.J., Kessler N., Marahiel M.A., Stubbs M.T. Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases. Proc. Natl. Acad. Sci. USA 2002, 99:12120-12125.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12120-12125
    • May, J.J.1    Kessler, N.2    Marahiel, M.A.3    Stubbs, M.T.4
  • 30
    • 79960739048 scopus 로고    scopus 로고
    • Characterisation of the ArmA adenylation domain implies a more diverse secondary metabolism in the genus Armillaria
    • Misiek M., Braesel J., Hoffmeister D. Characterisation of the ArmA adenylation domain implies a more diverse secondary metabolism in the genus Armillaria. Fungal Biol. 2011, 115:775-781.
    • (2011) Fungal Biol. , vol.115 , pp. 775-781
    • Misiek, M.1    Braesel, J.2    Hoffmeister, D.3
  • 31
    • 33750981838 scopus 로고    scopus 로고
    • NPS6, encoding a nonribosomal peptide synthetase involved in siderophore-mediated iron metabolism, is a conserved virulence determinant of plant pathogenic ascomycetes
    • Oide S., Moeder W., Krasnoff S., Gibson D., Haas H., Yoshioka K., Turgeon B.G. NPS6, encoding a nonribosomal peptide synthetase involved in siderophore-mediated iron metabolism, is a conserved virulence determinant of plant pathogenic ascomycetes. Plant Cell 2006, 18:2836-2853.
    • (2006) Plant Cell , vol.18 , pp. 2836-2853
    • Oide, S.1    Moeder, W.2    Krasnoff, S.3    Gibson, D.4    Haas, H.5    Yoshioka, K.6    Turgeon, B.G.7
  • 32
    • 65449145993 scopus 로고    scopus 로고
    • Combinatorial assembly of simple and complex d-lysergic acid alkaloid peptide classes in the ergot fungus Claviceps purpurea
    • Ortel I., Keller U. Combinatorial assembly of simple and complex d-lysergic acid alkaloid peptide classes in the ergot fungus Claviceps purpurea. J. Biol. Chem. 2009, 284:6650-6660.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6650-6660
    • Ortel, I.1    Keller, U.2
  • 33
    • 0030002729 scopus 로고    scopus 로고
    • D-Lysergyl peptide synthetase from the ergot fungus Claviceps purpurea
    • Riederer B., Han M., Keller U. d-Lysergyl peptide synthetase from the ergot fungus Claviceps purpurea. J. Biol. Chem. 1996, 271:27524-27530.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27524-27530
    • Riederer, B.1    Han, M.2    Keller, U.3
  • 34
    • 34250372830 scopus 로고    scopus 로고
    • A one-pot chemoenzymatic synthesis for the universal precursor of antidiabetes and antiviral bis-indolylquinones
    • Schneider P., Weber M., Rosenberger K., Hoffmeister D. A one-pot chemoenzymatic synthesis for the universal precursor of antidiabetes and antiviral bis-indolylquinones. Chem. Biol. 2007, 14:635-644.
    • (2007) Chem. Biol. , vol.14 , pp. 635-644
    • Schneider, P.1    Weber, M.2    Rosenberger, K.3    Hoffmeister, D.4
  • 35
    • 55149109662 scopus 로고    scopus 로고
    • Characterization of the atromentin biosynthesis genes and enzymes in the homobasidiomycete Tapinella panuoides
    • Schneider P., Bouhired S., Hoffmeister D. Characterization of the atromentin biosynthesis genes and enzymes in the homobasidiomycete Tapinella panuoides. Fungal Genet. Biol. 2008, 45:1487-1496.
    • (2008) Fungal Genet. Biol. , vol.45 , pp. 1487-1496
    • Schneider, P.1    Bouhired, S.2    Hoffmeister, D.3
  • 36
    • 38849108030 scopus 로고    scopus 로고
    • The Aspergillus nidulans enzyme TdiB catalyzes prenyltransfer to the precursor of bioactive asterriquinones
    • Schneider P., Weber M., Hoffmeister D. The Aspergillus nidulans enzyme TdiB catalyzes prenyltransfer to the precursor of bioactive asterriquinones. Fungal Genet. Biol. 2008, 45:302-309.
    • (2008) Fungal Genet. Biol. , vol.45 , pp. 302-309
    • Schneider, P.1    Weber, M.2    Hoffmeister, D.3
  • 37
    • 34547817781 scopus 로고    scopus 로고
    • Molecular basis of cytochalasan biosynthesis in fungi: gene cluster analysis and evidence for the involvement of a PKS-NRPS hybrid synthase by RNA silencing
    • Schümann J., Hertweck C. Molecular basis of cytochalasan biosynthesis in fungi: gene cluster analysis and evidence for the involvement of a PKS-NRPS hybrid synthase by RNA silencing. J. Am. Chem. Soc. 2007, 129:9564-9565.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9564-9565
    • Schümann, J.1    Hertweck, C.2
  • 39
    • 65749085312 scopus 로고    scopus 로고
    • Functional expression of the Aspergillus flavus PKS-NRPS hybrid CpaA involved in the biosynthesis of cyclopiazonic acid
    • Seshime Y., Juvvadi P.R., Tokuoka M., Koyama Y., Kitamoto K., Ebizuka Y., Fujii I. Functional expression of the Aspergillus flavus PKS-NRPS hybrid CpaA involved in the biosynthesis of cyclopiazonic acid. Bioorg. Med. Chem. Lett. 2009, 19:3288-3292.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 3288-3292
    • Seshime, Y.1    Juvvadi, P.R.2    Tokuoka, M.3    Koyama, Y.4    Kitamoto, K.5    Ebizuka, Y.6    Fujii, I.7
  • 40
    • 14844362054 scopus 로고    scopus 로고
    • Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics
    • Sieber S.A., Marahiel M.A. Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics. Chem. Rev. 2005, 105:715-738.
    • (2005) Chem. Rev. , vol.105 , pp. 715-738
    • Sieber, S.A.1    Marahiel, M.A.2
  • 41
    • 78650431078 scopus 로고    scopus 로고
    • Fungal cyclooligomer depsipeptides: from classical biochemistry to combinatorial biosynthesis
    • Süssmuth R., Müller J., von Döhren H., Molnár I. Fungal cyclooligomer depsipeptides: from classical biochemistry to combinatorial biosynthesis. Nat. Prod. Rep. 2011, 28:99-124.
    • (2011) Nat. Prod. Rep. , vol.28 , pp. 99-124
    • Süssmuth, R.1    Müller, J.2    von Döhren, H.3    Molnár, I.4
  • 42
    • 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
  • 43
    • 34249085909 scopus 로고    scopus 로고
    • Nonribosomal peptide synthesis in Aspergillus fumigatus and other fungi
    • Stack D., Neville C., Doyle S. Nonribosomal peptide synthesis in Aspergillus fumigatus and other fungi. Microbiology 2007, 153:1297-1306.
    • (2007) Microbiology , vol.153 , pp. 1297-1306
    • Stack, D.1    Neville, C.2    Doyle, S.3
  • 45
    • 79953065301 scopus 로고    scopus 로고
    • Ralfuranone biosynthesis in Ralstonia solanacearum suggests functional divergence in the quinone synthetase family of enzymes
    • Wackler B., Schneider P., Jacobs J.M., Pauly J., Allen C., Nett M., Hoffmeister D. Ralfuranone biosynthesis in Ralstonia solanacearum suggests functional divergence in the quinone synthetase family of enzymes. Chem. Biol. 2011, 18:354-360.
    • (2011) Chem. Biol. , vol.18 , pp. 354-360
    • Wackler, B.1    Schneider, P.2    Jacobs, J.M.3    Pauly, J.4    Allen, C.5    Nett, M.6    Hoffmeister, D.7
  • 46
    • 84864773080 scopus 로고    scopus 로고
    • Characterization of the Suillus grevillei quinone synthetase GreA supports a nonribosomal code for aromatic α-keto acids
    • Wackler B., Lackner G., Chooi Y.H., Hoffmeister D. Characterization of the Suillus grevillei quinone synthetase GreA supports a nonribosomal code for aromatic α-keto acids. Chembiochem 2012, 13:1798-1804.
    • (2012) Chembiochem , vol.13 , pp. 1798-1804
    • Wackler, B.1    Lackner, G.2    Chooi, Y.H.3    Hoffmeister, D.4
  • 47
    • 22144450632 scopus 로고    scopus 로고
    • Characterization of the ferrichrome A biosynthetic gene cluster in the homobasidiomycete Omphalotus olearius
    • Welzel K., Eisfeld K., Antelo L., Anke T., Anke H. Characterization of the ferrichrome A biosynthetic gene cluster in the homobasidiomycete Omphalotus olearius. FEMS Microbiol. Lett. 2005, 249:157-163.
    • (2005) FEMS Microbiol. Lett. , vol.249 , pp. 157-163
    • Welzel, K.1    Eisfeld, K.2    Antelo, L.3    Anke, T.4    Anke, H.5
  • 49
    • 84867577748 scopus 로고    scopus 로고
    • Molecular genetic analysis reveals that a nonribosomal peptide synthetase-like (NRPS-like) gene in Aspergillus nidulans is responsible for microperfuranone biosynthesis
    • Yeh H.H., Chiang Y.M., Entwistle R., Ahuja M., Lee K.H., Bruno K.S., Wu T.K., Oakley B.R., Wang C.C. Molecular genetic analysis reveals that a nonribosomal peptide synthetase-like (NRPS-like) gene in Aspergillus nidulans is responsible for microperfuranone biosynthesis. Appl. Microbiol. Biotechnol. 2012, 96:739-748.
    • (2012) Appl. Microbiol. Biotechnol. , vol.96 , pp. 739-748
    • Yeh, H.H.1    Chiang, Y.M.2    Entwistle, R.3    Ahuja, M.4    Lee, K.H.5    Bruno, K.S.6    Wu, T.K.7    Oakley, B.R.8    Wang, C.C.9


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