메뉴 건너뛰기




Volumn 8, Issue 12, 2010, Pages 879-889

New insights into the formation of fungal aromatic polyketides

Author keywords

[No Author keywords available]

Indexed keywords

POLYKETIDE SYNTHASE;

EID: 78449290452     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro2465     Document Type: Review
Times cited : (188)

References (108)
  • 1
    • 34848843433 scopus 로고    scopus 로고
    • The type i fatty acid and polyketide synthases: A tale of two megasynthases
    • Smith, S. & Tsai, S. C. The type I fatty acid and polyketide synthases: a tale of two megasynthases. Nat. Prod. Rep. 24, 1041-1072 (2007).
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 1041-1072
    • Smith, S.1    Tsai, S.C.2
  • 2
    • 64049116611 scopus 로고    scopus 로고
    • Bacterial fatty acid synthesis and its relationships with polyketide synthetic pathways
    • Cronan, J. E. & Thomas, J. Bacterial fatty acid synthesis and its relationships with polyketide synthetic pathways. Methods Enzymol. 459, 395-433 (2009).
    • (2009) Methods Enzymol. , vol.459 , pp. 395-433
    • Cronan, J.E.1    Thomas, J.2
  • 3
    • 0037015157 scopus 로고    scopus 로고
    • Mechanism of the b-ketoacyl synthase reaction catalyzed by the animal fatty acid synthase
    • Witkowski, A., Joshi, A. K. & Smith, S. Mechanism of the b-ketoacyl synthase reaction catalyzed by the animal fatty acid synthase. Biochemistry 41, 10877-10887 (2002).
    • (2002) Biochemistry , vol.41 , pp. 10877-10887
    • Witkowski, A.1    Joshi, A.K.2    Smith, S.3
  • 4
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosyn thesis: A millennium review
    • Staunton, J. & Weissman, K. J. Polyketide biosynthesis: a millennium review. Nat. Prod. Rep. 18, 380-416 (2001).
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 380-416
    • Staunton, J.1    Weissman, K.J.2
  • 5
    • 33846923183 scopus 로고    scopus 로고
    • Type II polyketide synthases: Gaining a deeper insight into enzymatic teamwork
    • Hertweck, C., Luzhetskyy, A., Rebets, Y. & Bechthold, A. Type II polyketide synthases: gaining a deeper insight into enzymatic teamwork. Nat. Prod. Rep. 24, 162-190 (2007).
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 162-190
    • Hertweck, C.1    Luzhetskyy, A.2    Rebets, Y.3    Bechthold, A.4
  • 6
    • 64049110816 scopus 로고    scopus 로고
    • In vitro analysis of type II polyketide synthase
    • Zhang, W. & Tang, Y. In vitro analysis of type II polyketide synthase. Methods Enzymol. 459, 367-393 (2009).
    • (2009) Methods Enzymol. , vol.459 , pp. 367-393
    • Zhang, W.1    Tang, Y.2
  • 7
    • 66149105072 scopus 로고    scopus 로고
    • Biosynthesis of aromatic polyketides in bacteria
    • Das, A. & Khosla, C. Biosynthesis of aromatic polyketides in bacteria. Acc. Chem. Res. 42, 631-639 (2009).
    • (2009) Acc. Chem. Res. , vol.42 , pp. 631-639
    • Das, A.1    Khosla, C.2
  • 8
    • 0037319699 scopus 로고    scopus 로고
    • The chalcone synthase superfamily of type III polyketide synthases
    • Austin, M. B. & Noel, J. P. The chalcone synthase superfamily of type III polyketide synthases. Nat. Prod. Rep. 20, 79-110 (2003).
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 79-110
    • Austin, M.B.1    Noel, J.P.2
  • 9
    • 7244239181 scopus 로고    scopus 로고
    • Crystal structure of a bacterial type III polyketide synthase and enzymatic control of reactive polyketide intermediates
    • Austin, M. B. et al. Crystal structure of a bacterial type III polyketide synthase and enzymatic control of reactive polyketide intermediates. J. Biol. Chem. 279, 45162-45174 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 45162-45174
    • Austin, M.B.1
  • 10
    • 34347255733 scopus 로고    scopus 로고
    • Pentaketide resorcylic acid synthesis by type III polyketide synthase from Neurospora crassa
    • Funa, N., Awakawa, T. & Horinouchi, S. Pentaketide resorcylic acid synthesis by type III polyketide synthase from Neurospora crassa. J. Biol. Chem. 282, 14476-14481 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 14476-14481
    • Funa, N.1    Awakawa, T.2    Horinouchi, S.3
  • 11
    • 59349116977 scopus 로고    scopus 로고
    • Heterologous expression systems for polyketide synthases
    • Fujii, I. Heterologous expression systems for polyketide synthases. Nat. Prod. Rep. 26, 155-169 (2009).
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 155-169
    • Fujii, I.1
  • 12
    • 64049111007 scopus 로고    scopus 로고
    • Introduction to polyketide biosynthesis
    • Weissman, K. J. Introduction to polyketide biosynthesis. Methods Enzymol. 459, 3-16 (2009).
    • (2009) Methods Enzymol. , vol.459 , pp. 3-16
    • Weissman, K.J.1
  • 13
    • 0037398774 scopus 로고    scopus 로고
    • Polyketide biosynthesis beyond the type I, II and III polyketide synthase paradigms
    • DOI 10.1016/S1367-5931(03)00020-6
    • Shen, B. Polyketide biosynthesis beyond the type I, II and III polyketide synthase paradigms. Curr. Opin. Chem. Biol. 7, 285-295 (2003). (Pubitemid 36514961)
    • (2003) Current Opinion in Chemical Biology , vol.7 , Issue.2 , pp. 285-295
    • Shen, B.1
  • 14
    • 7744220004 scopus 로고    scopus 로고
    • Don't classify polyketide synthases
    • Muller, R. Don't classify polyketide synthases. Chem. Biol. 11, 4-6 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 4-6
    • Muller, R.1
  • 15
    • 0032876464 scopus 로고    scopus 로고
    • Ketosynthase domain probes identify two subclasses of fungal polyketide synthase genes
    • Bingle, L. E., Simpson, T. J. & Lazarus, C. M. Ketosynthase domain probes identify two subclasses of fungal polyketide synthase genes. Fungal Genet. Biol. 26, 209-223 (1999).
    • (1999) Fungal Genet. Biol. , vol.26 , pp. 209-223
    • Bingle, L.E.1    Simpson, T.J.2    Lazarus, C.M.3
  • 16
    • 0035060868 scopus 로고    scopus 로고
    • Design and utility of oligonucleotide gene probes for fungal polyketide synthases
    • Nicholson, T. P. et al. Design and utility of oligonucleotide gene probes for fungal polyketide synthases. Chem. Biol. 8, 157-178 (2001).
    • (2001) Chem. Biol. , vol.8 , pp. 157-178
    • Nicholson, T.P.1
  • 17
    • 69249202590 scopus 로고    scopus 로고
    • The biosynthetic logic of polyketide diversity
    • Hertweck, C. The biosynthetic logic of polyketide diversity. Angew. Chem. Int. Ed. Engl. 48, 4688-4716 (2009).
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 4688-4716
    • Hertweck, C.1
  • 18
    • 64049094079 scopus 로고    scopus 로고
    • Fungal type i polyketide synthases
    • Cox, R. J. & Simpson, T. J. Fungal type I polyketide synthases. Methods Enzymol. 459, 49-78 (2009).
    • (2009) Methods Enzymol. , vol.459 , pp. 49-78
    • Cox, R.J.1    Simpson, T.J.2
  • 19
    • 0014708426 scopus 로고
    • Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis
    • Klenow, H. & Henningsen, I. Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis. Proc. Natl Acad. Sci. USA 65, 168-175 (1970).
    • (1970) Proc. Natl Acad. Sci. USA , vol.65 , pp. 168-175
    • Klenow, H.1    Henningsen, I.2
  • 20
    • 0021112906 scopus 로고
    • The architecture of the animal fatty acid synthetase complex. IV. Mapping of active centers and model for the mechanism of action
    • Tsukamoto, Y., Wong, H., Mattick, J. S. & Wakil, S. J. The architecture of the animal fatty acid synthetase complex. IV. Mapping of active centers and model for the mechanism of action. J. Biol. Chem. 258, 15312-15322 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 15312-15322
    • Tsukamoto, Y.1    Wong, H.2    Mattick, J.S.3    Wakil, S.J.4
  • 21
    • 0014939622 scopus 로고
    • Studies on the mechanism of fatty acid synthesis. XXIV. The acetyl-and malonyltransacylase activities of pigeon liver fatty acid synthetase
    • Plate, C. A., Joshi, V. C. & Wakil, S. J. Studies on the mechanism of fatty acid synthesis. XXIV. The acetyl-and malonyltransacylase activities of pigeon liver fatty acid synthetase. J. Biol. Chem. 245, 2868-2875 (1970).
    • (1970) J. Biol. Chem. , vol.245 , pp. 2868-2875
    • Plate, C.A.1    Joshi, V.C.2    Wakil, S.J.3
  • 22
    • 0036404537 scopus 로고    scopus 로고
    • A method for prediction of the locations of linker regions within large multifunctional proteins, and application to a type i polyketide synthase
    • Udwary, D. W., Merski, M. & Townsend, C. A. A method for prediction of the locations of linker regions within large multifunctional proteins, and application to a type I polyketide synthase. J. Mol. Biol. 323, 585-598 (2002).
    • (2002) J. Mol. Biol. , vol.323 , pp. 585-598
    • Udwary, D.W.1    Merski, M.2    Townsend, C.A.3
  • 23
    • 33750966150 scopus 로고    scopus 로고
    • Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type i polyketide synthase
    • Crawford, J. M., Dancy, B. C. R., Hill, E. A., Udwary, D. W. & Townsend, C. A. Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase. Proc. Natl Acad. Sci. USA 103, 16728-16733 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 16728-16733
    • Crawford, J.M.1    Dancy, B.C.R.2    Hill, E.A.3    Udwary, D.W.4    Townsend, C.A.5
  • 24
    • 38549095277 scopus 로고    scopus 로고
    • Starter unit specificity directs genome mining of polyketide synthase pathways in fungi
    • Crawford, J. M., Vagstad, A. L., Ehrlich, K. C. & Townsend, C. A. Starter unit specificity directs genome mining of polyketide synthase pathways in fungi. Bioorg. Chem. 36, 16-22 (2008).
    • (2008) Bioorg. Chem. , vol.36 , pp. 16-22
    • Crawford, J.M.1    Vagstad, A.L.2    Ehrlich, K.C.3    Townsend, C.A.4
  • 25
    • 46649115560 scopus 로고    scopus 로고
    • Synthetic strategy of nonreducing iterative polyketide synthases and the origin of the classical "starter-Unit Effect"
    • Crawford, J. M., Vagstad, A. L., Whitworth, K. P., Ehrlich, K. C. & Townsend, C. A. Synthetic strategy of nonreducing iterative polyketide synthases and the origin of the classical "Starter-Unit Effect". Chembiochem 9, 1019-1023 (2008).
    • (2008) Chembiochem , vol.9 , pp. 1019-1023
    • Crawford, J.M.1    Vagstad, A.L.2    Whitworth, K.P.3    Ehrlich, K.C.4    Townsend, C.A.5
  • 26
    • 48649095210 scopus 로고    scopus 로고
    • Acyl-carrier protein-phosphopantetheinyltransferase partnerships in fungal fatty acid synthases
    • Crawford, J. M., Vagstad, A. L., Ehrlich, K. C., Udwary, D. W. & Townsend, C. A. Acyl-carrier protein-phosphopantetheinyltransferase partnerships in fungal fatty acid synthases. Chembiochem 9, 1559-1563 (2008).
    • (2008) Chembiochem , vol.9 , pp. 1559-1563
    • Crawford, J.M.1    Vagstad, A.L.2    Ehrlich, K.C.3    Udwary, D.W.4    Townsend, C.A.5
  • 27
    • 42049099494 scopus 로고    scopus 로고
    • Deconstruction of iterative multidomain polyketide synthase function
    • Crawford, J. M. et al. Deconstruction of iterative multidomain polyketide synthase function. Science 320, 243-246 (2008).
    • (2008) Science , vol.320 , pp. 243-246
    • Crawford, J.M.1
  • 28
    • 70350496678 scopus 로고    scopus 로고
    • Structural basis for biosyntheticprogramming of fungal aromatic polyketide cyclization
    • Crawford, J. M. et al. Structural basis for biosyntheticprogramming of fungal aromatic polyketide cyclization.Nature 461, 1139-1143 (2009).
    • (2009) Nature , vol.461 , pp. 1139-1143
    • Crawford, J.M.1
  • 29
    • 77950901720 scopus 로고    scopus 로고
    • Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis
    • Korman, T. P. et al. Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis. Proc. Natl Acad. Sci. USA 107, 6246-6251 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 6246-6251
    • Korman, T.P.1
  • 30
    • 33845449100 scopus 로고    scopus 로고
    • Catalytic relationships between type i and type II iterative polyketide synthases: The Aspergillusparasiticus norsolorinic acid synthase
    • Ma, Y. et al. Catalytic relationships between type I and type II iterative polyketide synthases: the Aspergillusparasiticus norsolorinic acid synthase. Chembiochem 7, 1951-1958 (2006).
    • (2006) Chembiochem , vol.7 , pp. 1951-1958
    • Ma, Y.1
  • 31
    • 34249051051 scopus 로고    scopus 로고
    • Biochemical characterization of the minimal polyketide synthase domains in the lovastatin nonaketide synthase LovB
    • Ma, S. M. & Tang, Y. Biochemical characterization of the minimal polyketide synthase domains in the lovastatin nonaketide synthase LovB. FEBS J. 274, 2854-2864 (2007).
    • (2007) FEBS J. , vol.274 , pp. 2854-2864
    • Ma, S.M.1    Tang, Y.2
  • 32
    • 58549085193 scopus 로고    scopus 로고
    • Engineered biosynthesis of bacterial aromatic polyketides in Escherichia coli
    • Zhang, W., Li, Y. & Tang, Y. Engineered biosynthesis of bacterial aromatic polyketides in Escherichia coli. Proc. Natl Acad. Sci. USA 105, 20683-20688 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 20683-20688
    • Zhang, W.1    Li, Y.2    Tang, Y.3
  • 33
    • 84970596098 scopus 로고
    • Studies in relation to biosynthesis. VII. 2-hydroxy-6-methylbenzoic acid in Penicillium griseofulvum Dierckx
    • Birch, A. J., Massy-Westropp, R. A. & Moye, C. J. Studies in relation to biosynthesis. VII. 2-hydroxy-6-methylbenzoic acid in Penicillium griseofulvum Dierckx. Aus. J. Chem. 8, 539-544 (1955).
    • (1955) Aus. J. Chem. , vol.8 , pp. 539-544
    • Birch, A.J.1    Massy-Westropp, R.A.2    Moye, C.J.3
  • 36
    • 0000815060 scopus 로고
    • Applications of multinuclear NMR to structural and biosynthetic studies of polyketide microbial metabolites
    • Simpson, T. J. Applications of multinuclear NMR to structural and biosynthetic studies of polyketide microbial metabolites. Chem. Soc. Rev. 16, 123-160 (1987).
    • (1987) Chem. Soc. Rev. , vol.16 , pp. 123-160
    • Simpson, T.J.1
  • 37
    • 0344594238 scopus 로고    scopus 로고
    • eds Meth-Cohn, O., Barton, D. & Nakanishi, K. Elsevier, Oxford, UK
    • Townsend, C. & Minto, R. in Comprehensive Natural Products Chemistry Vol. 1 (eds Meth-Cohn, O., Barton, D. & Nakanishi, K.) 443-471 (Elsevier, Oxford, UK, 1999).
    • (1999) Comprehensive Natural Products Chemistry , vol.1 , pp. 443-471
    • Townsend, C.1    Minto, R.2
  • 38
    • 12144286398 scopus 로고    scopus 로고
    • Clustered pathway genes in aflatoxin biosynthesis
    • Yu, J. et al. Clustered pathway genes in aflatoxin biosynthesis. Appl. Environ. Microbiol. 70, 1253-1262 (2004).
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1253-1262
    • Yu, J.1
  • 39
    • 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. 64, 745-755 (2004).
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 745-755
    • Yabe, K.1    Nakajima, H.2
  • 40
    • 0029100271 scopus 로고
    • The Aspergillus parasiticus polyketide synthase gene pksA, a homolog of Aspergillus nidulans wA, is required for aflatoxin B1 biosynthesis
    • Chang, P. K., Cary, J. W., Yu, J., Bhatnagar, D. & Cleveland, T. E. The Aspergillus parasiticus polyketide synthase gene pksA, a homolog of Aspergillus nidulans wA, is required for aflatoxin B1 biosynthesis. Mol. Gen. Genet. 248, 270-277 (1995).
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 270-277
    • Chang, P.K.1    Cary, J.W.2    Yu, J.3    Bhatnagar, D.4    Cleveland, T.E.5
  • 41
    • 0030155688 scopus 로고    scopus 로고
    • Demonstration of the catalytic roles and evidence for the physical association of type i fatty acid synthases and a polyketide synthase in the biosynthesis of aflatoxin B1
    • Watanabe, C. M., Wilson, D., Linz, J. E. & Townsend, C. A. Demonstration of the catalytic roles and evidence for the physical association of type I fatty acid synthases and a polyketide synthase in the biosynthesis of aflatoxin B1. Chem. Biol. 3, 463-469 (1996).
    • (1996) Chem. Biol. , vol.3 , pp. 463-469
    • Watanabe, C.M.1    Wilson, D.2    Linz, J.E.3    Townsend, C.A.4
  • 43
    • 0000543572 scopus 로고
    • Hexanoate as a starter unit in polyketide biosynthesis
    • Townsend, C. A., Christensen, S. & Trautwein, K. Hexanoate as a starter unit in polyketide biosynthesis. J. Am. Chem. Soc. 106, 3868-3869 (1984).
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 3868-3869
    • Townsend, C.A.1    Christensen, S.2    Trautwein, K.3
  • 44
    • 0030069422 scopus 로고    scopus 로고
    • Biosynthesis of norsolorinic acid and averufin: Substrate specificity of norsolorinic acid synthase
    • McKeown, D. S. J., McNicholas, C., Simpson, T. J. & Willett, N. J. Biosynthesis of norsolorinic acid and averufin: substrate specificity of norsolorinic acid synthase. Chem. Commun. (Camb.) 1996, 301-302 (1996).
    • (1996) Chem. Commun. (Camb.) , vol.1996 , pp. 301-302
    • McKeown, D.S.J.1    McNicholas, C.2    Simpson, T.J.3    Willett, N.J.4
  • 46
    • 0029905023 scopus 로고    scopus 로고
    • Aspergillus has distinct fatty acid synthases for primary and secondary metabolism
    • Brown, D. W., Adams, T. H. & Keller, N. P. Aspergillus has distinct fatty acid synthases for primary and secondary metabolism. Proc. Natl Acad. Sci. USA 93, 14873-14877 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14873-14877
    • Brown, D.W.1    Adams, T.H.2    Keller, N.P.3
  • 47
    • 0035572966 scopus 로고    scopus 로고
    • 1 biosynthesis
    • 1 biosynthesis. Bioorg. Chem. 29, 293-307 (2001).
    • (2001) Bioorg. Chem. , vol.29 , pp. 293-307
    • Hitchman, T.1
  • 49
    • 34047210411 scopus 로고    scopus 로고
    • TP53 mutations and hepatocellular carcinoma: Insights into the etiology and pathogenesis of liver cancer
    • Hussain, S. P., Schwank, J., Staib, F., Wang, X. W. & Harris, C. C. TP53 mutations and hepatocellular carcinoma: insights into the etiology and pathogenesis of liver cancer. Oncogene 26, 2166-2176 (2007).
    • (2007) Oncogene , vol.26 , pp. 2166-2176
    • Hussain, S.P.1    Schwank, J.2    Staib, F.3    Wang, X.W.4    Harris, C.C.5
  • 50
    • 0036431904 scopus 로고    scopus 로고
    • The polyketide synthase gene pks4 from Gibberella fujikuroi encodes a key enzyme in the biosynthesis of the red pigment bikaverin
    • Linnemannstons, P. et al. The polyketide synthase gene pks4 from Gibberella fujikuroi encodes a key enzyme in the biosynthesis of the red pigment bikaverin. Fungal Genet. Biol. 37, 134-148 (2002).
    • (2002) Fungal Genet. Biol. , vol.37 , pp. 134-148
    • Linnemannstons, P.1
  • 51
    • 34848890676 scopus 로고    scopus 로고
    • Enzymatic synthesis of aromatic polyketides using PKS4 from Gibberella fujikuroi
    • Ma, S. M. et al. Enzymatic synthesis of aromatic polyketides using PKS4 from Gibberella fujikuroi. J. Am. Chem. Soc. 129, 10642-10643 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10642-10643
    • Ma, S.M.1
  • 52
    • 70350493673 scopus 로고    scopus 로고
    • Complete reconstitution of a highly reducing iterative polyketide synthase
    • Ma, S. M. et al. Complete reconstitution of a highly reducing iterative polyketide synthase. Science 326, 589-592 (2009).
    • (2009) Science , vol.326 , pp. 589-592
    • Ma, S.M.1
  • 53
    • 77950832433 scopus 로고    scopus 로고
    • Enzymatic synthesis of resorcylic acidlactones by cooperation of fungal iterative polyketidesynthases involved in hypothemycin biosynthesis
    • Zhou, H. et al. Enzymatic synthesis of resorcylic acidlactones by cooperation of fungal iterative polyketidesynthases involved in hypothemycin biosynthesis.J. Am. Chem. Soc. 132, 4530-4531 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4530-4531
    • Zhou, H.1
  • 54
    • 33644945871 scopus 로고    scopus 로고
    • Characterization of two polyketide synthase genes involved in zearalenone biosynthesis in Gibberella zeae
    • Gaffoor, I. & Trail, F. Characterization of two polyketide synthase genes involved in zearalenone biosynthesis in Gibberella zeae. Appl. Environ. Microbiol. 72, 1793-1799 (2006).
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1793-1799
    • Gaffoor, I.1    Trail, F.2
  • 55
    • 44049091848 scopus 로고    scopus 로고
    • A polyketide macrolactone synthase from the filamentous fungus Gibberella zeae
    • Zhou, H., Zhan, J., Watanabe, K., Xie, X. & Tang, Y. A polyketide macrolactone synthase from the filamentous fungus Gibberella zeae. Proc. Natl Acad. Sci. USA 105, 6249-6254 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 6249-6254
    • Zhou, H.1    Zhan, J.2    Watanabe, K.3    Xie, X.4    Tang, Y.5
  • 56
    • 50049117282 scopus 로고    scopus 로고
    • Genes for the biosynthesis of the fungal polyketides hypothemycin from Hypomyces subiculosus and radicicol from Pochonia chlamydosporia
    • Reeves, C. D., Hu, Z., Reid, R. & Kealey, J. T. Genes for the biosynthesis of the fungal polyketides hypothemycin from Hypomyces subiculosus and radicicol from Pochonia chlamydosporia. Appl. Environ. Microbiol. 74, 5121-5129 (2008).
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 5121-5129
    • Reeves, C.D.1    Hu, Z.2    Reid, R.3    Kealey, J.T.4
  • 57
    • 57649230837 scopus 로고    scopus 로고
    • Functional characterization of the biosynthesis of radicicol, an Hsp90 inhibitor resorcylic acid lactone from Chaetomium chiversii
    • Wang, S. et al. Functional characterization of the biosynthesis of radicicol, an Hsp90 inhibitor resorcylic acid lactone from Chaetomium chiversii. Chem. Biol. 15, 1328-1338 (2008).
    • (2008) Chem. Biol. , vol.15 , pp. 1328-1338
    • Wang, S.1
  • 58
    • 77949377752 scopus 로고    scopus 로고
    • Solution structure of an acyl carrier protein domain from a fungal type i polyketide synthase
    • Wattana-amorn, P. et al. Solution structure of an acyl carrier protein domain from a fungal type I polyketide synthase. Biochemistry 49, 2186-2193 (2010).
    • (2010) Biochemistry , vol.49 , pp. 2186-2193
    • Wattana-Amorn, P.1
  • 60
    • 77954937832 scopus 로고    scopus 로고
    • Classification prediction and verification of the regioselectivity of fungal polyketide synthase product template domains
    • Li, Y., Xu, W. & Tang, Y. Classification, prediction and verification of the regioselectivity of fungal polyketide synthase product template domains. J. Biol. Chem. 285, 22764-22773 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 22764-22773
    • Li, Y.1    Xu, W.2    Tang, Y.3
  • 61
    • 38349000749 scopus 로고    scopus 로고
    • Redirecting the cyclization steps offungal polyketide synthase
    • Ma, S. M. et al. Redirecting the cyclization steps offungal polyketide synthase. J. Am. Chem. Soc. 130,38-39 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 38-39
    • Ma, S.M.1
  • 62
    • 74849109709 scopus 로고    scopus 로고
    • Non-heme iron oxygenases generate natural structural diversity in carbapenem antibiotics
    • Bodner, M. J., Phelan, R. M., Freeman, M. F., Li, R. & Townsend, C. A. Non-heme iron oxygenases generate natural structural diversity in carbapenem antibiotics. J. Am. Chem. Soc. 132, 12-13 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 12-13
    • Bodner, M.J.1    Phelan, R.M.2    Freeman, M.F.3    Li, R.4    Townsend, C.A.5
  • 64
    • 0035802125 scopus 로고    scopus 로고
    • A biosynthetic classification of fungal and streptomycete fused-ring aromatic polyketides
    • Thomas, R. A biosynthetic classification of fungal and streptomycete fused-ring aromatic polyketides. Chembiochem 2, 612-627 (2001).
    • (2001) Chembiochem , vol.2 , pp. 612-627
    • Thomas, R.1
  • 65
    • 77953035258 scopus 로고    scopus 로고
    • Cyclization of aromatic polyketides from bacteria and fungi
    • Zhou, H., Li, Y. & Tang, Y. Cyclization of aromatic polyketides from bacteria and fungi. Nat. Prod. Rep. 27, 839-868 (2010).
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 839-868
    • Zhou, H.1    Li, Y.2    Tang, Y.3
  • 66
    • 70449427465 scopus 로고    scopus 로고
    • Multiple convergence in polyketidebiosyn thesis:a third folding mode to the anthraquinone chrysophanol
    • Bringmann, G., Gulder, T. A., Hamm, A., Goodfellow, M. & Fiedler, H. P. Multiple convergence in polyketidebiosynthesis: a third folding mode to the anthraquinone chrysophanol. Chem. Commun. (Camb.) 2009, 6810-6812 (2009).
    • (2009) Chem. Commun. (Camb.) , vol.2009 , pp. 6810-6812
    • Bringmann, G.1    Gulder, T.A.2    Hamm, A.3    Goodfellow, M.4    Fiedler, H.P.5
  • 67
    • 51149098989 scopus 로고    scopus 로고
    • The crystalstructure of a mammalian fatty acid synthase
    • Maier, T., Leibundgut, M. & Ban, N. The crystalstructure of a mammalian fatty acid synthase. Science321, 1315-1322 (2008).
    • (2008) Science , vol.321 , pp. 1315-1322
    • Maier, T.1    Leibundgut, M.2    Ban, N.3
  • 68
    • 13244267005 scopus 로고    scopus 로고
    • The Hotdog fold: Wrapping up a superfamily of thioesterases and dehydratases
    • Dillon, S. C. & Bateman, A. The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases. BMC Bioinformatics 5, 109 (2004).
    • (2004) BMC Bioinformatics , vol.5 , pp. 109
    • Dillon, S.C.1    Bateman, A.2
  • 69
    • 0030584655 scopus 로고    scopus 로고
    • Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: Two catalytic activities in one active site
    • Leesong, M., Henderson, B. S., Gillig, J. R., Schwab, J. M. & Smith, J. L. Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 4, 253-264 (1996).
    • (1996) Structure , vol.4 , pp. 253-264
    • Leesong, M.1    Henderson, B.S.2    Gillig, J.R.3    Schwab, J.M.4    Smith, J.L.5
  • 70
    • 56249096167 scopus 로고    scopus 로고
    • Crystal structure of the erythromycin polyketide synthase dehydratase
    • Keatinge-Clay, A. Crystal structure of the erythromycin polyketide synthase dehydratase. J. Mol. Biol. 384, 941-953 (2008).
    • (2008) J. Mol. Biol. , vol.384 , pp. 941-953
    • Keatinge-Clay, A.1
  • 71
    • 11844302312 scopus 로고    scopus 로고
    • Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzymetype 2
    • Koski, K. M., Haapalainen, A. M., Hiltunen, J. K. & Glumoff, T. Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzymetype 2. J. Mol. Biol. 345, 1157-1169 (2005).
    • (2005) J. Mol. Biol. , vol.345 , pp. 1157-1169
    • Koski, K.M.1    Haapalainen, A.M.2    Hiltunen, J.K.3    Glumoff, T.4
  • 72
    • 0347994901 scopus 로고    scopus 로고
    • Phylogenomic analysis of type i polyketide synthase genes in pathogenic and saprobic ascomycetes
    • Kroken, S., Glass, N. L., Taylor, J. W., Yoder, O. C. & Turgeon, B. G. Phylogenomic analysis of type I polyketide synthase genes in pathogenic and saprobic ascomycetes. Proc. Natl Acad. Sci. USA 100, 15670-15675 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15670-15675
    • Kroken, S.1    Glass, N.L.2    Taylor, J.W.3    Yoder, O.C.4    Turgeon, B.G.5
  • 73
    • 0000884859 scopus 로고
    • Solvent effects on keto-enol equilibria: Tests of quantitative models
    • Mills, S. G. & Beak, P. Solvent effects on keto-enol equilibria: tests of quantitative models. J. Org. Chem. 50, 1216-1224 (1985).
    • (1985) J. Org. Chem. , vol.50 , pp. 1216-1224
    • Mills, S.G.1    Beak, P.2
  • 74
    • 77956715871 scopus 로고
    • Hydrogen bonding and chemical reactivity
    • Hibbert, F. & Emsley, P. Hydrogen bonding and chemical reactivity. Adv. Phys. Org. Chem. 26, 255-379 (1991).
    • (1991) Adv. Phys. Org. Chem. , vol.26 , pp. 255-379
    • Hibbert, F.1    Emsley, P.2
  • 75
    • 44449157594 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of tetracenomycin ARO/CYC: Implications for cyclization specificity of aromatic polyketides
    • Ames, B. D. et al. Crystal structure and functional analysis of tetracenomycin ARO/CYC: implications for cyclization specificity of aromatic polyketides. Proc. Natl Acad. Sci. USA 105, 5349-5354 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 5349-5354
    • Ames, B.D.1
  • 76
    • 0035342462 scopus 로고    scopus 로고
    • Adaptations of the helix-grip fold for ligand binding and catalysis in the START domain superfamily
    • Iyer, L. M., Koonin, E. V. & Aravind, L. Adaptations of the helix-grip fold for ligand binding and catalysis in the START domain superfamily. Proteins 43, 134-144 (2001).
    • (2001) Proteins , vol.43 , pp. 134-144
    • Iyer, L.M.1    Koonin, E.V.2    Aravind, L.3
  • 77
    • 34250790717 scopus 로고    scopus 로고
    • Polyketides proteins and genes in fungi: Programmed nano-machines begin to reveal their secrets
    • Cox, R. J. Polyketides, proteins and genes in fungi: programmed nano-machines begin to reveal their secrets. Org. Biomol. Chem. 5, 2010-2026 (2007).
    • (2007) Org. Biomol. Chem. , vol.5 , pp. 2010-2026
    • Cox, R.J.1
  • 78
    • 57449105688 scopus 로고    scopus 로고
    • Identification and characterization of the asperthecin gene cluster of Aspergillus nidulans
    • Szewczyk, E. et al. Identification and characterization of the asperthecin gene cluster of Aspergillus nidulans. Appl. Environ. Microbiol. 74, 7607-7612 (2008).
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 7607-7612
    • Szewczyk, E.1
  • 79
    • 77954200418 scopus 로고    scopus 로고
    • Identification of the viridicatumtoxin and griseofulvin gene clusters from Penicillium aethiopicum
    • Chooi, Y. H., Cacho, R. & Tang, Y. Identification of the viridicatumtoxin and griseofulvin gene clusters from Penicillium aethiopicum. Chem. Biol. 17, 483-494 (2010).
    • (2010) Chem. Biol. , vol.17 , pp. 483-494
    • Chooi, Y.H.1    Cacho, R.2    Tang, Y.3
  • 80
    • 76249090018 scopus 로고    scopus 로고
    • PKS and NRPS release mechanisms
    • Du, L. & Lou, L. PKS and NRPS release mechanisms. Nat. Prod. Rep. 27, 255-278 (2010).
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 255-278
    • Du, L.1    Lou, L.2
  • 81
    • 0032890191 scopus 로고    scopus 로고
    • Re-identification of Aspergillus nidulans wA gene to code for a polyketide synthase of naphthopyrone
    • Watanabe, A. et al. Re-identification of Aspergillus nidulans wA gene to code for a polyketide synthase of naphthopyrone. Tetrahedron Lett. 40, 91-94 (1999).
    • (1999) Tetrahedron Lett. , vol.40 , pp. 91-94
    • Watanabe, A.1
  • 82
    • 0032532795 scopus 로고    scopus 로고
    • Product identification of polyketide synthase coded by Aspergillus nidulans wA gene
    • Watanabe, A. et al. Product identification of polyketide synthase coded by Aspergillus nidulans wA gene. Tetrahedron Lett. 39, 7733-7736 (1998).
    • (1998) Tetrahedron Lett. , vol.39 , pp. 7733-7736
    • Watanabe, A.1
  • 83
    • 0035068075 scopus 로고    scopus 로고
    • Identification of Claisen cyclase domain in fungal polyketide synthase WA, a naphthopyrone synthase of Aspergillus nidulans
    • Fujii, I., Watanabe, A., Sankawa, U. & Ebizuka, Y. Identification of Claisen cyclase domain in fungal polyketide synthase WA, a naphthopyrone synthase of Aspergillus nidulans. Chem. Biol. 8, 189-197 (2001).
    • (2001) Chem. Biol. , vol.8 , pp. 189-197
    • Fujii, I.1    Watanabe, A.2    Sankawa, U.3    Ebizuka, Y.4
  • 84
    • 4344598398 scopus 로고    scopus 로고
    • Unprecedented mechanism of chain length determination in fungal aromatic polyketide synthases
    • Watanabe, A. & Ebizuka, Y. Unprecedented mechanism of chain length determination in fungal aromatic polyketide synthases. Chem. Biol. 11, 1101-1106 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 1101-1106
    • Watanabe, A.1    Ebizuka, Y.2
  • 85
    • 0035800758 scopus 로고    scopus 로고
    • Pentaketide melanin biosynthesis in Aspergillus fumigatus requires chain-length shortening of a heptaketide precursor
    • Tsai, H. F. et al. Pentaketide melanin biosynthesis in Aspergillus fumigatus requires chain-length shortening of a heptaketide precursor. J. Biol. Chem. 276, 29292-29298 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29292-29298
    • Tsai, H.F.1
  • 86
    • 70349581781 scopus 로고    scopus 로고
    • Melanin is an essential component for the integrity of the cell wall of Aspergillus fumigatus conidia
    • Pihet, M. et al. Melanin is an essential component for the integrity of the cell wall of Aspergillus fumigatus conidia. BMC Microbiol. 9, 177 (2009).
    • (2009) BMC Microbiol. , vol.9 , pp. 177
    • Pihet, M.1
  • 87
    • 0037373742 scopus 로고    scopus 로고
    • Biosynthesis of fungal melanins and their importance for human pathogenic fungi
    • Langfelder, K., Streibel, M., Jahn, B., Haase, G. & Brakhage, A. A. Biosynthesis of fungal melanins and their importance for human pathogenic fungi. Fungal Genet. Biol. 38, 143-158 (2003).
    • (2003) Fungal Genet. Biol. , vol.38 , pp. 143-158
    • Langfelder, K.1    Streibel, M.2    Jahn, B.3    Haase, G.4    Brakhage, A.A.5
  • 88
    • 69749095952 scopus 로고    scopus 로고
    • Color me bad: Microbial pigments as virulence factors
    • Liu, G. Y. & Nizet, V. Color me bad: microbial pigments as virulence factors. Trends Microbiol. 17, 406-413 (2009).
    • (2009) Trends Microbiol. , vol.17 , pp. 406-413
    • Liu, G.Y.1    Nizet, V.2
  • 89
    • 0033173472 scopus 로고    scopus 로고
    • Heterologous expression and product identification of Colletotrichum lagenarium polyketide synthase encoded by the PKS1 gene involved in melanin biosynthesis
    • Fujii, I. et al. Heterologous expression and product identification of Colletotrichum lagenarium polyketide synthase encoded by the PKS1 gene involved in melanin biosynthesis. Biosci. Biotechnol. Biochem. 63, 1445-1452 (1999).
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 1445-1452
    • Fujii, I.1
  • 90
    • 0034254579 scopus 로고    scopus 로고
    • Enzymatic synthesis of 1 3 6,8-tetra-hydroxy naphthalene solely from malonyl coenzyme A by a fungal iterative type i polyketide synthase PKS1
    • Fujii, I. et al. Enzymatic synthesis of 1,3,6,8-tetra-hydroxy naphthalene solely from malonyl coenzyme A by a fungal iterative type I polyketide synthase PKS1. Biochemistry 39, 8853-8858 (2000).
    • (2000) Biochemistry , vol.39 , pp. 8853-8858
    • Fujii, I.1
  • 91
    • 0011218967 scopus 로고
    • 2H labelling studies on the biosynthesis of scytalone in Phialaphora lagerbergii
    • 2H labelling studies on the biosynthesis of scytalone in Phialaphora lagerbergii. Tetrahedron 39, 3539-3542 (1983).
    • (1983) Tetrahedron , vol.39 , pp. 3539-3542
    • Bardshiri, E.1    Simpson, T.J.2
  • 92
    • 54249111559 scopus 로고    scopus 로고
    • New biosynthetic step in the melanin pathway of Wangiella (Exophiala) dermatitidis: Evidence for 2-acetyl-1 3 6,8-tetra hydroxynaphthalene as a novel precursor
    • Wheeler, M. H. et al. New biosynthetic step in the melanin pathway of Wangiella (Exophiala) dermatitidis: evidence for 2-acetyl-1,3,6,8-tetra hydroxynaphthalene as a novel precursor. Eukaryot. Cell 7, 1699-1711 (2008).
    • (2008) Eukaryot. Cell , vol.7 , pp. 1699-1711
    • Wheeler, M.H.1
  • 93
    • 77952922758 scopus 로고    scopus 로고
    • Functional analysis of fungal polyketide biosynthesis genes
    • Fujii, I. Functional analysis of fungal polyketide biosynthesis genes. J. Antibiot. 63, 207-218 (2010).
    • (2010) J. Antibiot. , vol.63 , pp. 207-218
    • Fujii, I.1
  • 94
    • 0032784276 scopus 로고    scopus 로고
    • W. a/b hydrolase fold enzymes: The family keeps growing
    • Nardini, M. & Dijkstra, B. W. a/b hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol. 9, 732-737 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.2
  • 95
    • 0024280501 scopus 로고
    • Dissecting the catalytic triad of a serine protease
    • Carter, P. & Wells, J. Dissecting the catalytic triad of a serine protease. Nature 332, 564-568 (1988).
    • (1988) Nature , vol.332 , pp. 564-568
    • Carter, P.1    Wells, J.2
  • 96
    • 49649122848 scopus 로고    scopus 로고
    • Structural basis for the selectivity of the external thioesterase of the surfactin synthetase
    • Koglin, A. et al. Structural basis for the selectivity of the external thioesterase of the surfactin synthetase. Nature 454, 907-911 (2008).
    • (2008) Nature , vol.454 , pp. 907-911
    • Koglin, A.1
  • 97
    • 49649129083 scopus 로고    scopus 로고
    • Dynamic thiolation-thioesterase structure of a non-ribosomal peptide synthetase
    • Frueh, D. P. et al. Dynamic thiolation-thioesterase structure of a non-ribosomal peptide synthetase. Nature 454, 903-906 (2008).
    • (2008) Nature , vol.454 , pp. 903-906
    • Frueh, D.P.1
  • 98
    • 44049097046 scopus 로고    scopus 로고
    • Covalent linkage mediates communication between ACP and TE domains in modular polyketide synthases
    • Tran, L., Tosin, M., Spencer, J. B., Leadlay, P. F. & Weissman, K. J. Covalent linkage mediates communication between ACP and TE domains in modular polyketide synthases. Chembiochem 9, 905-915 (2008).
    • (2008) Chembiochem , vol.9 , pp. 905-915
    • Tran, L.1    Tosin, M.2    Spencer, J.B.3    Leadlay, P.F.4    Weissman, K.J.5
  • 99
    • 0033591447 scopus 로고    scopus 로고
    • Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis
    • Kennedy, J. et al. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 284, 1368-1372 (1999).
    • (1999) Science , vol.284 , pp. 1368-1372
    • Kennedy, J.1
  • 100
    • 69849085103 scopus 로고    scopus 로고
    • Production of octaketide polyenes by the calicheamicin polyketide synthase CalE8: Implications for the biosynthesis of enediyne core structures
    • Belecki, K., Crawford, J. M. & Townsend, C. A. Production of octaketide polyenes by the calicheamicin polyketide synthase CalE8: implications for the biosynthesis of enediyne core structures. J. Am. Chem. Soc. 131, 12564-12566 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12564-12566
    • Belecki, K.1    Crawford, J.M.2    Townsend, C.A.3
  • 101
    • 30544434099 scopus 로고    scopus 로고
    • Fungal secondary metabolism from biochemistry to genomics
    • Keller, N. P., Turner, G. & Bennett, J. W. Fungal secondary metabolism from biochemistry to genomics. Nature Rev. Microbiol. 3, 937-947 (2005).
    • (2005) Nature Rev. Microbiol. , vol.3 , pp. 937-947
    • Keller, N.P.1    Turner, G.2    Bennett, J.W.3
  • 102
    • 29244442741 scopus 로고    scopus 로고
    • Genome sequencing and analysis of Aspergillus oryzae
    • Machida, M. et al. Genome sequencing and analysis of Aspergillus oryzae. Nature 438, 1157-1161 (2005).
    • (2005) Nature , vol.438 , pp. 1157-1161
    • MacHida, M.1
  • 103
    • 28644434509 scopus 로고    scopus 로고
    • Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus
    • Nierman, W. C. et al. Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus. Nature 438, 1151-1156 (2005).
    • (2005) Nature , vol.438 , pp. 1151-1156
    • Nierman, W.C.1
  • 104
    • 28844461287 scopus 로고    scopus 로고
    • Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus andA. oryzae
    • Galagan, J. E. et al. Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus andA. oryzae. Nature 438, 1105-1115 (2005).
    • (2005) Nature , vol.438 , pp. 1105-1115
    • Galagan, J.E.1
  • 105
    • 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. 24, 393-416 (2007).
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 393-416
    • Hoffmeister, D.1    Keller, N.P.2
  • 106
    • 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. 124, 690-703 (2006).
    • (2006) J. Biotechnol. , vol.124 , pp. 690-703
    • Schumann, J.1    Hertweck, C.2
  • 108
    • 64549150542 scopus 로고    scopus 로고
    • Triggering cryptic natural product biosynthesis in microorganisms
    • Scherlach, K. & Hertweck, C. Triggering cryptic natural product biosynthesis in microorganisms. Org. Biomol. Chem. 7, 1753-1760 (2009).
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 1753-1760
    • Scherlach, K.1    Hertweck, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.