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Volumn 69, Issue 7, 2016, Pages 500-506

Recent advances of Diels-Alderases involved in natural product biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

DECALIN; ENZYME; MACROCYCLIC COMPOUND; NATURAL PRODUCT; PYRI4 ENZYME; PYRIDINE DERIVATIVE; UNCLASSIFIED DRUG; BIOLOGICAL PRODUCT; ISOMERASE; MACROPHOMATE SYNTHASE; MULTIENZYME COMPLEX; NAPHTHALENE DERIVATIVE; POLYKETIDE SYNTHASE; SOLANAPYRONE SYNTHASE;

EID: 84979766161     PISSN: 00218820     EISSN: 18811469     Source Type: Journal    
DOI: 10.1038/ja.2016.67     Document Type: Review
Times cited : (87)

References (52)
  • 2
    • 70350496831 scopus 로고    scopus 로고
    • Recent applications of intramolecular Diels-Alder reactions to natural product synthesis
    • Juhl, M., Tanner, D. Recent applications of intramolecular Diels-Alder reactions to natural product synthesis. Chem. Soc. Rev. 38, 2983-2992 (2009).
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 2983-2992
    • Juhl, M.1    Tanner, D.2
  • 5
    • 3042745794 scopus 로고    scopus 로고
    • Enzymatic catalysis of the Diels-Alder reaction in the biosynthesis of natural products
    • Oikawa, H., Tokiwano, T. Enzymatic catalysis of the Diels-Alder reaction in the biosynthesis of natural products. Nat. Prod. Rep. 21, 321-352 (2004).
    • (2004) Nat. Prod. Rep. , vol.21 , pp. 321-352
    • Oikawa, H.1    Tokiwano, T.2
  • 7
    • 0001340562 scopus 로고
    • Novel C-35 terpenoids from the panamanian liverwort Plagiochila moritziana
    • Spole, J., Becker, H., Gupta, M. P., Beith, M., Huch, V. Novel C-35 terpenoids from the panamanian liverwort Plagiochila moritziana. Tetrahedron 45, 5003-5014 (1989).
    • (1989) Tetrahedron , vol.45 , pp. 5003-5014
    • Spole, J.1    Becker, H.2    Gupta, M.P.3    Beith, M.4    Huch, V.5
  • 8
    • 0031886215 scopus 로고    scopus 로고
    • A novel bicyclo[2.2.2]octane skeleton diterpene, obtunone, from the heartwood of Chamaecyparis obtusa var. Formosana
    • Kuo, Y. H., Chan, C. H., Huang, S. L. A novel bicyclo[2.2.2]octane skeleton diterpene, obtunone, from the heartwood of Chamaecyparis obtusa var. formosana. Chem. Pharm. Bull. 46, 181-183 (1998).
    • (1998) Chem. Pharm. Bull. , vol.46 , pp. 181-183
    • Kuo, Y.H.1    Chan, C.H.2    Huang, S.L.3
  • 10
    • 0017372513 scopus 로고
    • Ircinianin a novel sesterterpene from a marine sponge
    • Hofheinz, W., Schonholzer, P. Ircinianin, a novel sesterterpene from a marine sponge. Helv. Chim. Acta 60, 1367-1370 (1977).
    • (1977) Helv. Chim. Acta , vol.60 , pp. 1367-1370
    • Hofheinz, W.1    Schonholzer, P.2
  • 11
    • 0002712007 scopus 로고
    • Structures of chaetoglobosin A and B, cytotoxic metabolites of Chaetomium globosum
    • Sekita, S., Yoshihira, K., Natori, S., Kuwano, H. Structures of chaetoglobosin A and B, cytotoxic metabolites of Chaetomium globosum. Tetrahedron Lett. 14, 2109-2112 (1973).
    • (1973) Tetrahedron Lett. , vol.14 , pp. 2109-2112
    • Sekita, S.1    Yoshihira, K.2    Natori, S.3    Kuwano, H.4
  • 12
    • 26844455704 scopus 로고    scopus 로고
    • Biomimetic synthesis of grandione from demethylsalvicanol via hetero-Diels-Alder type dimerization and structure revision of grandione
    • Aoyagi, Y. et al. Biomimetic synthesis of grandione from demethylsalvicanol via hetero-Diels-Alder type dimerization and structure revision of grandione. Tetrahedron Lett. 46, 7885-7887 (2005).
    • (2005) Tetrahedron Lett. , vol.46 , pp. 7885-7887
    • Aoyagi, Y.1
  • 13
    • 37049086431 scopus 로고
    • Enzymatic activity catalysing exo-selective Diels-Alder reaction in solanapyrone biosynthesis
    • Oikawa, H., Katayama, K., Suzuki, Y., Ichihara, A. Enzymatic activity catalysing exo-selective Diels-Alder reaction in solanapyrone biosynthesis. J. Chem. Soc. Chem. Commun. 1321-1322 (1995).
    • (1995) J. Chem. Soc. Chem. Commun. , pp. 1321-1322
    • Oikawa, H.1    Katayama, K.2    Suzuki, Y.3    Ichihara, A.4
  • 14
    • 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
  • 15
    • 0034032829 scopus 로고    scopus 로고
    • Macrophomate synthase: Characterization, sequence, and expression in Escherichia coli of the novel enzyme catalyzing unusual multistep transformation of 2-pyrones to benzoates
    • Watanabe, K. et al. Macrophomate synthase: Characterization, sequence, and expression in Escherichia coli of the novel enzyme catalyzing unusual multistep transformation of 2-pyrones to benzoates. J. Biochem. 127, 467-473 (2000).
    • (2000) J. Biochem. , vol.127 , pp. 467-473
    • Watanabe, K.1
  • 16
    • 0033578709 scopus 로고    scopus 로고
    • Macrophomate synthase: Unusual enzyme catalyzing multiple reactions from pyrones to benzoates
    • Oikawa, H. et al. Macrophomate synthase: Unusual enzyme catalyzing multiple reactions from pyrones to benzoates. Tetrahedron Lett. 40, 6983-6986 (1999).
    • (1999) Tetrahedron Lett. , vol.40 , pp. 6983-6986
    • Oikawa, H.1
  • 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. 106, 3468-3496 (2006).
    • (2006) Chem. Rev. , vol.106 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 18
    • 33644642932 scopus 로고    scopus 로고
    • Comparative Diels-Alder reactivities within a family of valence bond isomers: A biomimetic total synthesis of (+/-)-UCS1025A
    • Hoye, T. R., Dvornikovs, V. Comparative Diels-Alder reactivities within a family of valence bond isomers: a biomimetic total synthesis of (+/-)-UCS1025A. J. Am. Chem. Soc. 128, 2550-2551 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2550-2551
    • Hoye, T.R.1    Dvornikovs, V.2
  • 19
    • 0013628039 scopus 로고
    • Structures of betaenones A and B, novel phytotoxins from Phoma betae Fr
    • Ichihara, A., Oikawa, H., Hayashi, K., Sakamura, S. Structures of betaenones A and B, novel phytotoxins from Phoma betae Fr. J. Am. Chem. Soc. 105, 2907 (1983).
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 2907
    • Ichihara, A.1    Oikawa, H.2    Hayashi, K.3    Sakamura, S.4
  • 20
    • 0021042268 scopus 로고
    • A phytotoxin, betaenone C, and its related metabolites of Phoma betae Fr
    • Ichihara, A. et al. A phytotoxin, betaenone C, and its related metabolites of Phoma betae Fr. Agric. Biol. Chem. 47, 2965 (1983).
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 2965
    • Ichihara, A.1
  • 21
    • 84921451458 scopus 로고    scopus 로고
    • Heterologous expression of highly reducing polyketide synthase involved in betaenone biosynthesis
    • Ugai, T. et al. Heterologous expression of highly reducing polyketide synthase involved in betaenone biosynthesis. Chem. Commun. 51, 1878-1881 (2015).
    • (2015) Chem. Commun. , vol.51 , pp. 1878-1881
    • Ugai, T.1
  • 22
    • 37049072185 scopus 로고
    • Synthesis of (-)-probetaenone I: Structural conformation of biosynthetic precursor of betaenone B
    • Miki, S. et al. Synthesis of (-)-probetaenone I: Structural conformation of biosynthetic precursor of betaenone B. J. Chem. Soc. Perkin Trans. 1, 1228-1229 (1990).
    • (1990) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 1228-1229
    • Miki, S.1
  • 23
    • 79955697167 scopus 로고    scopus 로고
    • Fusarisetin A, an acinar morphogenesis inhibitor from a soil fungus, Fusarium sp. FN080326
    • Jang, J. H. et al. Fusarisetin A, an acinar morphogenesis inhibitor from a soil fungus, Fusarium sp. FN080326. J. Am. Chem. Soc. 133, 6865-6867 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 6865-6867
    • Jang, J.H.1
  • 24
    • 84937765426 scopus 로고    scopus 로고
    • A new enzyme involved in the control of the stereochemistry in the decalin formation during equisetin biosynthesis
    • Kato, K. et al. A new enzyme involved in the control of the stereochemistry in the decalin formation during equisetin biosynthesis. Biochem. Biophys. Res. Commun. 460, 210-215 (2015).
    • (2015) Biochem. Biophys. Res. Commun. , vol.460 , pp. 210-215
    • Kato, K.1
  • 25
    • 84929598168 scopus 로고    scopus 로고
    • Biosynthesis of the tetramic acids Sch210971 and Sch210972
    • Kakule, T. B., Zhang, S., Zhan, J., Schmidt, E. W. Biosynthesis of the tetramic acids Sch210971 and Sch210972. Org. Lett. 17, 2295-2297 (2015).
    • (2015) Org. Lett. , vol.17 , pp. 2295-2297
    • Kakule, T.B.1    Zhang, S.2    Zhan, J.3    Schmidt, E.W.4
  • 26
    • 84945190547 scopus 로고    scopus 로고
    • Involvement of lipocalin-like CghA in decalin-forming stereoselective intramolecular [4+2] cycloaddition
    • Sato, M. et al. Involvement of lipocalin-like CghA in decalin-forming stereoselective intramolecular [4+2] cycloaddition. Chem Bio Chem 16, 2294-2298 (2015).
    • (2015) Chem Bio Chem , vol.16 , pp. 2294-2298
    • Sato, M.1
  • 27
    • 84880534232 scopus 로고    scopus 로고
    • Two related pyrrolidinedione synthetase loci in Fusarium heterosporum ATCC74349 produce divergent metabolites
    • Kakule, T. B., Sardar, D., Lin, Z., Schmidt, E. W. Two related pyrrolidinedione synthetase loci in Fusarium heterosporum ATCC74349 produce divergent metabolites. ACS Chem. Biol. 8, 1549-1557 (2013).
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1549-1557
    • Kakule, T.B.1    Sardar, D.2    Lin, Z.3    Schmidt, E.W.4
  • 28
    • 84929590050 scopus 로고    scopus 로고
    • Native promoter strategy for high-yielding synthesis and engineering of fungal secondary metabolites
    • Kakule, T. B. et al. Native promoter strategy for high-yielding synthesis and engineering of fungal secondary metabolites. ACS. Synth. Biol. 4, 625-633 (2015).
    • (2015) ACS. Synth. Biol. , vol.4 , pp. 625-633
    • Kakule, T.B.1
  • 29
    • 80555131032 scopus 로고    scopus 로고
    • Identification and engineering of the cytochalasin gene cluster from Aspergillus clavatus NRRL 1
    • Qiao, K., Chooi, Y.-H., Tang, Y. Identification and engineering of the cytochalasin gene cluster from Aspergillus clavatus NRRL 1. Metab. Eng. 13, 723-732 (2011).
    • (2011) Metab. Eng. , vol.13 , pp. 723-732
    • Qiao, K.1    Chooi, Y.-H.2    Tang, Y.3
  • 30
    • 0028073170 scopus 로고
    • Pyrroindomycins, novel antibiotics produced by Streptomyces rugosporus sp. LL-42D005. I. Isolation and structure determination
    • Singh, M. P. et al. Pyrroindomycins, novel antibiotics produced by Streptomyces rugosporus sp. LL-42D005. I. Isolation and structure determination. J. Antibiot. 47, 1250-1257 (1994).
    • (1994) J. Antibiot. , vol.47 , pp. 1250-1257
    • Singh, M.P.1
  • 31
    • 0028102973 scopus 로고
    • Pyrroindomycins, novel antibiotics produced by Streptomyces rugosporus sp. LL-42D005. II. Biological activities
    • Singh, M. P. et al. Pyrroindomycins, novel antibiotics produced by Streptomyces rugosporus sp. LL-42D005. II. Biological activities. J. Antibiot. 47, 1258-1265 (1994).
    • (1994) J. Antibiot. , vol.47 , pp. 1258-1265
    • Singh, M.P.1
  • 32
    • 84926453060 scopus 로고    scopus 로고
    • An enzymatic [4+2] cyclization cascade creates the pentacyclic core of pyrroindomycins
    • Tian, Z. et al. An enzymatic [4+2] cyclization cascade creates the pentacyclic core of pyrroindomycins. Nat. Chem. Biol. 11, 259-265 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 259-265
    • Tian, Z.1
  • 33
    • 84921516173 scopus 로고    scopus 로고
    • Biosynthesis of versipelostatin: Identification of an enzymecatalyzed [4+2]-cycloaddition required for macrocyclization of spirotetronatecontaining polyketides
    • Hashimoto, T. et al. Biosynthesis of versipelostatin: Identification of an enzymecatalyzed [4+2]-cycloaddition required for macrocyclization of spirotetronatecontaining polyketides. J. Am. Chem. Soc. 137, 572-575 (2015).
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 572-575
    • Hashimoto, T.1
  • 34
    • 33745184421 scopus 로고    scopus 로고
    • Genetic characterization of the chlorothricin gene cluster as a model for spirotetronate antibiotic biosynthesis
    • Jia, X.-Y. et al. Genetic characterization of the chlorothricin gene cluster as a model for spirotetronate antibiotic biosynthesis. Chem. Biol. 13, 575-585 (2006).
    • (2006) Chem. Biol. , vol.13 , pp. 575-585
    • Jia, X.-Y.1
  • 35
    • 36749055680 scopus 로고    scopus 로고
    • Elucidation of the kijanimicin gene cluster: Insights into the biosynthesis of spirotetronate antibiotics and nitrosugars
    • Zhang, H. et al. Elucidation of the kijanimicin gene cluster: Insights into the biosynthesis of spirotetronate antibiotics and nitrosugars. J. Am. Chem. Soc. 129, 14670-14683 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14670-14683
    • Zhang, H.1
  • 36
    • 50249101630 scopus 로고    scopus 로고
    • Cloning and characterization of the tetrocarcin A gene cluster from Micromonospora chalcea NRRL11289 reveals a highly conserved strategy for tetronate biosynthesis in spirotetronate antibiotics
    • Fang, J. et al. Cloning and characterization of the tetrocarcin A gene cluster from Micromonospora chalcea NRRL11289 reveals a highly conserved strategy for tetronate biosynthesis in spirotetronate antibiotics. J. Bacteriol. 190, 6014-6025 (2008).
    • (2008) J. Bacteriol. , vol.190 , pp. 6014-6025
    • Fang, J.1
  • 37
    • 77953375007 scopus 로고    scopus 로고
    • Solanapyrone synthase, a possible Diels-Alderase and iterative type i polyketide synthase encoded in a biosynthetic gene cluster from Alternaria solani
    • Kasahara, K. et al. Solanapyrone synthase, a possible Diels-Alderase and iterative type I polyketide synthase encoded in a biosynthetic gene cluster from Alternaria solani. Chem Bio Chem 14, 1245-1252 (2010).
    • (2010) Chem Bio Chem , vol.14 , pp. 1245-1252
    • Kasahara, K.1
  • 38
    • 70350493673 scopus 로고    scopus 로고
    • Complete reconstitution of a highly reducing iterative polyketide synthase
    • 38Ma, 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
  • 39
    • 0025917476 scopus 로고
    • A83543A-D, unique fermentation-derived tetracyclic macrolides
    • Kirst, H. A. et al. A83543A-D, unique fermentation-derived tetracyclic macrolides. Tetrahedron Lett. 32, 4839-4842 (1991).
    • (1991) Tetrahedron Lett. , vol.32 , pp. 4839-4842
    • Kirst, H.A.1
  • 40
    • 0035017135 scopus 로고    scopus 로고
    • Cloning and analysis of the spinosad biosynthetic gene cluster of Saccharopolyspora spinosa
    • Waldron, C et al. Cloning and analysis of the spinosad biosynthetic gene cluster of Saccharopolyspora spinosa. Chem. Biol. 8, 487-499 (2001).
    • (2001) Chem. Biol. , vol.8 , pp. 487-499
    • Waldron, C.1
  • 41
    • 79955642774 scopus 로고    scopus 로고
    • Enzyme-catalysed [4+2] cycloaddition is a key step in the biosynthesis of spinosyn A
    • Kim, H. J., Ruszczycky, M. W., Choi, S. H., Liu, H.-W. Enzyme-catalysed [4+2] cycloaddition is a key step in the biosynthesis of spinosyn A. Nature 473, 109-112 (2001).
    • (2001) Nature , vol.473 , pp. 109-112
    • Kim, H.J.1    Ruszczycky, M.W.2    Choi, S.H.3    Liu, H.-W.4
  • 42
    • 84926472764 scopus 로고    scopus 로고
    • The structure of SpnF, a standalone enzyme that catalyzes [4+2] cycloaddition
    • Fage, C. D. et al. The structure of SpnF, a standalone enzyme that catalyzes [4+2] cycloaddition. Nat. Chem. Biol. 11, 256-268 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 256-268
    • Fage, C.D.1
  • 43
    • 84962109823 scopus 로고    scopus 로고
    • Dynamically complex [6+4] and [4+2] cycloadditions in the biosynthesis of spinosyn A
    • Patel, A. et al. Dynamically complex [6+4] and [4+2] cycloadditions in the biosynthesis of spinosyn A. J. Am. Chem. Soc. 138, 3631-3634 (2016).
    • (2016) J. Am. Chem. Soc. , vol.138 , pp. 3631-3634
    • Patel, A.1
  • 44
    • 77956253458 scopus 로고    scopus 로고
    • Thiazolyl peptide antibiotic biosynthesis: A cascade of post-translational modifications on ribosomal nascent proteins
    • Walsh, C. T., Acker, M. G., Bowers, A. A. Thiazolyl peptide antibiotic biosynthesis: a cascade of post-translational modifications on ribosomal nascent proteins. J. Biol. Chem. 285, 27525-27531 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 27525-27531
    • Walsh, C.T.1    Acker, M.G.2    Bowers, A.A.3
  • 45
    • 84925252380 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of thiazolyl peptide natural products featuring an enzyme-catalyzed forma [4+2] cycloaddition
    • Wever, W. J. et al. Chemoenzymatic synthesis of thiazolyl peptide natural products featuring an enzyme-catalyzed forma [4+2] cycloaddition. J. Am. Chem. Soc. 137, 3494-3497 (2015).
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 3494-3497
    • Wever, W.J.1
  • 47
    • 84863477081 scopus 로고    scopus 로고
    • Generation of thiocillin ring size variants by prepeptide gene replacement and in vivo processing by Bacillus cereus
    • Bowers, A. A., Acker, M. G., Young, T. S., Walsh, C. T. Generation of thiocillin ring size variants by prepeptide gene replacement and in vivo processing by Bacillus cereus. J. Am. Chem. Soc. 134, 10313-10316 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 10313-10316
    • Bowers, A.A.1    Acker, M.G.2    Young, T.S.3    Walsh, C.T.4
  • 48
    • 84925460979 scopus 로고    scopus 로고
    • Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB
    • Ortega, M. A. et al. Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB. Nature 517, 509-512 (2015).
    • (2015) Nature , vol.517 , pp. 509-512
    • Ortega, M.A.1
  • 49
    • 84965159401 scopus 로고    scopus 로고
    • Enzyme-dependent [4+2] cycloaddition depends on lid-like interaction of the N-terminal sequence with the catalytic core in PyrI4
    • Zheng, Q. et al. Enzyme-dependent [4+2] cycloaddition depends on lid-like interaction of the N-terminal sequence with the catalytic core in PyrI4. Cell Chem. Biol. 23, 352-360 (2016).
    • (2016) Cell Chem. Biol. , vol.23 , pp. 352-360
    • Zheng, Q.1
  • 50
    • 84901855811 scopus 로고    scopus 로고
    • Impact of scaffold rigidity on the design and evolution of an artificial Diels-Alderase
    • Preiswerk, N. et al. Impact of scaffold rigidity on the design and evolution of an artificial Diels-Alderase. Proc. Natl Acad. Sci. USA 111, 8013-8018 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 8013-8018
    • Preiswerk, N.1
  • 51
    • 20244375551 scopus 로고    scopus 로고
    • Structural basis for Diels-Alder ribozyme-catalyzed carbon-carbon bond formation
    • Serganov, A. et al. Structural basis for Diels-Alder ribozyme-catalyzed carbon-carbon bond formation. Nat. Struct. Mol. Biol. 12, 218-224 (2005).
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 218-224
    • Serganov, A.1
  • 52
    • 77954811495 scopus 로고    scopus 로고
    • Computational design of an enzyme catalyst for a stereoselective bimolecular Diels-Alder reaction
    • Siegel, J. B. et al. Computational design of an enzyme catalyst for a stereoselective bimolecular Diels-Alder reaction. Science 329, 309-313 (2010).
    • (2010) Science , vol.329 , pp. 309-313
    • Siegel, J.B.1


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