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Volumn 3, Issue 5, 2011, Pages 388-392

Regio- and stereodivergent antibiotic oxidative carbocyclizations catalysed by Rieske oxygenase-like enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; OXYGENASE;

EID: 79955082670     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.1024     Document Type: Article
Times cited : (102)

References (40)
  • 1
    • 0018630489 scopus 로고
    • Cell-free conversion of d-(l-α-aminoadiphyl)-L-cysteinyl-D-valine into an antibiotic with the properties of isopenicillin N in Cephalosporium acremonium
    • Konomi, T. et al. Cell-free conversion of d-(L-alpha-aminoadipyl)-L- cysteinyl-Dvaline into an antibiotic with the properties of isopenicillin N in Cephalosporium acremonium. Biochem. J. 184, 427-430 (1979). (Pubitemid 10182942)
    • (1979) Biochemical Journal , vol.184 , Issue.2 , pp. 427-430
    • Konomi, T.1    Herchen, S.2    Baldwin, J.E.3
  • 2
    • 0023622631 scopus 로고
    • Isolation of two novel intracellular b-lactams and a novel dioxygenase cyclizing enzyme from Streptomyces clavuligerus
    • Elson, S. W. et al. Isolation of two novel intracellular b-lactams and a novel dioxygenase cyclizing enzyme from Streptomyces clavuligerus. J. Chem. Soc., Chem. Commun. 1736-1738 (1987).
    • (1987) J. Chem. Soc., Chem. Commun. , pp. 1736-1738
    • Elson, S.W.1
  • 3
    • 0026050593 scopus 로고
    • Studies on the biosynthesis of fosfomycin. 2. Conversion of 2-hydroxypropyl-phosphonic acid to fosfomycin by blocked mutants of Streptomyces wedmorensis
    • Seto, H. et al. Studies on the biosynthesis of fosfomycin. 2. Conversion of 2-hydroxypropyl-phosphonic acid to fosfomycin by blocked mutants of Streptomyces wedmorensis. J. Antibiot. 44, 1286-1288 (1991).
    • (1991) J. Antibiot. , vol.44 , pp. 1286-1288
    • Seto, H.1
  • 4
    • 0008713567 scopus 로고
    • Biosynthesis of natural products with a P-C bond. Part 8: On the origin of the oxirane oxygen atom of fosfomycin in Streptomyces fradiae
    • Hammerschmidt, F. Biosynthesis of natural products with a P-C bond. Part 8: on the origin of the oxirane oxygen atom of fosfomycin in Streptomyces fradiae. J. Chem. Soc. Perkin Trans. 1 1993-1996 (1991).
    • (1991) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 1993-1996
    • Hammerschmidt, F.1
  • 5
    • 10944269741 scopus 로고    scopus 로고
    • An oxidative phenol coupling reaction catalyzed by OxyB, a cytochrome P450 from the vancomycin-producing microorganism
    • DOI 10.1002/anie.200461278
    • Zerbe, K. et al. An oxidative phenol coupling reaction catalyzed by OxyB, a cytochrome P450 from the vancomycin-producing microorganism. Angew. Chem. Int. Ed. 43, 6709-6713 (2004). (Pubitemid 40019007)
    • (2004) Angewandte Chemie - International Edition , vol.43 , Issue.48 , pp. 6709-6713
    • Zerbe, K.1    Woithe, K.2    Li, D.B.3    Vitali, F.4    Bigler, L.5    Robinson, J.A.6
  • 6
    • 0021367608 scopus 로고
    • A pure enzyme catalyzing penicillin biosynthesis
    • Hollander, I. J., Shen, Y.-Q., Heim, J., Demain, A. L. & Wolfe, S. A pure enzyme catalyzing penicillin biosynthesis. Science 224, 610-612 (1984). (Pubitemid 14137530)
    • (1984) Science , vol.224 , Issue.4649 , pp. 610-612
    • Hollander, I.J.1    Shen, Y.Q.2    Heim, J.3
  • 8
    • 0029038392 scopus 로고
    • Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
    • Roach, P. L. et al. Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes. Nature 375, 700-704 (1995).
    • (1995) Nature , vol.375 , pp. 700-704
    • Roach, P.L.1
  • 10
    • 27144467824 scopus 로고    scopus 로고
    • Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme
    • DOI 10.1038/nature03924, PII N03924
    • Higgins, L. J., Yan, F., Liu, P., Liu, H.-W. & Drennan, C. L. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature 437, 838-844 (2005). (Pubitemid 41486753)
    • (2005) Nature , vol.437 , Issue.7060 , pp. 838-844
    • Higgins, L.J.1    Yan, F.2    Liu, P.3    Liu, H.-W.4    Drennan, C.L.5
  • 12
    • 33748758449 scopus 로고    scopus 로고
    • Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC, and RebC on chromopyrrolic acid
    • DOI 10.1021/ja063898m
    • Howard-Jones A. R. & Walsh, C. T. Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC and RebC on chromopyrrolic acid. J. Am. Chem. Soc. 128, 12289-12298 (2006). (Pubitemid 44413860)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.37 , pp. 12289-12298
    • Howard-Jones, A.R.1    Walsh, C.T.2
  • 13
    • 56249097931 scopus 로고    scopus 로고
    • A concerted mechanism for berberine bridge enzyme
    • Winkler A. et al. A concerted mechanism for berberine bridge enzyme. Nature Chem. Biol. 4, 739-741 (2008).
    • (2008) Nature Chem. Biol. , vol.4 , pp. 739-741
    • Winkler, A.1
  • 16
    • 0038747011 scopus 로고    scopus 로고
    • The first direct characterization of a high-valent iron intermediate in the reaction of an α-ketoglutarate-dependent dioxygenase: A high-spin Fe(IV) complex in taurine/α-ketoglutarate dioxygenase (TauD) from Escherichia coli
    • DOI 10.1021/bi030011f
    • Price, J. C., Barr, E.W., Tirupati, B., Bollinger, J. M. Jr & Krebs, C. The first direct characterization of a high-valent iron intermediate in the reaction of an a-ketoglutarate-dependent dioxygenase: a high-spin FeIV complex in taurine/a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 42, 7497-7508 (2003). (Pubitemid 36740493)
    • (2003) Biochemistry , vol.42 , Issue.24 , pp. 7497-7508
    • Price, J.C.1    Barr, E.W.2    Tirupati, B.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 18
    • 0001617810 scopus 로고
    • Biosynthesis of prodigiosin. III. Carbon-13 Fourier transform NMR. X. Biosynthesis of metacycloprodigiosin and undecylprodigiosin
    • Wasserman, H. H., Shaw, C. K., Sykes, R. J. & Cushley, R. J. Biosynthesis of prodigiosin. III. Carbon-13 Fourier transform NMR. X. Biosynthesis of metacycloprodigiosin and undecylprodigiosin. Tetrahedron Lett. 2787-2790 (1974).
    • (1974) Tetrahedron Lett. , pp. 2787-2790
    • Wasserman, H.H.1    Shaw, C.K.2    Sykes, R.J.3    Cushley, R.J.4
  • 19
    • 0014691401 scopus 로고
    • Metacycloprodigiosin a tripyrrole pigment from Streptomyces longisporus ruber
    • Wasserman, H. H., Rodgers, G. C. & Keith, D. D. Metacycloprodigiosin, a tripyrrole pigment from Streptomyces longisporus ruber. J. Am. Chem. Soc. 91, 1263-1264 (1969).
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 1263-1264
    • Wasserman, H.H.1    Rodgers, G.C.2    Keith, D.D.3
  • 20
    • 33947416198 scopus 로고
    • Structure and synthesis of undecylprodigiosin. Prodigiosin analog from Streptomyces
    • Wasserman, H. H., Rodgers, G. C. & Keith, D. D. Structure and synthesis of undecylprodigiosin. Prodigiosin analog from Streptomyces. Chem. Commun. 825-826 (1966).
    • (1966) Chem. Commun. , pp. 825-826
    • Wasserman, H.H.1    Rodgers, G.C.2    Keith, D.D.3
  • 21
    • 0026031214 scopus 로고
    • Butyl-meta-cycloheptylprodiginine - A revision of the structure of the former ortho-isomer
    • Laatsch, H., Kellner, M. & Weyland, H. Butyl-meta- cycloheptylprodiginine - a revision of the structure of the former ortho-isomer. J. Antibiot. 44, 187-191 (1991).
    • (1991) J. Antibiot. , vol.44 , pp. 187-191
    • Laatsch, H.1    Kellner, M.2    Weyland, H.3
  • 22
    • 49049085250 scopus 로고    scopus 로고
    • A prodigiosin from the roseophilin producer Streptomyces griseoviridis
    • Kawasaki, T., Sakurai, F. & Hayakawa, Y. A prodigiosin from the roseophilin producer Streptomyces griseoviridis. J. Nat. Prod. 71, 1265-1267 (2008).
    • (2008) J. Nat. Prod. , vol.71 , pp. 1265-1267
    • Kawasaki, T.1    Sakurai, F.2    Hayakawa, Y.3
  • 24
    • 37649023004 scopus 로고    scopus 로고
    • Small molecule obatoclax (GX15-070) antagonizes MCL-1 and overcomes MCL-1-mediated resistance to apoptosis
    • Nguyen, M. et al. Small molecule obatoclax (GX15-070) antagonizes MCL-1 and overcomes MCL-1-mediated resistance to apoptosis. Proc. Natl Acad. Sci. USA 104, 19512-19517 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19512-19517
    • Nguyen, M.1
  • 25
    • 39149120828 scopus 로고    scopus 로고
    • Elucidation of the Streptomyces coelicolor pathway to 2-undecylpyrrole, a key intermediate in undecylprodiginine and streptorubin B biosynthesis
    • Mo, S. J. et al. Elucidation of the Streptomyces coelicolor pathway to 2-undecylpyrrole, a key intermediate in undecylprodiginine and streptorubin B biosynthesis. Chem. Biol. 15, 137-148 (2008).
    • (2008) Chem. Biol. , vol.15 , pp. 137-148
    • Mo, S.J.1
  • 26
    • 33749045718 scopus 로고    scopus 로고
    • Elucidation of the Streptomyces coelicolor pathway to 4-methoxy-2,2- bipyrrole-5-carboxaldehyde, an intermediate in prodiginine biosynthesis
    • DOI 10.1039/b609556a
    • Stanley, A. E., Walton, L. J., Kourdi-Zerikly, M., Corre, C. & Challis, G. L. Elucidation of the Streptomyces coelicolor pathway to 4-methoxy-2,2Œ-bipyrrole- 5-carboxaldehyde, an intermediate in prodiginine biosynthesis. Chem. Commun. 3981-3983 (2006). (Pubitemid 44465553)
    • (2006) Chemical Communications , Issue.38 , pp. 3981-3983
    • Stanley, A.E.1    Walton, L.J.2    Kourdi Zerikly, M.3    Corre, C.4    Challis, G.L.5
  • 27
    • 41849109815 scopus 로고    scopus 로고
    • Role and substrate specificity of the Streptomyces coelicolor RedH enzyme in undecylprodiginine biosynthesis
    • DOI 10.1039/b801677a
    • Haynes, S. W., Sydor, P. K., Stanley, A. E., Song, L. & Challis, G. L. Role and substrate specificity of the Streptomyces coelicolor RedH enzyme in undecylprodiginine biosynthesis. Chem. Commun. 1865-1867 (2008). (Pubitemid 351503470)
    • (2008) Chemical Communications , Issue.16 , pp. 1865-1867
    • Haynes, S.W.1    Sydor, P.K.2    Stanley, A.E.3    Song, L.4    Challis, G.L.5
  • 28
    • 0034872156 scopus 로고    scopus 로고
    • Analysis of the prodiginine biosynthesis gene cluster of Streptomyces coelicolor A3(2): New mechanisms for chain initiation and termination in modular multienzymes
    • DOI 10.1016/S1074-5521(01)00054-0, PII S1074552101000540
    • Cerdeno, A. M., Bibb M. J. & Challis, G. L. Analysis of the prodiginine biosynthesis gene cluster of Streptomyces coelicolor A3(2): new mechanisms for chain initiation and termination in modular multienzymes. Chem. Biol. 8, 817-829 (2001). (Pubitemid 32752460)
    • (2001) Chemistry and Biology , vol.8 , Issue.8 , pp. 817-829
    • Cerdeno, A.M.1    Bibb, M.J.2    Challis, G.L.3
  • 30
    • 0034029015 scopus 로고    scopus 로고
    • Aromatic hydrocarbon dioxygenases in environmental biotechnology
    • DOI 10.1016/S0958-1669(00)00090-2
    • Gibson, D. T. & Parales R. E. Aromatic hydrocarbon dioxygenases in environmental biotechnology. Curr. Opin. Biotechnol. 11, 236-243 (2000). (Pubitemid 30326469)
    • (2000) Current Opinion in Biotechnology , vol.11 , Issue.3 , pp. 236-243
    • Gibson, D.T.1    Parales, R.E.2
  • 31
    • 27744589609 scopus 로고    scopus 로고
    • And characterization of aminopyrrolnitrin oxygenase, a Rieske N-oxygenase that catalyzes unusual arylamine oxidation
    • Lee, J., Simurdiak, M. & Zhao, H. Reconstitution and characterization of aminopyrrolnitrin oxygenase, a Rieske N-oxygenase that catalyzes unusual arylamine oxidation. J. Biol. Chem. 280, 36719-36727 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 36719-36727
    • Lee, J.1    Simurdiak, M.2    Reconstitution, Z.H.3
  • 32
    • 27544477399 scopus 로고    scopus 로고
    • Rieske business: Structure-function of Rieske non-heme oxygenases
    • DOI 10.1016/j.bbrc.2005.08.222, PII S0006291X05019480
    • Ferraro D. J., Gakhar L. & Ramaswamy S. Rieske business: structure-function of Rieske non-heme oxygenases. Biochem. Biophys. Res. Commun. 338, 175-190 (2005). (Pubitemid 41540554)
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 175-190
    • Ferraro, D.J.1    Gakhar, L.2    Ramaswamy, S.3
  • 34
    • 79951521145 scopus 로고    scopus 로고
    • Enantioselective total synthesis and confirmation of the absolute and relative stereochemistry of streptorubin B
    • Hu, D. X., Clift, M. D., Lazarski, K. E. & Thomson R. J. Enantioselective total synthesis and confirmation of the absolute and relative stereochemistry of streptorubin B. J. Am. Chem. Soc. 133, 1799-1804 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 1799-1804
    • Hu, D.X.1    Clift, M.D.2    Lazarski, K.E.3    Thomson, R.J.4
  • 36
    • 67649998608 scopus 로고    scopus 로고
    • Prodigiosin biosynthesis gene cluster in the roseophilin producer Streptomyces griseoviridis
    • Kawasaki, T., Sakurai, F., Nagatsuka, S. & Hayakawa, Y. Prodigiosin biosynthesis gene cluster in the roseophilin producer Streptomyces griseoviridis. J. Antibiot. 62, 271-276 (2009).
    • (2009) J. Antibiot. , vol.62 , pp. 271-276
    • Kawasaki, T.1    Sakurai, F.2    Nagatsuka, S.3    Hayakawa, Y.4
  • 37
    • 43049091488 scopus 로고    scopus 로고
    • Non-heme iron-dependent dioxygenases: Unraveling catalytic mechanisms for complex enzymatic oxidations
    • Bugg, T. D. H. & Ramaswamy, S. Non-heme iron-dependent dioxygenases: unraveling catalytic mechanisms for complex enzymatic oxidations. Curr. Opin. Chem. Biol. 12, 134-140 (2008).
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 134-140
    • Bugg, T.D.H.1    Ramaswamy, S.2
  • 39
    • 40949096433 scopus 로고    scopus 로고
    • A predictably selective aliphatic C-H oxidation reaction for complex molecule synthesis
    • DOI 10.1126/science.1148597
    • Chen, M. S. & White, M. C. A predictably selective aliphatic C-H oxidation reaction for complex molecule synthesis. Science 318, 783-787 (2007). (Pubitemid 351411767)
    • (2007) Science , vol.318 , Issue.5851 , pp. 783-787
    • Chen, M.S.1    White, M.C.2
  • 40
    • 70349556477 scopus 로고    scopus 로고
    • Total synthesis and study of 6-deoxyerythronolide B by late-stage C-H oxidation
    • Stang, E. M. & White, M. C. Total synthesis and study of 6-deoxyerythronolide B by late-stage C-H oxidation. Nature Chem. 1, 547-551 (2009).
    • (2009) Nature Chem. , vol.1 , pp. 547-551
    • Stang, E.M.1    White, M.C.2


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