메뉴 건너뛰기




Volumn 16, Issue 4, 2009, Pages 351-364

Divergent Pathways in the Biosynthesis of Bisindole Natural Products

Author keywords

CHEMBIO

Indexed keywords

BIOLOGICAL FACTOR; CARBAZOLE DERIVATIVE; INDOLE DERIVATIVE; TRYPTOPHAN; VIOLACEIN;

EID: 64749111045     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2009.01.017     Document Type: Review
Times cited : (112)

References (71)
  • 2
    • 40949164743 scopus 로고    scopus 로고
    • Evolving biosynthetic tangos negotiate mechanistic landscapes
    • Austin M.B., O'Maille P.E., and Noel J.P. Evolving biosynthetic tangos negotiate mechanistic landscapes. Nat. Chem. Biol. 4 (2008) 217-222
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 217-222
    • Austin, M.B.1    O'Maille, P.E.2    Noel, J.P.3
  • 3
    • 0030944043 scopus 로고    scopus 로고
    • DNA cleavage by topoisomerase I in the presence of indolocarbazole derivatives of rebeccamycin
    • Bailly C., Riou J.F., Colson P., Houssier C., Rodrigues-Pereira E., and Prudhomme M. DNA cleavage by topoisomerase I in the presence of indolocarbazole derivatives of rebeccamycin. Biochemistry 36 (1997) 3917-3929
    • (1997) Biochemistry , vol.36 , pp. 3917-3929
    • Bailly, C.1    Riou, J.F.2    Colson, P.3    Houssier, C.4    Rodrigues-Pereira, E.5    Prudhomme, M.6
  • 4
    • 33845934004 scopus 로고    scopus 로고
    • In vitro biosynthesis of violacein from L-tryptophan by the enzymes VioA-E from Chromobacterium violaceum
    • Balibar C.J., and Walsh C.T. In vitro biosynthesis of violacein from L-tryptophan by the enzymes VioA-E from Chromobacterium violaceum. Biochemistry 45 (2006) 15444-15457
    • (2006) Biochemistry , vol.45 , pp. 15444-15457
    • Balibar, C.J.1    Walsh, C.T.2
  • 5
    • 34548069725 scopus 로고    scopus 로고
    • Terrequinone A biosynthesis through L-tryptophan oxidation, dimerization and bisprenylation
    • Balibar C.J., Howard-Jones A.R., and Walsh C.T. Terrequinone A biosynthesis through L-tryptophan oxidation, dimerization and bisprenylation. Nat. Chem. Biol. 3 (2007) 584-592
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 584-592
    • Balibar, C.J.1    Howard-Jones, A.R.2    Walsh, C.T.3
  • 8
    • 0003468279 scopus 로고
    • Matiere colorante se formant dans la colle de farine
    • Boisbaudran L.D. Matiere colorante se formant dans la colle de farine. C. R. Acad. Sci. 94 (1882) 562
    • (1882) C. R. Acad. Sci. , vol.94 , pp. 562
    • Boisbaudran, L.D.1
  • 11
    • 0035963668 scopus 로고    scopus 로고
    • Cloning and heterologous expression of a natural product biosynthetic gene cluster from eDNA
    • Brady S.F., Chao C.J., Handelsman J., and Clardy J. Cloning and heterologous expression of a natural product biosynthetic gene cluster from eDNA. Org. Lett. 3 (2001) 1981-1984
    • (2001) Org. Lett. , vol.3 , pp. 1981-1984
    • Brady, S.F.1    Chao, C.J.2    Handelsman, J.3    Clardy, J.4
  • 12
    • 0141758343 scopus 로고    scopus 로고
    • The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability
    • Brazilian National Genome Project Consortium
    • Brazilian National Genome Project Consortium. The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability. Proc. Natl. Acad. Sci. USA 100 (2003) 11660-11665
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11660-11665
  • 13
    • 0035089406 scopus 로고    scopus 로고
    • Granulatimide and 6-bromogranulatimide, minor alkaloids of the Brazilian ascidian Didemnum granulatum
    • Britton R., de Oliveira J.H.L., Andersen R.J., and Berlinck R.G. Granulatimide and 6-bromogranulatimide, minor alkaloids of the Brazilian ascidian Didemnum granulatum. J. Nat. Prod. 64 (2001) 254-255
    • (2001) J. Nat. Prod. , vol.64 , pp. 254-255
    • Britton, R.1    de Oliveira, J.H.L.2    Andersen, R.J.3    Berlinck, R.G.4
  • 14
  • 15
    • 0029586252 scopus 로고
    • Structure of cytochrome P450eryF involved in erythromycin biosynthesis
    • Cupp-Vickery J.R., and Poulos T.L. Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat. Struct. Biol. 2 (1995) 144-153
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 144-153
    • Cupp-Vickery, J.R.1    Poulos, T.L.2
  • 16
    • 64749115201 scopus 로고    scopus 로고
    • Secondary metabolism: the building blocks and construction mechanisms
    • John Wiley & Sons, Chichester
    • Dewick P.M. Secondary metabolism: the building blocks and construction mechanisms. Medicinal Natural Products: A Biosynthetic Approach (2001), John Wiley & Sons, Chichester 7-34
    • (2001) Medicinal Natural Products: A Biosynthetic Approach , pp. 7-34
    • Dewick, P.M.1
  • 18
    • 25844517049 scopus 로고    scopus 로고
    • Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination
    • Dong C., Flecks S., Unversucht S., Haupt C., van Pée K.H., and Naismith J.H. Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination. Science 309 (2005) 2216-2219
    • (2005) Science , vol.309 , pp. 2216-2219
    • Dong, C.1    Flecks, S.2    Unversucht, S.3    Haupt, C.4    van Pée, K.H.5    Naismith, J.H.6
  • 19
    • 0034805976 scopus 로고    scopus 로고
    • Chromobacterium violaceum: a review of pharmacological and industrial perspectives
    • Durán N., and Menck C.F. Chromobacterium violaceum: a review of pharmacological and industrial perspectives. Crit. Rev. Microbiol. 27 (2001) 201-222
    • (2001) Crit. Rev. Microbiol. , vol.27 , pp. 201-222
    • Durán, N.1    Menck, C.F.2
  • 21
    • 0031005987 scopus 로고    scopus 로고
    • Semicochliodinol A and B: inhibitors of HIV-1 protease and EGF-R protein tyrosine kinase related to asterriquinones produced by the fungus Chrysosporium merdarium
    • Fredenhagen A., Petersen F., Tintelnot-Blomley M., Rösel J., Mett H., and Hug P. Semicochliodinol A and B: inhibitors of HIV-1 protease and EGF-R protein tyrosine kinase related to asterriquinones produced by the fungus Chrysosporium merdarium. J. Antibiot. (Tokyo) 50 (1997) 395-401
    • (1997) J. Antibiot. (Tokyo) , vol.50 , pp. 395-401
    • Fredenhagen, A.1    Petersen, F.2    Tintelnot-Blomley, M.3    Rösel, J.4    Mett, H.5    Hug, P.6
  • 22
    • 33746218306 scopus 로고    scopus 로고
    • Deciphering indolocarbazole and enediyne aminodideoxypentose biosynthesis through comparative genomics: insights from the AT2433 biosynthetic locus
    • Gao Q., Zhang C., Blanchard S., and Thorson J.S. Deciphering indolocarbazole and enediyne aminodideoxypentose biosynthesis through comparative genomics: insights from the AT2433 biosynthetic locus. Chem. Biol. 13 (2006) 733-743
    • (2006) Chem. Biol. , vol.13 , pp. 733-743
    • Gao, Q.1    Zhang, C.2    Blanchard, S.3    Thorson, J.S.4
  • 24
    • 34547095509 scopus 로고    scopus 로고
    • Simple indole alkaloids and those with a nonrearranged monoterpenoid unit
    • Higuchi K., and Kawasaki T. Simple indole alkaloids and those with a nonrearranged monoterpenoid unit. Nat. Prod. Rep. 24 (2007) 843-868
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 843-868
    • Higuchi, K.1    Kawasaki, T.2
  • 25
    • 44449099801 scopus 로고    scopus 로고
    • Crystal structure of VioE, a key player in the construction of the molecular skeleton of violacein
    • Hirano S., Asamizu S., Onaka H., Shiro Y., and Nagano S. Crystal structure of VioE, a key player in the construction of the molecular skeleton of violacein. J. Biol. Chem. 283 (2008) 6459-6466
    • (2008) J. Biol. Chem. , vol.283 , pp. 6459-6466
    • Hirano, S.1    Asamizu, S.2    Onaka, H.3    Shiro, Y.4    Nagano, S.5
  • 26
    • 0035039381 scopus 로고    scopus 로고
    • DNA binding properties of the marine sponge pigment fascaplysin
    • Hörmann A., Chaudhuri B., and Fretz H. DNA binding properties of the marine sponge pigment fascaplysin. Bioorg. Med. Chem. 9 (2001) 917-921
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 917-921
    • Hörmann, A.1    Chaudhuri, B.2    Fretz, H.3
  • 27
    • 28544449005 scopus 로고    scopus 로고
    • Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD
    • Howard-Jones A.R., and Walsh C.T. Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD. Biochemistry 44 (2005) 15652-15663
    • (2005) Biochemistry , vol.44 , pp. 15652-15663
    • Howard-Jones, A.R.1    Walsh, C.T.2
  • 28
    • 33748758449 scopus 로고    scopus 로고
    • Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC, and RebC on chromopyrrolic acid
    • Howard-Jones A.R., and 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 (2006) 12289-12298
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12289-12298
    • Howard-Jones, A.R.1    Walsh, C.T.2
  • 29
    • 34548803584 scopus 로고    scopus 로고
    • Nonenzymatic oxidative steps accompanying action of the cytochrome P450 enzymes StaP and RebP in the biosynthesis of staurosporine and rebeccamycin
    • Howard-Jones A.R., and Walsh C.T. Nonenzymatic oxidative steps accompanying action of the cytochrome P450 enzymes StaP and RebP in the biosynthesis of staurosporine and rebeccamycin. J. Am. Chem. Soc. 129 (2007) 11016-11017
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11016-11017
    • Howard-Jones, A.R.1    Walsh, C.T.2
  • 30
    • 0037415016 scopus 로고    scopus 로고
    • The biosynthesis of indolocarbazoles in a heterologous E. coli host
    • Hyun C.G., Bililign T., Liao J., and Thorson J.S. The biosynthesis of indolocarbazoles in a heterologous E. coli host. ChemBioChem 4 (2003) 114-117
    • (2003) ChemBioChem , vol.4 , pp. 114-117
    • Hyun, C.G.1    Bililign, T.2    Liao, J.3    Thorson, J.S.4
  • 31
    • 0022500301 scopus 로고
    • K-252a, a potent inhibitor of protein kinase C from microbial origin
    • Kase H., Iwahashi K., and Matsuda Y. K-252a, a potent inhibitor of protein kinase C from microbial origin. J. Antibiot. (Tokyo) 39 (1986) 1059-1065
    • (1986) J. Antibiot. (Tokyo) , vol.39 , pp. 1059-1065
    • Kase, H.1    Iwahashi, K.2    Matsuda, Y.3
  • 32
    • 34250675327 scopus 로고    scopus 로고
    • Genetic organization of the biosynthetic gene cluster for the indolocarbazole K-252a in Nonomuraea longicatena JCM 11136
    • Kim S.Y., Park J.S., Chae C.S., Hyun C.G., Choi B.W., Shin J., and Oh K.B. Genetic organization of the biosynthetic gene cluster for the indolocarbazole K-252a in Nonomuraea longicatena JCM 11136. Appl. Microbiol. Biotechnol. 75 (2007) 1119-1126
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 1119-1126
    • Kim, S.Y.1    Park, J.S.2    Chae, C.S.3    Hyun, C.G.4    Choi, B.W.5    Shin, J.6    Oh, K.B.7
  • 33
    • 0342646973 scopus 로고    scopus 로고
    • A new bioactive sesterterpene and antiplasmodial alkaloids from the marine sponge Hyrtios cf. erecta
    • Kirsch G., Köng G.M., Wright A.D., and Kaminsky R. A new bioactive sesterterpene and antiplasmodial alkaloids from the marine sponge Hyrtios cf. erecta. J. Nat. Prod. 63 (2000) 825-829
    • (2000) J. Nat. Prod. , vol.63 , pp. 825-829
    • Kirsch, G.1    Köng, G.M.2    Wright, A.D.3    Kaminsky, R.4
  • 34
    • 0034178126 scopus 로고    scopus 로고
    • Diketopiperazine alkaloids from the fungus Penicillium piscarium Westling
    • Kozlovskiǐ A.G., Vinokurova N.G., and Adanin V.M. Diketopiperazine alkaloids from the fungus Penicillium piscarium Westling. Prikl. Biokhim. Mikrobiol. 36 (2000) 317-321
    • (2000) Prikl. Biokhim. Mikrobiol. , vol.36 , pp. 317-321
    • Kozlovskiǐ, A.G.1    Vinokurova, N.G.2    Adanin, V.M.3
  • 35
    • 0036914164 scopus 로고    scopus 로고
    • The albonoursin gene cluster of S. noursei biosynthesis of diketopiperazine metabolites independent of nonribosomal peptide synthetases
    • Lautru S., Gondry M., Genet R., and Pernodet J.L. The albonoursin gene cluster of S. noursei biosynthesis of diketopiperazine metabolites independent of nonribosomal peptide synthetases. Chem. Biol. 9 (2002) 1355-1364
    • (2002) Chem. Biol. , vol.9 , pp. 1355-1364
    • Lautru, S.1    Gondry, M.2    Genet, R.3    Pernodet, J.L.4
  • 36
    • 34547424283 scopus 로고    scopus 로고
    • Crystal structures and catalytic mechanism of cytochrome P450 StaP that produces the indolocarbazole skeleton
    • Makino M., Sugimoto H., Shiro Y., Asamizu S., Onaka H., and Nagano S. Crystal structures and catalytic mechanism of cytochrome P450 StaP that produces the indolocarbazole skeleton. Proc. Natl. Acad. Sci. USA 104 (2007) 11591-11596
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11591-11596
    • Makino, M.1    Sugimoto, H.2    Shiro, Y.3    Asamizu, S.4    Onaka, H.5    Nagano, S.6
  • 37
    • 0024333037 scopus 로고
    • AT2433-A1, AT2433-A2, AT2433-B1, and AT2433-B2 novel antitumor antibiotic compounds produced by Actinomadura melliaura. Taxonomy, fermentation, isolation and biological properties
    • Matson J.A., Claridge C., Bush J.A., Titus J., Bradner W.T., Doyle T.W., Horan A.C., and Patel M. AT2433-A1, AT2433-A2, AT2433-B1, and AT2433-B2 novel antitumor antibiotic compounds produced by Actinomadura melliaura. Taxonomy, fermentation, isolation and biological properties. J. Antibiot. (Tokyo) 42 (1989) 1547-1555
    • (1989) J. Antibiot. (Tokyo) , vol.42 , pp. 1547-1555
    • Matson, J.A.1    Claridge, C.2    Bush, J.A.3    Titus, J.4    Bradner, W.T.5    Doyle, T.W.6    Horan, A.C.7    Patel, M.8
  • 38
    • 0036247452 scopus 로고    scopus 로고
    • Indocarbazostatin and indocarbazostatin B, novel inhibitors of NGF-induced neuronal differentiation in PC12 Cells. I. Screening, taxonomy, fermentation and biological activities
    • Matsuura N., Tamehiro N., Andoh T., Kawashima A., and Ubukata M. Indocarbazostatin and indocarbazostatin B, novel inhibitors of NGF-induced neuronal differentiation in PC12 Cells. I. Screening, taxonomy, fermentation and biological activities. J. Antibiot. (Tokyo) 55 (2002) 355-362
    • (2002) J. Antibiot. (Tokyo) , vol.55 , pp. 355-362
    • Matsuura, N.1    Tamehiro, N.2    Andoh, T.3    Kawashima, A.4    Ubukata, M.5
  • 40
    • 0031467411 scopus 로고    scopus 로고
    • Quorum sensing and Chromobacterium violaceum: exploitation of violacein production and inhibition for the detection of N-acylhomoserine lactones
    • McClean K.H., Winson M.K., Fish L., Taylor A., Chhabra S.R., Camara M., Daykin M., Lamb J.H., Swift S., Bycroft B.W., et al. Quorum sensing and Chromobacterium violaceum: exploitation of violacein production and inhibition for the detection of N-acylhomoserine lactones. Microbiology 143 (1997) 3703-3711
    • (1997) Microbiology , vol.143 , pp. 3703-3711
    • McClean, K.H.1    Winson, M.K.2    Fish, L.3    Taylor, A.4    Chhabra, S.R.5    Camara, M.6    Daykin, M.7    Lamb, J.H.8    Swift, S.9    Bycroft, B.W.10
  • 42
    • 0021816422 scopus 로고
    • Isolation and structure of rebeccamycin-a new antitumor antibiotic from Nocardia Aerocoligenes
    • Nettleton D., Doyle T., Krishnan B., Matsumoto T., and Clardy J. Isolation and structure of rebeccamycin-a new antitumor antibiotic from Nocardia Aerocoligenes. Tetrahedron Lett. 26 (1985) 4011-4014
    • (1985) Tetrahedron Lett. , vol.26 , pp. 4011-4014
    • Nettleton, D.1    Doyle, T.2    Krishnan, B.3    Matsumoto, T.4    Clardy, J.5
  • 43
    • 14644432391 scopus 로고    scopus 로고
    • Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243
    • Nishizawa T., Aldrich C.C., and Sherman D.H. Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243. J. Bacteriol. 187 (2005) 2084-2092
    • (2005) J. Bacteriol. , vol.187 , pp. 2084-2092
    • Nishizawa, T.1    Aldrich, C.C.2    Sherman, D.H.3
  • 45
    • 33746520558 scopus 로고    scopus 로고
    • Chemistry and biology of monoterpene indole alkaloid biosynthesis
    • O'Connor S.E., and Maresh J.J. Chemistry and biology of monoterpene indole alkaloid biosynthesis. Nat. Prod. Rep. 23 (2006) 532-547
    • (2006) Nat. Prod. Rep. , vol.23 , pp. 532-547
    • O'Connor, S.E.1    Maresh, J.J.2
  • 47
    • 0036952785 scopus 로고    scopus 로고
    • Cloning of the staurosporine biosynthetic gene cluster from Streptomyces sp. TP-A0274 and its heterologous expression in Streptomyces lividans
    • Onaka H., Taniguchi S., Igarashi Y., and Furumai T. Cloning of the staurosporine biosynthetic gene cluster from Streptomyces sp. TP-A0274 and its heterologous expression in Streptomyces lividans. J. Antibiot. (Tokyo) 55 (2002) 1063-1071
    • (2002) J. Antibiot. (Tokyo) , vol.55 , pp. 1063-1071
    • Onaka, H.1    Taniguchi, S.2    Igarashi, Y.3    Furumai, T.4
  • 48
    • 0028052780 scopus 로고
    • Pathway engineering in secondary metabolite-producing actinomycetes
    • Piepersberg W. Pathway engineering in secondary metabolite-producing actinomycetes. Crit. Rev. Biotechnol. 14 (1994) 251-285
    • (1994) Crit. Rev. Biotechnol. , vol.14 , pp. 251-285
    • Piepersberg, W.1
  • 50
    • 6444232494 scopus 로고    scopus 로고
    • Biological targets of antitumor indolocarbazoles bearing a sugar moiety
    • Prudhomme M. Biological targets of antitumor indolocarbazoles bearing a sugar moiety. Curr. Med. Chem. Anticancer Agents 4 (2004) 509-521
    • (2004) Curr. Med. Chem. Anticancer Agents , vol.4 , pp. 509-521
    • Prudhomme, M.1
  • 51
    • 0024394417 scopus 로고
    • Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases
    • Rüegg U.T., and Burgess G.M. Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases. Trends Pharmacol. Sci. 10 (1989) 218-220
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 218-220
    • Rüegg, U.T.1    Burgess, G.M.2
  • 53
    • 44449103827 scopus 로고    scopus 로고
    • The violacein biosynthetic enzyme VioE shares a fold with lipoprotein transporter proteins
    • Ryan K.S., Balibar C.J., Turo K.E., Walsh C.T., and Drennan C.L. The violacein biosynthetic enzyme VioE shares a fold with lipoprotein transporter proteins. J. Biol. Chem. 283 (2008) 6467-6475
    • (2008) J. Biol. Chem. , vol.283 , pp. 6467-6475
    • Ryan, K.S.1    Balibar, C.J.2    Turo, K.E.3    Walsh, C.T.4    Drennan, C.L.5
  • 54
    • 0025875228 scopus 로고
    • Nortopsentins A, B, and C. Cytotoxic and antifungal imidazolediylbis[indoles] from the sponge Spongosorites ruetzleri
    • Sakemi S., and Sun H.H. Nortopsentins A, B, and C. Cytotoxic and antifungal imidazolediylbis[indoles] from the sponge Spongosorites ruetzleri. J. Org. Chem. 56 (1991) 4304-4307
    • (1991) J. Org. Chem. , vol.56 , pp. 4304-4307
    • Sakemi, S.1    Sun, H.H.2
  • 55
    • 26244438853 scopus 로고    scopus 로고
    • Deciphering the late steps in the biosynthesis of the anti-tumour indolocarbazole staurosporine: sugar donor substrate flexibility of the StaG glycosyltransferase
    • Salas A.P., Zhu L., Sánchez C., Braña A.F., Rohr J., Méndez C., and Salas J.A. Deciphering the late steps in the biosynthesis of the anti-tumour indolocarbazole staurosporine: sugar donor substrate flexibility of the StaG glycosyltransferase. Mol. Microbiol. 58 (2005) 17-27
    • (2005) Mol. Microbiol. , vol.58 , pp. 17-27
    • Salas, A.P.1    Zhu, L.2    Sánchez, C.3    Braña, A.F.4    Rohr, J.5    Méndez, C.6    Salas, J.A.7
  • 57
    • 33747160432 scopus 로고    scopus 로고
    • Reevaluation of the violacein biosynthetic pathway and its relationship to indolocarbazole biosynthesis
    • Sánchez C., Braña A.F., Méndez C., and Salas J.A. Reevaluation of the violacein biosynthetic pathway and its relationship to indolocarbazole biosynthesis. ChemBioChem 7 (2006) 1231-1240
    • (2006) ChemBioChem , vol.7 , pp. 1231-1240
    • Sánchez, C.1    Braña, A.F.2    Méndez, C.3    Salas, J.A.4
  • 58
    • 33751335837 scopus 로고    scopus 로고
    • Indolocarbazole natural products: occurrence, biosynthesis, and biological activity
    • Sánchez C., Méndez C., and Salas J.A. Indolocarbazole natural products: occurrence, biosynthesis, and biological activity. Nat. Prod. Rep. 23 (2006) 1007-1045
    • (2006) Nat. Prod. Rep. , vol.23 , pp. 1007-1045
    • Sánchez, C.1    Méndez, C.2    Salas, J.A.3
  • 59
    • 0033534343 scopus 로고    scopus 로고
    • Iheyamines, new cytotoxic bisindole pigments from a colonial ascidian, Polycitorella sp
    • Sasaki T., Ohtani I.I., Tanaka J., and Higa T. Iheyamines, new cytotoxic bisindole pigments from a colonial ascidian, Polycitorella sp. Tetrahedron Lett. 40 (1999) 303-306
    • (1999) Tetrahedron Lett. , vol.40 , pp. 303-306
    • Sasaki, T.1    Ohtani, I.I.2    Tanaka, J.3    Higa, T.4
  • 60
    • 0032560721 scopus 로고    scopus 로고
    • Rhopaladins A-D, new indole alkaloids from marine tunicate Rhopalaea sp
    • Sato H., Tsuda M., Watanabe K., and Kobayashi J. Rhopaladins A-D, new indole alkaloids from marine tunicate Rhopalaea sp. Tetrahedron 54 (1998) 8687-8690
    • (1998) Tetrahedron , vol.54 , pp. 8687-8690
    • Sato, H.1    Tsuda, M.2    Watanabe, K.3    Kobayashi, J.4
  • 61
    • 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., and Hoffmeister D. A one-pot chemoenzymatic synthesis for the universal precursor of antidiabetes and antiviral bis-indolylquinones. Chem. Biol. 14 (2007) 635-644
    • (2007) Chem. Biol. , vol.14 , pp. 635-644
    • Schneider, P.1    Weber, M.2    Rosenberger, K.3    Hoffmeister, D.4
  • 62
    • 38849108030 scopus 로고    scopus 로고
    • The Aspergillus nidulans enzyme TdiB catalyzes prenyltransfer to the precursor of bioactive asterriquinones
    • Schneider P., Weber M., and Hoffmeister D. The Aspergillus nidulans enzyme TdiB catalyzes prenyltransfer to the precursor of bioactive asterriquinones. Fungal Genet. Biol. 45 (2008) 302-309
    • (2008) Fungal Genet. Biol. , vol.45 , pp. 302-309
    • Schneider, P.1    Weber, M.2    Hoffmeister, D.3
  • 64
    • 0001401541 scopus 로고
    • Slime moulds (Myxomycetes) as a source of new biologically active metabolites
    • Steglich W. Slime moulds (Myxomycetes) as a source of new biologically active metabolites. Pure Appl. Chem. 61 (1989) 281-288
    • (1989) Pure Appl. Chem. , vol.61 , pp. 281-288
    • Steglich, W.1
  • 65
    • 0005088460 scopus 로고
    • Isolation of violacein
    • Strong F.M. Isolation of violacein. Science 100 (1944) 287
    • (1944) Science , vol.100 , pp. 287
    • Strong, F.M.1
  • 67
    • 15244349569 scopus 로고    scopus 로고
    • Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis
    • Yeh E., Garneau S., and Walsh C.T. Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis. Proc. Natl. Acad. Sci. USA 102 (2005) 3960-3965
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3960-3965
    • Yeh, E.1    Garneau, S.2    Walsh, C.T.3
  • 68
    • 33745963527 scopus 로고    scopus 로고
    • Flavin redox chemistry precedes substrate chlorination during the reaction of the flavin-dependent halogenase RebH
    • Yeh E., Cole L.J., Barr E.W., Bollinger Jr. J.M., Ballou D.P., and Walsh C.T. Flavin redox chemistry precedes substrate chlorination during the reaction of the flavin-dependent halogenase RebH. Biochemistry 45 (2006) 7904-7912
    • (2006) Biochemistry , vol.45 , pp. 7904-7912
    • Yeh, E.1    Cole, L.J.2    Barr, E.W.3    Bollinger Jr., J.M.4    Ballou, D.P.5    Walsh, C.T.6
  • 69
    • 33846842522 scopus 로고    scopus 로고
    • Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases
    • Yeh E., Blasiak L.C., Koglin A., Drennan C.L., and Walsh C.T. Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases. Biochemistry 46 (2007) 1284-1292
    • (2007) Biochemistry , vol.46 , pp. 1284-1292
    • Yeh, E.1    Blasiak, L.C.2    Koglin, A.3    Drennan, C.L.4    Walsh, C.T.5
  • 71
    • 40549122653 scopus 로고    scopus 로고
    • The tryptophan aminotransferase Tam1 catalyses the single biosynthetic step for tryptophan-dependent pigment synthesis in Ustilago maydis
    • Zuther K., Mayser P., Hettwer U., Wu W., Spiteller P., Kindler B.L.J., Karlovsky P., Basse C.W., and Schirawski J. The tryptophan aminotransferase Tam1 catalyses the single biosynthetic step for tryptophan-dependent pigment synthesis in Ustilago maydis. Mol. Microbiol. 68 (2008) 152-172
    • (2008) Mol. Microbiol. , vol.68 , pp. 152-172
    • Zuther, K.1    Mayser, P.2    Hettwer, U.3    Wu, W.4    Spiteller, P.5    Kindler, B.L.J.6    Karlovsky, P.7    Basse, C.W.8    Schirawski, J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.