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Volumn 15, Issue 10, 2008, Pages 1046-1057

Characterization of the Alnumycin Gene Cluster Reveals Unusual Gene Products for Pyran Ring Formation and Dioxan Biosynthesis

Author keywords

CHEMBIO

Indexed keywords

1,4-DIOXANE; ALNUMYCIN; DIOXANE; DIOXANE DERIVATIVE; MACROLIDE; NAPHTHOQUINONE; PYRAN DERIVATIVE;

EID: 53649108989     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2008.07.022     Document Type: Article
Times cited : (52)

References (59)
  • 2
    • 0028351394 scopus 로고
    • Cloning, sequencing and deduced functions of a cluster of Streptomyces genes probably encoding biosynthesis of the polyketide antibiotic frenolicin
    • Bibb M.J., Sherman D.H., Omura S., and Hopwood D.A. Cloning, sequencing and deduced functions of a cluster of Streptomyces genes probably encoding biosynthesis of the polyketide antibiotic frenolicin. Gene 142 (1994) 31-39
    • (1994) Gene , vol.142 , pp. 31-39
    • Bibb, M.J.1    Sherman, D.H.2    Omura, S.3    Hopwood, D.A.4
  • 3
    • 0031948321 scopus 로고    scopus 로고
    • Alnumycin a new naphthoquinone antibiotic produced by an endophytic Streptomyces sp
    • Bieber B., Nuske J., Ritzau M., and Grafe U. Alnumycin a new naphthoquinone antibiotic produced by an endophytic Streptomyces sp. J. Antibiot. (Tokyo) 51 (1998) 381-382
    • (1998) J. Antibiot. (Tokyo) , vol.51 , pp. 381-382
    • Bieber, B.1    Nuske, J.2    Ritzau, M.3    Grafe, U.4
  • 4
    • 29244446754 scopus 로고    scopus 로고
    • Structure, activity, synthesis and biosynthesis of aryl-C-glycosides
    • Bililign T., Griffith B.R., and Thorson J.S. Structure, activity, synthesis and biosynthesis of aryl-C-glycosides. Nat. Prod. Rep. 22 (2005) 742-760
    • (2005) Nat. Prod. Rep. , vol.22 , pp. 742-760
    • Bililign, T.1    Griffith, B.R.2    Thorson, J.S.3
  • 5
    • 53649101402 scopus 로고    scopus 로고
    • Björn, B., and Jörg, N. April 1998. Alnumycin useful as antibiotic. German patent DE19745914.
    • Björn, B., and Jörg, N. April 1998. Alnumycin useful as antibiotic. German patent DE19745914.
  • 6
    • 0033152235 scopus 로고    scopus 로고
    • Pyranonaphthoquinone antibiotics-isolation, structure and biological activity
    • Brimble M.A., Duncalf L.J., and Nairn M.R. Pyranonaphthoquinone antibiotics-isolation, structure and biological activity. Nat. Prod. Rep. 16 (1999) 267-281
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 267-281
    • Brimble, M.A.1    Duncalf, L.J.2    Nairn, M.R.3
  • 7
    • 0025837029 scopus 로고
    • Organisation and functions of the actVA region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor
    • Caballero J.L., Martinez E., Malpartida F., and Hopwood D.A. Organisation and functions of the actVA region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor. Mol. Gen. Genet. 230 (1991) 401-412
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 401-412
    • Caballero, J.L.1    Martinez, E.2    Malpartida, F.3    Hopwood, D.A.4
  • 8
    • 0018840878 scopus 로고
    • Streptomyces albus G mutants defective in the SalGI restriction-modification system
    • Chater K.F., and Wilde L.C. Streptomyces albus G mutants defective in the SalGI restriction-modification system. J. Gen. Microbiol. 116 (1980) 323-334
    • (1980) J. Gen. Microbiol. , vol.116 , pp. 323-334
    • Chater, K.F.1    Wilde, L.C.2
  • 9
    • 0030972114 scopus 로고    scopus 로고
    • Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2)
    • Crump M.P., Crosby J., Dempsey C.E., Parkinson J.A., Murray M., Hopwood D.A., and Simpson T.J. Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2). Biochemistry 36 (1997) 6000-6008
    • (1997) Biochemistry , vol.36 , pp. 6000-6008
    • Crump, M.P.1    Crosby, J.2    Dempsey, C.E.3    Parkinson, J.A.4    Murray, M.5    Hopwood, D.A.6    Simpson, T.J.7
  • 10
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko K.A., and Wanner B.L. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 6640-6645
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 11
    • 0025899144 scopus 로고
    • The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of Streptomyces
    • Fernandez-Moreno M.A., Caballero J.L., Hopwood D.A., and Malpartida F. The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of Streptomyces. Cell 66 (1991) 769-780
    • (1991) Cell , vol.66 , pp. 769-780
    • Fernandez-Moreno, M.A.1    Caballero, J.L.2    Hopwood, D.A.3    Malpartida, F.4
  • 12
    • 0026657813 scopus 로고
    • Nucleotide sequence and deduced functions of a set of cotranscribed genes of Streptomyces coelicolor A3(2) including the polyketide synthase for the antibiotic actinorhodin
    • Fernandez-Moreno M.A., Martinez E., Boto L., Hopwood D.A., and Malpartida F. Nucleotide sequence and deduced functions of a set of cotranscribed genes of Streptomyces coelicolor A3(2) including the polyketide synthase for the antibiotic actinorhodin. J. Biol. Chem. 267 (1992) 19278-19290
    • (1992) J. Biol. Chem. , vol.267 , pp. 19278-19290
    • Fernandez-Moreno, M.A.1    Martinez, E.2    Boto, L.3    Hopwood, D.A.4    Malpartida, F.5
  • 13
    • 0027971383 scopus 로고
    • DNA sequence and functions of the actVI region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor A3(2)
    • Fernandez-Moreno M.A., Martinez E., Caballero J.L., Ichinose K., Hopwood D.A., and Malpartida F. DNA sequence and functions of the actVI region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor A3(2). J. Biol. Chem. 269 (1994) 24854-24863
    • (1994) J. Biol. Chem. , vol.269 , pp. 24854-24863
    • Fernandez-Moreno, M.A.1    Martinez, E.2    Caballero, J.L.3    Ichinose, K.4    Hopwood, D.A.5    Malpartida, F.6
  • 14
    • 0343293841 scopus 로고    scopus 로고
    • Comparative study of the relaxation behaviour of acrylic polymers with flexible cyclic groups in their structure
    • García N., Compañ V., Díaz-Calleja R., Guzmán J., and Riande E. Comparative study of the relaxation behaviour of acrylic polymers with flexible cyclic groups in their structure. Polymer 41 (2000) 6603-6611
    • (2000) Polymer , vol.41 , pp. 6603-6611
    • García, N.1    Compañ, V.2    Díaz-Calleja, R.3    Guzmán, J.4    Riande, E.5
  • 15
    • 33745143939 scopus 로고    scopus 로고
    • Isolation, characterization, and heterologous expression of the biosynthesis gene cluster for the antitumor anthracycline steffimycin
    • Gullon S., Olano C., Abdelfattah M.S., Brana A.F., Rohr J., Mendez C., and Salas J.A. Isolation, characterization, and heterologous expression of the biosynthesis gene cluster for the antitumor anthracycline steffimycin. Appl. Environ. Microbiol. 72 (2006) 4172-4183
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 4172-4183
    • Gullon, S.1    Olano, C.2    Abdelfattah, M.S.3    Brana, A.F.4    Rohr, J.5    Mendez, C.6    Salas, J.A.7
  • 16
    • 4644370904 scopus 로고    scopus 로고
    • The crystal structure of the actIII actinorhodin polyketide reductase: proposed mechanism for ACP and polyketide binding
    • Hadfield A.T., Limpkin C., Teartasin W., Simpson T.J., Crosby J., and Crump M.P. The crystal structure of the actIII actinorhodin polyketide reductase: proposed mechanism for ACP and polyketide binding. Structure 12 (2004) 1865-1875
    • (2004) Structure , vol.12 , pp. 1865-1875
    • Hadfield, A.T.1    Limpkin, C.2    Teartasin, W.3    Simpson, T.J.4    Crosby, J.5    Crump, M.P.6
  • 17
    • 0024274121 scopus 로고
    • Nucleotide sequence, transcription and deduced function of a gene involved in polyketide antibiotic synthesis in Streptomyces coelicolor
    • Hallam S.E., Malpartida F., and Hopwood D.A. Nucleotide sequence, transcription and deduced function of a gene involved in polyketide antibiotic synthesis in Streptomyces coelicolor. Gene 74 (1988) 305-320
    • (1988) Gene , vol.74 , pp. 305-320
    • Hallam, S.E.1    Malpartida, F.2    Hopwood, D.A.3
  • 18
    • 33846923183 scopus 로고    scopus 로고
    • Type II polyketide synthases: gaining a deeper insight into enzymatic teamwork
    • Hertweck C., Luzhetskyy A., Rebets Y., and Bechthold A. Type II polyketide synthases: gaining a deeper insight into enzymatic teamwork. Nat. Prod. Rep. 24 (2007) 162-190
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 162-190
    • Hertweck, C.1    Luzhetskyy, A.2    Rebets, Y.3    Bechthold, A.4
  • 19
    • 0032575051 scopus 로고    scopus 로고
    • A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants
    • Hoang T.T., Karkhoff-Schweizer R.R., Kutchma A.J., and Schweizer H.P. A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants. Gene 212 (1998) 77-86
    • (1998) Gene , vol.212 , pp. 77-86
    • Hoang, T.T.1    Karkhoff-Schweizer, R.R.2    Kutchma, A.J.3    Schweizer, H.P.4
  • 21
    • 0001747786 scopus 로고    scopus 로고
    • Genetic contributions to understanding polyketide synthases
    • Hopwood D.A. Genetic contributions to understanding polyketide synthases. Chem. Rev. 97 (1997) 2465-2497
    • (1997) Chem. Rev. , vol.97 , pp. 2465-2497
    • Hopwood, D.A.1
  • 22
    • 0032213555 scopus 로고    scopus 로고
    • The granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tu22: sequence analysis and expression in a heterologous host
    • Ichinose K., Bedford D.J., Tornus D., Bechthold A., Bibb M.J., Revill W.P., Floss H.G., and Hopwood D.A. The granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tu22: sequence analysis and expression in a heterologous host. Chem. Biol. 5 (1998) 647-659
    • (1998) Chem. Biol. , vol.5 , pp. 647-659
    • Ichinose, K.1    Bedford, D.J.2    Tornus, D.3    Bechthold, A.4    Bibb, M.J.5    Revill, W.P.6    Floss, H.G.7    Hopwood, D.A.8
  • 23
    • 0033535067 scopus 로고    scopus 로고
    • Proof that the actVI genetic region of Streptomyces coelicolor A3(2) is involved in stereospecific pyran ring formation in the biosynthesis of actinorhodin
    • Ichinose K., Surti C., Taguchi T., Malpartida F., Booker-Milburn K., Stephenson G., Ebizuka Y., and Hopwood D. Proof that the actVI genetic region of Streptomyces coelicolor A3(2) is involved in stereospecific pyran ring formation in the biosynthesis of actinorhodin. Bioorg. Med. Chem. Lett. 9 (1999) 395-400
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 395-400
    • Ichinose, K.1    Surti, C.2    Taguchi, T.3    Malpartida, F.4    Booker-Milburn, K.5    Stephenson, G.6    Ebizuka, Y.7    Hopwood, D.8
  • 24
    • 0035026551 scopus 로고    scopus 로고
    • Functional complementation of pyran ring formation in actinorhodin biosynthesis in Streptomyces coelicolor A3(2) by ketoreductase genes for granaticin biosynthesis
    • Ichinose K., Taquchi T., Bedford D.J., Ebizuka Y., and Hopwood D.A. Functional complementation of pyran ring formation in actinorhodin biosynthesis in Streptomyces coelicolor A3(2) by ketoreductase genes for granaticin biosynthesis. J. Bacteriol. 183 (2001) 3247-3250
    • (2001) J. Bacteriol. , vol.183 , pp. 3247-3250
    • Ichinose, K.1    Taquchi, T.2    Bedford, D.J.3    Ebizuka, Y.4    Hopwood, D.A.5
  • 25
    • 0038148677 scopus 로고    scopus 로고
    • Cloning, sequencing and heterologous expression of the medermycin biosynthetic gene cluster of Streptomyces sp. AM-7161: towards comparative analysis of the benzoisochromanequinone gene clusters
    • Ichinose K., Ozawa M., Itou K., Kunieda K., and Ebizuka Y. Cloning, sequencing and heterologous expression of the medermycin biosynthetic gene cluster of Streptomyces sp. AM-7161: towards comparative analysis of the benzoisochromanequinone gene clusters. Microbiology 149 (2003) 1633-1645
    • (2003) Microbiology , vol.149 , pp. 1633-1645
    • Ichinose, K.1    Ozawa, M.2    Itou, K.3    Kunieda, K.4    Ebizuka, Y.5
  • 26
    • 34447333393 scopus 로고    scopus 로고
    • Actinorhodin biosynthesis: structural requirements for post-PKS tailoring intermediates revealed by functional analysis of ActVI-ORF1 reductase
    • Itoh T., Taguchi T., Kimberley M.R., Booker-Milburn K.I., Stephenson G.R., Ebizuka Y., and Ichinose K. Actinorhodin biosynthesis: structural requirements for post-PKS tailoring intermediates revealed by functional analysis of ActVI-ORF1 reductase. Biochemistry 46 (2007) 8181-8188
    • (2007) Biochemistry , vol.46 , pp. 8181-8188
    • Itoh, T.1    Taguchi, T.2    Kimberley, M.R.3    Booker-Milburn, K.I.4    Stephenson, G.R.5    Ebizuka, Y.6    Ichinose, K.7
  • 27
    • 33644766092 scopus 로고    scopus 로고
    • Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity
    • Kallio P., Sultana A., Niemi J., Mäntsälä P., and Schneider G. Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity. J. Mol. Biol. 357 (2006) 210-220
    • (2006) J. Mol. Biol. , vol.357 , pp. 210-220
    • Kallio, P.1    Sultana, A.2    Niemi, J.3    Mäntsälä, P.4    Schneider, G.5
  • 29
    • 34247112830 scopus 로고    scopus 로고
    • Multi-oxygenase complexes of the gilvocarcin and jadomycin biosyntheses
    • Kharel M.K., Zhu L., Liu T., and Rohr J. Multi-oxygenase complexes of the gilvocarcin and jadomycin biosyntheses. J. Am. Chem. Soc. 129 (2007) 3780-3781
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 3780-3781
    • Kharel, M.K.1    Zhu, L.2    Liu, T.3    Rohr, J.4
  • 31
    • 8744305865 scopus 로고    scopus 로고
    • Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity
    • Korman T.P., Hill J.A., Vu T.N., and Tsai S.C. Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity. Biochemistry 43 (2004) 14529-14538
    • (2004) Biochemistry , vol.43 , pp. 14529-14538
    • Korman, T.P.1    Hill, J.A.2    Vu, T.N.3    Tsai, S.C.4
  • 35
    • 27644473551 scopus 로고    scopus 로고
    • Functional studies on a ketoreductase gene from Streptomyces sp. AM-7161 to control the stereochemistry in medermycin biosynthesis
    • Li A., Itoh T., Taguchi T., Xiang T., Ebizuka Y., and Ichinose K. Functional studies on a ketoreductase gene from Streptomyces sp. AM-7161 to control the stereochemistry in medermycin biosynthesis. Bioorg. Med. Chem. 13 (2005) 6856-6863
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 6856-6863
    • Li, A.1    Itoh, T.2    Taguchi, T.3    Xiang, T.4    Ebizuka, Y.5    Ichinose, K.6
  • 36
    • 0034721884 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence, and heterologous expression of the biosynthetic gene cluster for R1128, a non-steroidal estrogen receptor antagonist. Insights into an unusual priming mechanism
    • Marti T., Hu Z., Pohl N.L., Shah A.N., and Khosla C. Cloning, nucleotide sequence, and heterologous expression of the biosynthetic gene cluster for R1128, a non-steroidal estrogen receptor antagonist. Insights into an unusual priming mechanism. J. Biol. Chem. 275 (2000) 33443-33448
    • (2000) J. Biol. Chem. , vol.275 , pp. 33443-33448
    • Marti, T.1    Hu, Z.2    Pohl, N.L.3    Shah, A.N.4    Khosla, C.5
  • 38
    • 0035846645 scopus 로고    scopus 로고
    • In vitro reconstitution and analysis of the chain initiating enzymes of the R1128 polyketide synthase
    • Meadows E.S., and Khosla C. In vitro reconstitution and analysis of the chain initiating enzymes of the R1128 polyketide synthase. Biochemistry 40 (2001) 14855-14861
    • (2001) Biochemistry , vol.40 , pp. 14855-14861
    • Meadows, E.S.1    Khosla, C.2
  • 39
    • 0036731845 scopus 로고    scopus 로고
    • Molecular evolution of aromatic polyketides and comparative sequence analysis of polyketide ketosynthase and 16S ribosomal DNA genes from various Streptomyces species
    • Metsä-Ketelä M., Halo L., Munukka E., Hakala J., Mäntsälä P., and Ylihonko K. Molecular evolution of aromatic polyketides and comparative sequence analysis of polyketide ketosynthase and 16S ribosomal DNA genes from various Streptomyces species. Appl. Environ. Microbiol. 68 (2002) 4472-4479
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4472-4479
    • Metsä-Ketelä, M.1    Halo, L.2    Munukka, E.3    Hakala, J.4    Mäntsälä, P.5    Ylihonko, K.6
  • 41
    • 0031843807 scopus 로고    scopus 로고
    • K1115 A, a new anthraquinone that inhibits the binding of activator protein-1 (AP-1) to its recognition sites. II. Taxonomy, fermentation, isolation, physico-chemical properties and structure determination
    • Naruse N., Goto M., Watanabe Y., Terasawa T., and Dobashi K. K1115 A, a new anthraquinone that inhibits the binding of activator protein-1 (AP-1) to its recognition sites. II. Taxonomy, fermentation, isolation, physico-chemical properties and structure determination. J. Antibiot. (Tokyo) 51 (1998) 545-552
    • (1998) J. Antibiot. (Tokyo) , vol.51 , pp. 545-552
    • Naruse, N.1    Goto, M.2    Watanabe, Y.3    Terasawa, T.4    Dobashi, K.5
  • 43
    • 0038544618 scopus 로고    scopus 로고
    • The enzymology of combinatorial biosynthesis
    • Reeves C.D. The enzymology of combinatorial biosynthesis. Crit. Rev. Biotechnol. 23 (2003) 95-147
    • (2003) Crit. Rev. Biotechnol. , vol.23 , pp. 95-147
    • Reeves, C.D.1
  • 44
    • 0036168701 scopus 로고    scopus 로고
    • Characterization of indigoidine biosynthetic genes in Erwinia chrysanthemi and role of this blue pigment in pathogenicity
    • Reverchon S., Rouanet C., Expert D., and Nasser W. Characterization of indigoidine biosynthetic genes in Erwinia chrysanthemi and role of this blue pigment in pathogenicity. J. Bacteriol. 184 (2002) 654-665
    • (2002) J. Bacteriol. , vol.184 , pp. 654-665
    • Reverchon, S.1    Rouanet, C.2    Expert, D.3    Nasser, W.4
  • 45
    • 0023631193 scopus 로고
    • A new shuttle cosmid vector, pKC505, for streptomycetes: its use in the cloning of three different spiramycin-resistance genes from a Streptomyces ambofaciens library
    • Richardson M.A., Kuhstoss S., Solenberg P., Schaus N.A., and Rao R.N. A new shuttle cosmid vector, pKC505, for streptomycetes: its use in the cloning of three different spiramycin-resistance genes from a Streptomyces ambofaciens library. Gene 61 (1987) 231-241
    • (1987) Gene , vol.61 , pp. 231-241
    • Richardson, M.A.1    Kuhstoss, S.2    Solenberg, P.3    Schaus, N.A.4    Rao, R.N.5
  • 46
    • 0036774667 scopus 로고    scopus 로고
    • Modification of post-PKS tailoring steps through combinatorial biosynthesis
    • Rix U., Fischer C., Remsing L.L., and Rohr J. Modification of post-PKS tailoring steps through combinatorial biosynthesis. Nat. Prod. Rep. 19 (2002) 542-580
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 542-580
    • Rix, U.1    Fischer, C.2    Remsing, L.L.3    Rohr, J.4
  • 49
    • 0035930003 scopus 로고    scopus 로고
    • A new mode of stereochemical control revealed by analysis of the biosynthesis of dihydrogranaticin in Streptomyces violaceoruber Tu22
    • Taguchi T., Ebizuka Y., Hopwood D.A., and Ichinose K. A new mode of stereochemical control revealed by analysis of the biosynthesis of dihydrogranaticin in Streptomyces violaceoruber Tu22. J. Am. Chem. Soc. 123 (2001) 11376-11380
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11376-11380
    • Taguchi, T.1    Ebizuka, Y.2    Hopwood, D.A.3    Ichinose, K.4
  • 51
    • 33947389659 scopus 로고    scopus 로고
    • Possible involvement of ActVI-ORFA in transcriptional regulation of actVI tailoring-step genes for actinorhodin biosynthesis
    • Taguchi T., Okamoto S., Lezhava A., Li A., Ochi K., Ebizuka Y., and Ichinose K. Possible involvement of ActVI-ORFA in transcriptional regulation of actVI tailoring-step genes for actinorhodin biosynthesis. FEMS Microbiol. Lett. 269 (2007) 234-239
    • (2007) FEMS Microbiol. Lett. , vol.269 , pp. 234-239
    • Taguchi, T.1    Okamoto, S.2    Lezhava, A.3    Li, A.4    Ochi, K.5    Ebizuka, Y.6    Ichinose, K.7
  • 52
    • 34247881849 scopus 로고    scopus 로고
    • Cloning and characterization of a Streptomyces single module type non-ribosomal peptide synthetase catalyzing a blue pigment synthesis
    • Takahashi H., Kumagai T., Kitani K., Mori M., Matoba Y., and Sugiyama M. Cloning and characterization of a Streptomyces single module type non-ribosomal peptide synthetase catalyzing a blue pigment synthesis. J. Biol. Chem. 282 (2007) 9073-9081
    • (2007) J. Biol. Chem. , vol.282 , pp. 9073-9081
    • Takahashi, H.1    Kumagai, T.2    Kitani, K.3    Mori, M.4    Matoba, Y.5    Sugiyama, M.6
  • 53
    • 3242738305 scopus 로고    scopus 로고
    • The acyltransferase homologue from the initiation module of the R1128 polyketide synthase is an acyl-ACP thioesterase that edits acetyl primer units
    • Tang Y., Koppisch A.T., and Khosla C. The acyltransferase homologue from the initiation module of the R1128 polyketide synthase is an acyl-ACP thioesterase that edits acetyl primer units. Biochemistry 43 (2004) 9546-9555
    • (2004) Biochemistry , vol.43 , pp. 9546-9555
    • Tang, Y.1    Koppisch, A.T.2    Khosla, C.3
  • 55
    • 33644857427 scopus 로고    scopus 로고
    • An aromatic hydroxylation reaction catalyzed by a two-component FMN-dependent Monooxygenase. The ActVA-ActVB system from Streptomyces coelicolor
    • Valton J., Fontecave M., Douki T., Kendrew S.G., and Niviere V. An aromatic hydroxylation reaction catalyzed by a two-component FMN-dependent Monooxygenase. The ActVA-ActVB system from Streptomyces coelicolor. J. Biol. Chem. 281 (2006) 27-35
    • (2006) J. Biol. Chem. , vol.281 , pp. 27-35
    • Valton, J.1    Fontecave, M.2    Douki, T.3    Kendrew, S.G.4    Niviere, V.5
  • 56
    • 0030929313 scopus 로고    scopus 로고
    • A novel family of proteins that regulates antibiotic production in streptomycetes appears to contain an OmpR-like DNA-binding fold
    • Wietzorrek A., and Bibb M. A novel family of proteins that regulates antibiotic production in streptomycetes appears to contain an OmpR-like DNA-binding fold. Mol. Microbiol. 25 (1997) 1181-1184
    • (1997) Mol. Microbiol. , vol.25 , pp. 1181-1184
    • Wietzorrek, A.1    Bibb, M.2
  • 57
    • 19544376849 scopus 로고    scopus 로고
    • Biosynthesis of the antitumor agent chartreusin involves the oxidative rearrangement of an anthracyclic polyketide
    • Xu Z., Jakobi K., Welzel K., and Hertweck C. Biosynthesis of the antitumor agent chartreusin involves the oxidative rearrangement of an anthracyclic polyketide. Chem. Biol. 12 (2005) 579-588
    • (2005) Chem. Biol. , vol.12 , pp. 579-588
    • Xu, Z.1    Jakobi, K.2    Welzel, K.3    Hertweck, C.4
  • 58
    • 0028233242 scopus 로고
    • Isolation and characterization of aclacinomycin A-non-producing Streptomyces galilaeus (ATCC 31615) mutants
    • Ylihonko K., Hakala J., Niemi J., Lundell J., and Mäntsälä P. Isolation and characterization of aclacinomycin A-non-producing Streptomyces galilaeus (ATCC 31615) mutants. Microbiology 140 (1994) 1359-1365
    • (1994) Microbiology , vol.140 , pp. 1359-1365
    • Ylihonko, K.1    Hakala, J.2    Niemi, J.3    Lundell, J.4    Mäntsälä, P.5
  • 59
    • 0029937535 scopus 로고    scopus 로고
    • A gene cluster involved in nogalamycin biosynthesis from Streptomyces nogalater: sequence analysis and complementation of early-block mutations in the anthracycline pathway
    • Ylihonko K., Tuikkanen J., Jussila S., Cong L., and Mäntsälä P. A gene cluster involved in nogalamycin biosynthesis from Streptomyces nogalater: sequence analysis and complementation of early-block mutations in the anthracycline pathway. Mol. Gen. Genet. 251 (1996) 113-120
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 113-120
    • Ylihonko, K.1    Tuikkanen, J.2    Jussila, S.3    Cong, L.4    Mäntsälä, P.5


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