메뉴 건너뛰기




Volumn 9, Issue 9, 2002, Pages 1017-1026

A gene cluster from a marine Streptomyces encoding the biosynthesis of the aromatic spiroketal polyketide griseorhodin A

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRACENES; CLONING, MOLECULAR; ENZYME INHIBITORS; GENE EXPRESSION REGULATION, BACTERIAL; GENES, BACTERIAL; MULTIENZYME COMPLEXES; MULTIGENE FAMILY; NAPHTHOQUINONES; OPEN READING FRAMES; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; STREPTOMYCES; TELOMERASE;

EID: 0036753178     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(02)00223-5     Document Type: Article
Times cited : (154)

References (59)
  • 1
    • 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
  • 2
    • 0033180108 scopus 로고    scopus 로고
    • Biosynthesis of polyketides (other than actinomycete macrolides)
    • Rawlings B.J. Biosynthesis of polyketides (other than actinomycete macrolides). Nat. Prod. Rep. 16:1999;425-484.
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 425-484
    • Rawlings, B.J.1
  • 3
    • 0034521526 scopus 로고    scopus 로고
    • Cloning, sequencing and analysis of the enterocin biosynthesis gene cluster from the marine isolate "Streptomyces maritimus": Evidence for the derailment of an aromatic polyketide synthase
    • Piel J., Hertweck C., Shipley P.R., Hunt D.M., Newman M.S., Moore B.S. Cloning, sequencing and analysis of the enterocin biosynthesis gene cluster from the marine isolate "Streptomyces maritimus" evidence for the derailment of an aromatic polyketide synthase Chem. Biol. 7:2000;943-955.
    • (2000) Chem. Biol. , vol.7 , pp. 943-955
    • Piel, J.1    Hertweck, C.2    Shipley, P.R.3    Hunt, D.M.4    Newman, M.S.5    Moore, B.S.6
  • 4
    • 4244059507 scopus 로고    scopus 로고
    • Harnessing the biosynthetic potential of modular polyketide synthases
    • Khosla C. Harnessing the biosynthetic potential of modular polyketide synthases. Chem. Rev. 97:1997;2577-2590.
    • (1997) Chem. Rev. , vol.97 , pp. 2577-2590
    • Khosla, C.1
  • 5
    • 0035501490 scopus 로고    scopus 로고
    • Altering the glycosylation pattern of bioactive compounds
    • Mendez C., Salas J.A. Altering the glycosylation pattern of bioactive compounds. Trends Biotechnol. 19:2001;449-456.
    • (2001) Trends Biotechnol. , vol.19 , pp. 449-456
    • Mendez, C.1    Salas, J.A.2
  • 6
    • 0011111092 scopus 로고
    • Antibiotics from Actinomycetes - chemical composition of antibiotic griseorhodin A
    • Tresselt D., Eckardt K., Ihn W. Antibiotics from Actinomycetes - chemical composition of antibiotic griseorhodin A. Tetrahedron. 34:1978;2693-2699.
    • (1978) Tetrahedron , vol.34 , pp. 2693-2699
    • Tresselt, D.1    Eckardt, K.2    Ihn, W.3
  • 7
    • 0034005507 scopus 로고    scopus 로고
    • Structural and biosynthetic investigations of the rubromycins
    • Puder, C., Loya, S., Hizi, A., and Zeeck, A. (2000). Structural and biosynthetic investigations of the rubromycins. Eur. J. Org. Chem., 729-735.
    • (2000) Eur. J. Org. Chem. , pp. 729-735
    • Puder, C.1    Loya, S.2    Hizi, A.3    Zeeck, A.4
  • 9
    • 0025303195 scopus 로고
    • Inhibition of human immunodeficiency virus 1 reverse- transcriptase activity by rubromycins - competitive interaction at the template - primer site
    • Goldman M.E., Salituro G.S., Bowen J.A., Williamson J.M., Zink D.L., Schleif W.A., Emini E.A. Inhibition of human immunodeficiency virus 1 reverse- transcriptase activity by rubromycins - competitive interaction at the template - primer site. Mol. Pharmacol. 38:1990;20-25.
    • (1990) Mol. Pharmacol. , vol.38 , pp. 20-25
    • Goldman, M.E.1    Salituro, G.S.2    Bowen, J.A.3    Williamson, J.M.4    Zink, D.L.5    Schleif, W.A.6    Emini, E.A.7
  • 10
    • 0033859753 scopus 로고    scopus 로고
    • Determination of the absolute configurations of γ-rubromycin and related spiro compounds by quantum chemical CD calculations
    • Bringmann, G., Kraus, J., Schmitt, U., Puder, C., and Zeeck, A. (2000). Determination of the absolute configurations of γ-rubromycin and related spiro compounds by quantum chemical CD calculations. Eur. J. Org. Chem., 2729-2734.
    • (2000) Eur. J. Org. Chem. , pp. 2729-2734
    • Bringmann, G.1    Kraus, J.2    Schmitt, U.3    Puder, C.4    Zeeck, A.5
  • 11
    • 0031218916 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence of the putative polyketide synthase genes for pradimicin biosynthesis from Actinomadura hibisca
    • Dairi T., Hamano Y., Igarashi Y., Furumai T., Oki T. Cloning and nucleotide sequence of the putative polyketide synthase genes for pradimicin biosynthesis from Actinomadura hibisca. Biosci. Biotechnol. Biochem. 61:1997;1445-1453.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1445-1453
    • Dairi, T.1    Hamano, Y.2    Igarashi, Y.3    Furumai, T.4    Oki, T.5
  • 12
    • 0032975332 scopus 로고    scopus 로고
    • Development of a self-cloning system for Actinomadura verrucosospora and identification of polyketide synthase genes essential for production of the angucyclic antibiotic pradimicin
    • Dairi T., Hamano Y., Furumai T., Oki T. Development of a self-cloning system for Actinomadura verrucosospora and identification of polyketide synthase genes essential for production of the angucyclic antibiotic pradimicin. Appl. Environ. Microbiol. 65:1999;2703-2709.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2703-2709
    • Dairi, T.1    Hamano, Y.2    Furumai, T.3    Oki, T.4
  • 13
    • 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
    • Fernández-Moreno M.A., Martinez E., Boto L., Hopwood D.A., 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
    • Fernández-Moreno, M.A.1    Martinez, E.2    Boto, L.3    Hopwood, D.A.4    Malpartida, F.5
  • 14
    • 0034711399 scopus 로고    scopus 로고
    • Dissecting the chain length specificity in bacterial aromatic polyketide synthases using chimeric genes
    • Burson K.K., Khosla C. Dissecting the chain length specificity in bacterial aromatic polyketide synthases using chimeric genes. Tetrahedron. 56:2000;9401-9408.
    • (2000) Tetrahedron , vol.56 , pp. 9401-9408
    • Burson, K.K.1    Khosla, C.2
  • 15
    • 0028555349 scopus 로고
    • Characterization of the Streptomyces peucetius ATCC 29050 genes encoding doxorubicin polyketide synthase
    • Grimm A., Madduri K., Ali A., Hutchinson C.R. Characterization of the Streptomyces peucetius ATCC 29050 genes encoding doxorubicin polyketide synthase. Gene. 151:1994;1-10.
    • (1994) Gene , vol.151 , pp. 1-10
    • Grimm, A.1    Madduri, K.2    Ali, A.3    Hutchinson, C.R.4
  • 16
    • 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.H., Pohl N.L., Shah A.N., 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.H.2    Pohl, N.L.3    Shah, A.N.4    Khosla, C.5
  • 18
    • 0024315260 scopus 로고
    • The mechanism of biotin-dependent enzymes
    • Knowles J.R. The mechanism of biotin-dependent enzymes. Annu. Rev. Biochem. 58:1989;195-221.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 195-221
    • Knowles, J.R.1
  • 19
    • 0034081009 scopus 로고    scopus 로고
    • An acyl-coenzyme A carboxylase encoding gene associated with jadomycin biosynthesis in Streptomyces venezuelae ISP5230
    • Han L., Yang K., Kulowski K., Wendt-Pienkowski E., Hutchinson C.R., Vining L.C. An acyl-coenzyme A carboxylase encoding gene associated with jadomycin biosynthesis in Streptomyces venezuelae ISP5230. Microbiology. 146:2000;903-910.
    • (2000) Microbiology , vol.146 , pp. 903-910
    • Han, L.1    Yang, K.2    Kulowski, K.3    Wendt-Pienkowski, E.4    Hutchinson, C.R.5    Vining, L.C.6
  • 20
    • 0027381037 scopus 로고
    • The tcmVI region of the tetracenomycin C biosynthetic gene cluster of Streptomyces-glaucescens encodes the tetracenomycin F1 monooxygenase, tetracenomycin F2 cyclase, and, most likely, a 2nd cyclase
    • Summers R.G., Wendtpienkowski E., Motamedi H., Hutchinson C.R. The tcmVI region of the tetracenomycin C biosynthetic gene cluster of Streptomyces-glaucescens encodes the tetracenomycin F1 monooxygenase, tetracenomycin F2 cyclase, and, most likely, a 2nd cyclase. J. Bacteriol. 175:1993;7571-7580.
    • (1993) J. Bacteriol. , vol.175 , pp. 7571-7580
    • Summers, R.G.1    Wendtpienkowski, E.2    Motamedi, H.3    Hutchinson, C.R.4
  • 22
    • 0029900903 scopus 로고    scopus 로고
    • Deciphering the mechanism for the assembly of aromatic polyketides by a bacterial polyketide synthase
    • Shen B., Hutchinson C.R. Deciphering the mechanism for the assembly of aromatic polyketides by a bacterial polyketide synthase. Proc. Natl. Acad. Sci. USA. 93:1996;6600-6604.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6600-6604
    • Shen, B.1    Hutchinson, C.R.2
  • 23
  • 24
    • 0032474472 scopus 로고    scopus 로고
    • Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis
    • Bao W.L., Wendt-Pienkowski E., Hutchinson C.R. Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis. Biochemistry. 37:1998;8132-8138.
    • (1998) Biochemistry , vol.37 , pp. 8132-8138
    • Bao, W.L.1    Wendt-Pienkowski, E.2    Hutchinson, C.R.3
  • 25
    • 0031941120 scopus 로고    scopus 로고
    • Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs
    • Mewies M., McIntire W.S., Scrutton N.S. Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes. The current state of affairs Protein Sci. 7:1998;7-20.
    • (1998) Protein Sci. , vol.7 , pp. 7-20
    • Mewies, M.1    McIntire, W.S.2    Scrutton, N.S.3
  • 26
    • 0037149649 scopus 로고    scopus 로고
    • Mutational analysis of the enterocin Favorskii biosynthetic rearrangement
    • Xiang L.K., Kalaitzis J.A., Nilsen G., Chen L., Moore B.S. Mutational analysis of the enterocin Favorskii biosynthetic rearrangement. Org. Lett. 4:2002;957-960.
    • (2002) Org. Lett. , vol.4 , pp. 957-960
    • Xiang, L.K.1    Kalaitzis, J.A.2    Nilsen, G.3    Chen, L.4    Moore, B.S.5
  • 27
    • 0033117369 scopus 로고    scopus 로고
    • Molecular characterization and analysis of the biosynthetic gene cluster for the antitumor antibiotic mitomycin C from Streptomyces lavendulae NRRL 2564
    • Mao Y.Q., Varoglu M., Sherman D.H. Molecular characterization and analysis of the biosynthetic gene cluster for the antitumor antibiotic mitomycin C from Streptomyces lavendulae NRRL 2564. Chem. Biol. 6:1999;251-263.
    • (1999) Chem. Biol. , vol.6 , pp. 251-263
    • Mao, Y.Q.1    Varoglu, M.2    Sherman, D.H.3
  • 28
    • 13144258781 scopus 로고    scopus 로고
    • Biosynthesis of the ansamycin antibiotic rifamycin: Deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699
    • August P.R., Tang L., Yoon Y.J., Ning S., Muller R., Yu T.W., Taylor M., Hoffmann D., Kim C.G., Zhang X.H.et al. Biosynthesis of the ansamycin antibiotic rifamycin. Deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699 Chem. Biol. 5:1998;69-79.
    • (1998) Chem. Biol. , vol.5 , pp. 69-79
    • August, P.R.1    Tang, L.2    Yoon, Y.J.3    Ning, S.4    Muller, R.5    Yu, T.W.6    Taylor, M.7    Hoffmann, D.8    Kim, C.G.9    Zhang, X.H.10
  • 29
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos T.L., Finzel B.C., Howard A.J. High-resolution crystal structure of cytochrome P450cam. J. Mol. Biol. 195:1987;687-700.
    • (1987) J. Mol. Biol. , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 30
    • 0003002061 scopus 로고    scopus 로고
    • Electron transfer proteins of cytochrome P450 systems
    • Hanukoglu I. Electron transfer proteins of cytochrome P450 systems. Adv. Mol. Cell. Biol. 14:1996;29-55.
    • (1996) Adv. Mol. Cell. Biol. , vol.14 , pp. 29-55
    • Hanukoglu, I.1
  • 31
    • 0029820893 scopus 로고    scopus 로고
    • Purification and sequence analysis of 4-methyl-5-nitrocatechol oxygenase from Burkholderia sp. strain DNT
    • Haigler B.E., Suen W.C., Spain J.C. Purification and sequence analysis of 4-methyl-5-nitrocatechol oxygenase from Burkholderia sp. strain DNT. J. Bacteriol. 178:1996;6019-6024.
    • (1996) J. Bacteriol. , vol.178 , pp. 6019-6024
    • Haigler, B.E.1    Suen, W.C.2    Spain, J.C.3
  • 32
    • 0034517750 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of tetracenomycin A2 oxygenase: A flavoprotein hydroxylase involved in polyketide biosynthesis
    • Beynon J., Rafanan E.R., Shen B., Fisher A.J. Crystallization and preliminary X-ray analysis of tetracenomycin A2 oxygenase. a flavoprotein hydroxylase involved in polyketide biosynthesis Acta Crystallogr. D Biol. Crystallogr. 56:2000;1647-1651.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1647-1651
    • Beynon, J.1    Rafanan, E.R.2    Shen, B.3    Fisher, A.J.4
  • 34
    • 0029921869 scopus 로고    scopus 로고
    • Structural and sequence comparisons of quinone oxidoreductase, ζ-crystallin, and glucose and alcohol dehydrogenases
    • Edwards K.J., Barton J.D., Rossjohn J., Thorn J.M., Taylor G.L., Ollis D.L. Structural and sequence comparisons of quinone oxidoreductase, ζ-crystallin, and glucose and alcohol dehydrogenases. Arch. Biochem. Biophys. 328:1996;173-183.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 173-183
    • Edwards, K.J.1    Barton, J.D.2    Rossjohn, J.3    Thorn, J.M.4    Taylor, G.L.5    Ollis, D.L.6
  • 35
    • 0026556950 scopus 로고
    • Identification and characterization of the enzymatic activity of ζ-crystallin from guinea pig lens - a novel NADPHquinone oxidoreductase
    • Rao P.V., Krishna C.M., Zigler J.S. Identification and characterization of the enzymatic activity of ζ-crystallin from guinea pig lens - a novel NADPHquinone oxidoreductase. J. Biol. Chem. 267:1992;96-102.
    • (1992) J. Biol. Chem. , vol.267 , pp. 96-102
    • Rao, P.V.1    Krishna, C.M.2    Zigler, J.S.3
  • 36
    • 0027771429 scopus 로고
    • Xenobiotic induction of quinone oxidoreductase activity in lens epithelial cells
    • Tumminia S.J., Rao P.V., Zigler J.S., Russell P. Xenobiotic induction of quinone oxidoreductase activity in lens epithelial cells. Biochim. Biophys. Acta. 1203:1993;251-259.
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 251-259
    • Tumminia, S.J.1    Rao, P.V.2    Zigler, J.S.3    Russell, P.4
  • 38
    • 0033036925 scopus 로고    scopus 로고
    • Analysis of two chromosomal regions adjacent to genes for a type II polyketide synthase involved in the biosynthesis of the antitumor polyketide mithramycin in Streptomyces argillaceus
    • Prado L., Lombo F., Brana A.F., Mendez C., Rohr J., Salas J.A. Analysis of two chromosomal regions adjacent to genes for a type II polyketide synthase involved in the biosynthesis of the antitumor polyketide mithramycin in Streptomyces argillaceus. Mol. Gen. Genet. 261:1999;216-225.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 216-225
    • Prado, L.1    Lombo, F.2    Brana, A.F.3    Mendez, C.4    Rohr, J.5    Salas, J.A.6
  • 39
    • 0026588622 scopus 로고
    • Nucleotide sequence of the tcmII-tcmIV region of the tetracenomycin C biosynthetic gene cluster of Streptomyces glaucescens and evidence that the tcmN gene encodes a multifunctional cyclase dehydratase-ortho-methyl transferase
    • Summers R.G., Wendtpienkowski E., Motamedi H., Hutchinson C.R. Nucleotide sequence of the tcmII-tcmIV region of the tetracenomycin C biosynthetic gene cluster of Streptomyces glaucescens and evidence that the tcmN gene encodes a multifunctional cyclase dehydratase-ortho-methyl transferase. J. Bacteriol. 174:1992;1810-1820.
    • (1992) J. Bacteriol. , vol.174 , pp. 1810-1820
    • Summers, R.G.1    Wendtpienkowski, E.2    Motamedi, H.3    Hutchinson, C.R.4
  • 40
    • 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., 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
  • 41
    • 0036166719 scopus 로고    scopus 로고
    • Differential roles of two SARP-encoding regulatory genes during tylosin biosynthesis
    • Bate N., Stratigopoulos G., Cundliffe E. Differential roles of two SARP-encoding regulatory genes during tylosin biosynthesis. Mol. Microbiol. 43:2002;449-458.
    • (2002) Mol. Microbiol. , vol.43 , pp. 449-458
    • Bate, N.1    Stratigopoulos, G.2    Cundliffe, E.3
  • 42
    • 0029025536 scopus 로고
    • Characterization of MarR, the repressor of the multiple antibiotic resistance (Mar) operon in Escherichia coli
    • Seoane A.S., Levy S.B. Characterization of MarR, the repressor of the multiple antibiotic resistance (Mar) operon in Escherichia coli. J. Bacteriol. 177:1995;3414-3419.
    • (1995) J. Bacteriol. , vol.177 , pp. 3414-3419
    • Seoane, A.S.1    Levy, S.B.2
  • 43
    • 0028882479 scopus 로고
    • Cloning and characterization of a polyketide synthase gene from Streptomyces fradiae Tü2717, which carries the genes for biosynthesis of the angucycline antibiotic urdamycin A and a gene probably involved in its oxygenation
    • Decker H., Haag S. Cloning and characterization of a polyketide synthase gene from Streptomyces fradiae Tü2717, which carries the genes for biosynthesis of the angucycline antibiotic urdamycin A and a gene probably involved in its oxygenation. J. Bacteriol. 177:1995;6126-6136.
    • (1995) J. Bacteriol. , vol.177 , pp. 6126-6136
    • Decker, H.1    Haag, S.2
  • 45
    • 0034603795 scopus 로고    scopus 로고
    • Identification of two polyketide synthase gene clusters on the linear plasmid pSLA2-L in Streptomyces rochei
    • Suwa M., Sugino H., Sasaoka A., Mori E., Fujii S., Shinkawa H., Nimi O., Kinashi H. Identification of two polyketide synthase gene clusters on the linear plasmid pSLA2-L in Streptomyces rochei. Gene. 246:2000;123-131.
    • (2000) Gene , vol.246 , pp. 123-131
    • Suwa, M.1    Sugino, H.2    Sasaoka, A.3    Mori, E.4    Fujii, S.5    Shinkawa, H.6    Nimi, O.7    Kinashi, H.8
  • 47
    • 0033079834 scopus 로고    scopus 로고
    • Mechanism and specificity of the terminal thioesterase domain from the erythromycin polyketide synthase
    • Gokhale R.S., Hunziker D., Cane D.E., Khosla C. Mechanism and specificity of the terminal thioesterase domain from the erythromycin polyketide synthase. Chem. Biol. 6:1999;117-125.
    • (1999) Chem. Biol. , vol.6 , pp. 117-125
    • Gokhale, R.S.1    Hunziker, D.2    Cane, D.E.3    Khosla, C.4
  • 48
    • 0035068571 scopus 로고    scopus 로고
    • Role of type II thioesterases: Evidence for removal of short acyl chains produced by aberrant decarboxylation of chain extender units
    • Heathcole M.L., Staunton J., Leadlay P.F. Role of type II thioesterases. evidence for removal of short acyl chains produced by aberrant decarboxylation of chain extender units Chem. Biol. 8:2001;207-220.
    • (2001) Chem. Biol. , vol.8 , pp. 207-220
    • Heathcole, M.L.1    Staunton, J.2    Leadlay, P.F.3
  • 49
    • 0035685204 scopus 로고    scopus 로고
    • Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1
    • Mavrodi D.V., Bonsall R.F., Delaney S.M., Soule M.J., Phillips G., Thomashow L.S. Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1. J. Bacteriol. 183:2001;6454-6465.
    • (2001) J. Bacteriol. , vol.183 , pp. 6454-6465
    • Mavrodi, D.V.1    Bonsall, R.F.2    Delaney, S.M.3    Soule, M.J.4    Phillips, G.5    Thomashow, L.S.6
  • 50
    • 0024369423 scopus 로고
    • The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity
    • Vanheeke G., Schuster S.M. The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. J. Biol. Chem. 264:1989;19475-19477.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19475-19477
    • Vanheeke, G.1    Schuster, S.M.2
  • 51
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • Bierman M., Logan R., Obrien K., Seno E.T., Rao R.N., Schoner B.E. Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp. Gene. 116:1992;43-49.
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    Obrien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 52
    • 0028131912 scopus 로고
    • Repeated polyketide synthase modules involved in the biosynthesis of a heptaene macrolide by Streptomyces sp. Fr-008
    • Hu Z.H., Bao K., Zhou X.F., Zhou Q., Hopwood D.A., Kieser T., Deng Z.X. Repeated polyketide synthase modules involved in the biosynthesis of a heptaene macrolide by Streptomyces sp. Fr-008. Mol. Microbiol. 14:1994;163-172.
    • (1994) Mol. Microbiol. , vol.14 , pp. 163-172
    • Hu, Z.H.1    Bao, K.2    Zhou, X.F.3    Zhou, Q.4    Hopwood, D.A.5    Kieser, T.6    Deng, Z.X.7
  • 53
    • 0035032072 scopus 로고    scopus 로고
    • Collinone, a new recombinant angular polyketide antibiotic made by an engineered Streptomyces strain
    • Martin R., Sterner O., Alvarez M.A., de Clercq E., Bailey J.E., Minas W. Collinone, a new recombinant angular polyketide antibiotic made by an engineered Streptomyces strain. J. Antibiot. 54:2001;239-249.
    • (2001) J. Antibiot. , vol.54 , pp. 239-249
    • Martin, R.1    Sterner, O.2    Alvarez, M.A.3    De Clercq, E.4    Bailey, J.E.5    Minas, W.6
  • 54
    • 0029934431 scopus 로고    scopus 로고
    • Characterization of Streptomyces argillaceus genes encoding a polyketide synthase involved in the biosynthesis of the antitumor mithramycin
    • Lombo F., Blanco G., Fernandez E., Mendez C., Salas J.A. Characterization of Streptomyces argillaceus genes encoding a polyketide synthase involved in the biosynthesis of the antitumor mithramycin. Gene. 172:1996;87-91.
    • (1996) Gene , vol.172 , pp. 87-91
    • Lombo, F.1    Blanco, G.2    Fernandez, E.3    Mendez, C.4    Salas, J.A.5
  • 55
    • 0027248795 scopus 로고
    • 2-Step epoxidation of hyoscyamine to scopolamine Is catalyzed by bifunctional hyoscyamine 6-β-hydroxylase
    • Hashimoto T., Matsuda J., Yamada Y. 2-Step epoxidation of hyoscyamine to scopolamine Is catalyzed by bifunctional hyoscyamine 6-β-hydroxylase. FEBS Lett. 329:1993;35-39.
    • (1993) FEBS Lett. , vol.329 , pp. 35-39
    • Hashimoto, T.1    Matsuda, J.2    Yamada, Y.3
  • 59
    • 0032213555 scopus 로고    scopus 로고
    • The granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tü22: 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., Hopwood D.A. The granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tü22. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.